ALDR_HUMAN
ID ALDR_HUMAN Reviewed; 316 AA.
AC P15121; B2R8N3; Q5U031; Q6FGA4; Q6ICP2; Q9BS21; Q9UCI9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Aldo-keto reductase family 1 member B1;
DE EC=1.1.1.300 {ECO:0000269|PubMed:12732097};
DE EC=1.1.1.372 {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:8245005};
DE EC=1.1.1.54 {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:21329684};
DE AltName: Full=Aldehyde reductase;
DE AltName: Full=Aldose reductase;
DE Short=AR;
DE EC=1.1.1.21 {ECO:0000269|PubMed:8245005};
GN Name=AKR1B1; Synonyms=ALDR1, ALR2 {ECO:0000303|PubMed:17368668};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2498333; DOI=10.1016/s0021-9258(18)60566-6;
RA Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.;
RT "The aldo-keto reductase superfamily. cDNAs and deduced amino acid
RT sequences of human aldehyde and aldose reductases.";
RL J. Biol. Chem. 264:9547-9551(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=2504709; DOI=10.1016/s0021-9258(18)63766-4;
RA Chung S., Lamendola J.;
RT "Cloning and sequence determination of human placental aldose reductase
RT gene.";
RL J. Biol. Chem. 264:14775-14777(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetus;
RX PubMed=2510130; DOI=10.1093/nar/17.20.8368;
RA Graham A., Hedge P.J., Powell S.J., Riley J., Brown L., Gammack A.,
RA Carey F., Markham A.F.;
RT "Nucleotide sequence of cDNA for human aldose reductase.";
RL Nucleic Acids Res. 17:8368-8368(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Placenta;
RX PubMed=2111143; DOI=10.1089/dna.1990.9.149;
RA Grundmann U., Bohn H., Obermeier R., Amann E.;
RT "Cloning and prokaryotic expression of a biologically active human
RT placental aldose reductase.";
RL DNA Cell Biol. 9:149-157(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2112546; DOI=10.1016/s0021-9258(19)38740-x;
RA Nishimura C., Matsuura Y., Kokai Y., Akera T., Carper D., Morjana N.,
RA Lyons C., Flynn T.G.;
RT "Cloning and expression of human aldose reductase.";
RL J. Biol. Chem. 265:9788-9792(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1901857; DOI=10.1016/s0021-9258(20)89582-9;
RA Graham A., Brown L., Hedge P.J., Gammack A.J., Markham A.F.;
RT "Structure of the human aldose reductase gene.";
RL J. Biol. Chem. 266:6872-6877(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9195951; DOI=10.1074/jbc.272.26.16431;
RA Ko B.C.B., Ruepp B., Bohren K.M., Gabbay K.H., Chung S.S.;
RT "Identification and characterization of multiple osmotic response sequences
RT in the human aldose reductase gene.";
RL J. Biol. Chem. 272:16431-16437(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
RT "SEREX identification of new tumour-associated antigens in cutaneous T-cell
RT lymphoma.";
RL Br. J. Dermatol. 150:252-258(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP PROTEIN SEQUENCE OF 131-162, AND TISSUE SPECIFICITY.
RX PubMed=8435445; DOI=10.1016/0167-4889(93)90218-e;
RA Ferraretto A., Negri A., Giuliani A., De Grada L., Fuhrman Conti A.M.,
RA Ronchi S.;
RT "Aldose reductase is involved in long-term adaptation of EUE cells to
RT hyperosmotic stress.";
RL Biochim. Biophys. Acta 1175:283-288(1993).
RN [16]
RP PROTEIN SEQUENCE OF 244-275.
RX PubMed=2492527; DOI=10.1016/s0021-9258(19)81699-x;
RA Morjana N.A., Lyons C., Flynn T.G.;
RT "Aldose reductase from human psoas muscle. Affinity labeling of an active
RT site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-
RT adenosine.";
RL J. Biol. Chem. 264:2912-2919(1989).
RN [17]
RP PROTEIN SEQUENCE OF 276-294, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [18]
RP PROTEIN SEQUENCE OF 298-316, AND ACTIVITY REGULATION.
RX PubMed=8343525; DOI=10.1016/0167-4838(93)90258-s;
RA Liu S.Q., Bhatnagar A., Ansari N.H., Srivastava S.K.;
RT "Identification of the reactive cysteine residue in human placenta aldose
RT reductase.";
RL Biochim. Biophys. Acta 1164:268-272(1993).
RN [19]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
RC TISSUE=Muscle;
RX PubMed=8281941; DOI=10.1111/j.1432-1033.1993.tb18445.x;
RA Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O.,
RA Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F.,
RA van Dorsselaer A.;
RT "Sequence of pig lens aldose reductase and electrospray mass spectrometry
RT of non-covalent and covalent complexes.";
RL Eur. J. Biochem. 218:893-903(1993).
RN [20]
RP CATALYTIC ACTIVITY.
RX PubMed=1936586; DOI=10.2337/diab.40.10.1233;
RA Hamada Y., Kitoh R., Raskin P.;
RT "Crucial role of aldose reductase activity and plasma glucose level in
RT sorbitol accumulation in erythrocytes from diabetic patients.";
RL Diabetes 40:1233-1240(1991).
RN [21]
RP MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111, AND CATALYTIC ACTIVITY.
RX PubMed=8245005; DOI=10.1016/s0021-9258(19)74444-5;
RA Tarle I., Borhani D.W., Wilson D.K., Quiocho F.A., Petrash J.M.;
RT "Probing the active site of human aldose reductase. Site-directed
RT mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.";
RL J. Biol. Chem. 268:25687-25693(1993).
RN [22]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=10510318; DOI=10.1042/bj3430487;
RA O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D.;
RT "Major differences exist in the function and tissue-specific expression of
RT human aflatoxin B1 aldehyde reductase and the principal human aldo-keto
RT reductase AKR1 family members.";
RL Biochem. J. 343:487-504(1999).
RN [23]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=12732097; DOI=10.1042/bj20021818;
RA Crosas B., Hyndman D.J., Gallego O., Martras S., Pares X., Flynn T.G.,
RA Farres J.;
RT "Human aldose reductase and human small intestine aldose reductase are
RT efficient retinal reductases: consequences for retinoid metabolism.";
RL Biochem. J. 373:973-979(2003).
RN [24]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=17381426; DOI=10.1042/bj20061743;
RA Spite M., Baba S.P., Ahmed Y., Barski O.A., Nijhawan K., Petrash J.M.,
RA Bhatnagar A., Srivastava S.;
RT "Substrate specificity and catalytic efficiency of aldo-keto reductases
RT with phospholipid aldehydes.";
RL Biochem. J. 405:95-105(2007).
RN [25]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=19010934; DOI=10.1093/jb/mvn152;
RA Kabututu Z., Manin M., Pointud J.C., Maruyama T., Nagata N., Lambert S.,
RA Lefrancois-Martinez A.M., Martinez A., Urade Y.;
RT "Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3
RT and 1B7.";
RL J. Biochem. 145:161-168(2009).
RN [26]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=21329684; DOI=10.1016/j.cbi.2011.02.004;
RA Shen Y., Zhong L., Johnson S., Cao D.;
RT "Human aldo-keto reductases 1B1 and 1B10: a comparative study on their
RT enzyme activity toward electrophilic carbonyl compounds.";
RL Chem. Biol. Interact. 191:192-198(2011).
RN [27]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=21329680; DOI=10.1016/j.cbi.2011.02.007;
RA Ruiz F.X., Moro A., Gallego O., Ardevol A., Rovira C., Petrash J.M.,
RA Pares X., Farres J.;
RT "Human and rodent aldo-keto reductases from the AKR1B subfamily and their
RT specificity with retinaldehyde.";
RL Chem. Biol. Interact. 191:199-205(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-222 AND LYS-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=1621098; DOI=10.1126/science.1621098;
RA Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A.;
RT "An unlikely sugar substrate site in the 1.65 A structure of the human
RT aldose reductase holoenzyme implicated in diabetic complications.";
RL Science 257:81-84(1992).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
RX PubMed=1447221; DOI=10.2210/pdb1abn/pdb;
RA Borhani D.W., Harter T.M., Pertrash J.M.;
RT "The crystal structure of the aldose reductase.NADPH binary complex.";
RL J. Biol. Chem. 267:24841-24847(1992).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8234324; DOI=10.1073/pnas.90.21.9847;
RA Wilson D.K., Tarle I., Petrash J.M., Quiocho F.A.;
RT "Refined 1.8-A structure of human aldose reductase complexed with the
RT potent inhibitor zopolrestat.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9847-9851(1993).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9405046; DOI=10.1021/bi9717136;
RA Harrison D.H., Bohren K.M., Petsko G.A., Ringe D., Gabbay K.H.;
RT "The alrestatin double-decker: binding of two inhibitor molecules to human
RT aldose reductase reveals a new specificity determinant.";
RL Biochemistry 36:16134-16140(1997).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC
RP INHIBITOR, AND ACTIVE SITE.
RX PubMed=15272156; DOI=10.1107/s0907444904011370;
RA Ruiz F., Hazemann I., Mitschler A., Joachimiak A., Schneider T.,
RA Karplus M., Podjarny A.;
RT "The crystallographic structure of the aldose reductase-IDD552 complex
RT shows direct proton donation from tyrosine 48.";
RL Acta Crystallogr. D 60:1347-1354(2004).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC
RP INHIBITOR.
RX PubMed=15146478; DOI=10.1002/prot.20015;
RA Howard E.I., Sanishvili R., Cachau R.E., Mitschler A., Chevrier B.,
RA Barth P., Lamour V., Van Zandt M., Sibley E., Bon C., Moras D.,
RA Schneider T.R., Joachimiak A., Podjarny A.;
RT "Ultrahigh resolution drug design I: details of interactions in human
RT aldose reductase-inhibitor complex at 0.66 A.";
RL Proteins 55:792-804(2004).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE
RP ANALOG.
RX PubMed=16337231; DOI=10.1016/j.jmb.2005.10.067;
RA Steuber H., Zentgraf M., Podjarny A., Heine A., Klebe G.;
RT "High-resolution crystal structure of aldose reductase complexed with the
RT novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site
RT anchoring group.";
RL J. Mol. Biol. 356:45-56(2006).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
RX PubMed=17505104; DOI=10.1107/s0907444907011997;
RA Biadene M., Hazemann I., Cousido A., Ginell S., Joachimiak A.,
RA Sheldrick G.M., Podjarny A., Schneider T.R.;
RT "The atomic resolution structure of human aldose reductase reveals that
RT rearrangement of a bound ligand allows the opening of the safety-belt
RT loop.";
RL Acta Crystallogr. D 63:665-672(2007).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC
RP INHIBITOR.
RX PubMed=17418233; DOI=10.1016/j.jmb.2007.03.021;
RA Steuber H., Zentgraf M., La Motta C., Sartini S., Heine A., Klebe G.;
RT "Evidence for a novel binding site conformer of aldose reductase in ligand-
RT bound state.";
RL J. Mol. Biol. 369:186-197(2007).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC
RP INHIBITOR.
RX PubMed=17368668; DOI=10.1016/j.jmb.2006.12.004;
RA Steuber H., Heine A., Klebe G.;
RT "Structural and thermodynamic study on aldose reductase: nitro-substituted
RT inhibitors with strong enthalpic binding contribution.";
RL J. Mol. Biol. 368:618-638(2007).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC carbonyl-containing compounds to their corresponding alcohols. Displays
CC enzymatic activity towards endogenous metabolites such as aromatic and
CC aliphatic aldehydes, ketones, monosacharides, bile acids and
CC xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes
CC reduction of glucose to sorbitol during hyperglycemia (PubMed:1936586).
CC Reduces steroids and their derivatives and prostaglandins. Displays low
CC enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-
CC retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes
CC the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-
CC (5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related
CC phospholipid aldehydes that are generated from the oxydation of
CC phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426).
CC Plays a role in detoxifying dietary and lipid-derived unsaturated
CC carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal,
CC trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-
CC carbonyls) (PubMed:21329684). {ECO:0000269|PubMed:12732097,
CC ECO:0000269|PubMed:17381426, ECO:0000269|PubMed:19010934,
CC ECO:0000269|PubMed:1936586, ECO:0000269|PubMed:21329684,
CC ECO:0000269|PubMed:8343525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC Evidence={ECO:0000269|PubMed:8245005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000269|PubMed:12732097,
CC ECO:0000269|PubMed:21329680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:21329680};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:12732097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000269|PubMed:10510318,
CC ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1936586,
CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:8245005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH;
CC Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000269|PubMed:10510318,
CC ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1936586,
CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:8245005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prenol = 3-methyl-2-butenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58420, ChEBI:CHEBI:15378, ChEBI:CHEBI:15825,
CC ChEBI:CHEBI:16019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:21329684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205;
CC Evidence={ECO:0000269|PubMed:21329684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)-2,4-hexadienal +
CC H(+) + NADPH; Xref=Rhea:RHEA:58428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:82334,
CC ChEBI:CHEBI:142625; Evidence={ECO:0000269|PubMed:21329684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-hydroxynonen-1-ol + NADP(+) = a 4-hydroxynonenal + H(+) +
CC NADPH; Xref=Rhea:RHEA:58336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142593, ChEBI:CHEBI:142606;
CC Evidence={ECO:0000269|PubMed:21329684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:19010934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH;
CC Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54;
CC Evidence={ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:21329684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pyridine 3-methanol = H(+) + NADPH + pyridine-3-
CC carbaldehyde; Xref=Rhea:RHEA:58776, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28345, ChEBI:CHEBI:45213, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:12732097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H(+) + NADPH = 1-hexadecanoyl-2-(5-hydroxypentanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58512, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77890,
CC ChEBI:CHEBI:142747; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine
CC + H(+) + NADPH = 1-hexadecanoyl-2-(7-hydroxyheptanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58752, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:134601,
CC ChEBI:CHEBI:142748; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H(+) + NADPH = 1-hexadecanoyl-2-(9-hydroxynonanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61042,
CC ChEBI:CHEBI:142749; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphoethanolamine + H(+) + NADPH = 1-hexadecanoyl-2-(5-
CC hydroxypentanoyl)-sn-glycero-3-phosphoethanolamine + NADP(+);
CC Xref=Rhea:RHEA:58756, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142750, ChEBI:CHEBI:142751;
CC Evidence={ECO:0000269|PubMed:17381426};
CC -!- ACTIVITY REGULATION: Cys-299 may regulate the kinetic and inhibition
CC properties of the enzyme, but does not participate in catalysis
CC (PubMed:8343525). Tolrestat inhibits retinal reduction
CC (PubMed:12732097). {ECO:0000269|PubMed:12732097,
CC ECO:0000269|PubMed:8343525}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:12732097};
CC KM=76000 uM for glucose {ECO:0000269|PubMed:12732097};
CC KM=14 uM for pyridine-3-carbaldehyde {ECO:0000269|PubMed:12732097};
CC KM=10 uM for all-trans-retinal {ECO:0000269|PubMed:12732097};
CC KM=12 uM for 9-cis-retinal {ECO:0000269|PubMed:12732097};
CC KM=14 uM for 13-cis-retinal {ECO:0000269|PubMed:12732097};
CC KM=8.8 uM for 1-O-palmitoyl-2-O-(5-oxovaleryl)-sn-glycero-3-
CC phosphocholine (POVPC) {ECO:0000269|PubMed:17381426};
CC KM=16 uM for 1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:17381426};
CC KM=13 uM for 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:17381426};
CC KM=11 uM for 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphoethanolamine {ECO:0000269|PubMed:17381426};
CC KM=884 uM for acrolein {ECO:0000269|PubMed:21329684};
CC KM=9643 uM for 3-methyl-2-butenal {ECO:0000269|PubMed:21329684};
CC KM=878 uM for (E)-2-hexenal {ECO:0000269|PubMed:21329684};
CC KM=905 uM for (E,E)-2,4-hexadienal {ECO:0000269|PubMed:21329684};
CC KM=716 uM for 4-hydroxynonenal {ECO:0000269|PubMed:21329684};
CC KM=122 uM for GS-(E)-4-hexenal {ECO:0000269|PubMed:21329684};
CC KM=7 uM for GS-hexenal {ECO:0000269|PubMed:21329684};
CC KM=5 uM for GS-4-hydroxynonenal {ECO:0000269|PubMed:21329684};
CC KM=1.9 uM for prostaglandin H2 {ECO:0000269|PubMed:19010934};
CC Vmax=26 nmol/min/mg enzyme for prostaglandin H2
CC {ECO:0000269|PubMed:19010934};
CC Note=kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is
CC 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-
CC cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for
CC acrolein as substrate. kcat is 31 min(-1) for 3-methyl-2-butenal as
CC substrate. kcat is 41 min(-1) for (E)-2-hexenal as substrate. kcat is
CC 43 min(-1) for (E,E)-2,4-hexadienal as substrate. kcat is 50 min(-1)
CC for 4-hydroxynonenal as substrate. kcat is 16 min(-1) for GS-(E)-4-
CC hexenal as substrate. kcat is 16 min(-1) for GS-hexenal as substrate.
CC kcat is 13 min(-1) for GS-4-hydroxynonenal as substrate
CC (PubMed:21329684). kcat is 31 min(-1) for D,L-glyceraldehyde
CC (PubMed:21329680). {ECO:0000269|PubMed:12732097,
CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:21329684};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15146478,
CC ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231,
CC ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233,
CC ECO:0000269|PubMed:17505104}.
CC -!- INTERACTION:
CC P15121; Q9BUY7: EFCAB11; NbExp=3; IntAct=EBI-1052491, EBI-18688654;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic epithelial cells
CC (EUE) in response to osmotic stress. {ECO:0000269|PubMed:8435445}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; J04795; AAA51713.1; -; mRNA.
DR EMBL; J05017; AAA51714.1; -; mRNA.
DR EMBL; X15414; CAA33460.1; -; mRNA.
DR EMBL; M34720; AAA35560.1; -; mRNA.
DR EMBL; M34721; AAA35561.1; -; Genomic_DNA.
DR EMBL; J05474; AAA51715.1; -; mRNA.
DR EMBL; M59783; AAA51712.1; -; Genomic_DNA.
DR EMBL; M59856; AAA51712.1; JOINED; Genomic_DNA.
DR EMBL; AF032455; AAB88851.1; -; Genomic_DNA.
DR EMBL; AF328729; AAN09721.1; -; mRNA.
DR EMBL; AK313439; BAG36230.1; -; mRNA.
DR EMBL; CR450351; CAG29347.1; -; mRNA.
DR EMBL; CR542203; CAG47000.1; -; mRNA.
DR EMBL; BT019859; AAV38662.1; -; mRNA.
DR EMBL; CH236950; EAL24070.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83814.1; -; Genomic_DNA.
DR EMBL; BC000260; AAH00260.1; -; mRNA.
DR EMBL; BC005387; AAH05387.1; -; mRNA.
DR EMBL; BC010391; AAH10391.1; -; mRNA.
DR CCDS; CCDS5831.1; -.
DR PIR; A39763; A39763.
DR RefSeq; NP_001619.1; NM_001628.3.
DR PDB; 1ABN; X-ray; 2.40 A; A=2-316.
DR PDB; 1ADS; X-ray; 1.65 A; A=2-316.
DR PDB; 1AZ1; X-ray; 1.80 A; A=2-316.
DR PDB; 1AZ2; X-ray; 2.90 A; A=2-316.
DR PDB; 1EF3; X-ray; 2.80 A; A/B=2-316.
DR PDB; 1EL3; X-ray; 1.70 A; A=1-316.
DR PDB; 1IEI; X-ray; 2.50 A; A=1-316.
DR PDB; 1MAR; X-ray; 1.80 A; A=2-316.
DR PDB; 1PWL; X-ray; 1.10 A; A=1-316.
DR PDB; 1PWM; X-ray; 0.92 A; A=1-316.
DR PDB; 1T40; X-ray; 1.80 A; A=1-316.
DR PDB; 1T41; X-ray; 1.05 A; A=1-316.
DR PDB; 1US0; X-ray; 0.66 A; A=1-316.
DR PDB; 1X96; X-ray; 1.40 A; A=1-316.
DR PDB; 1X97; X-ray; 1.40 A; A=1-316.
DR PDB; 1X98; X-ray; 1.30 A; A=1-316.
DR PDB; 1XGD; X-ray; 2.10 A; A=2-316.
DR PDB; 1Z3N; X-ray; 1.04 A; A=1-316.
DR PDB; 1Z89; X-ray; 1.43 A; A=1-316.
DR PDB; 1Z8A; X-ray; 0.95 A; A=1-316.
DR PDB; 2ACQ; X-ray; 1.76 A; A=2-316.
DR PDB; 2ACR; X-ray; 1.76 A; A=2-316.
DR PDB; 2ACS; X-ray; 1.76 A; A=2-316.
DR PDB; 2ACU; X-ray; 1.76 A; A=2-316.
DR PDB; 2AGT; X-ray; 1.00 A; A=1-316.
DR PDB; 2DUX; X-ray; 1.60 A; A=1-316.
DR PDB; 2DUZ; X-ray; 1.60 A; A=1-316.
DR PDB; 2DV0; X-ray; 1.62 A; A=1-316.
DR PDB; 2F2K; X-ray; 1.94 A; A=1-316.
DR PDB; 2FZ8; X-ray; 1.48 A; A=1-316.
DR PDB; 2FZ9; X-ray; 1.60 A; A=1-316.
DR PDB; 2FZB; X-ray; 1.50 A; A=6-316.
DR PDB; 2FZD; X-ray; 1.08 A; A=6-316.
DR PDB; 2HV5; X-ray; 1.59 A; A=1-316.
DR PDB; 2HVN; X-ray; 1.58 A; A=1-316.
DR PDB; 2HVO; X-ray; 1.65 A; A=1-316.
DR PDB; 2I16; X-ray; 0.81 A; A=1-316.
DR PDB; 2I17; X-ray; 0.81 A; A=1-316.
DR PDB; 2IKG; X-ray; 1.43 A; A=1-316.
DR PDB; 2IKH; X-ray; 1.55 A; A=1-316.
DR PDB; 2IKI; X-ray; 1.47 A; A=1-316.
DR PDB; 2IKJ; X-ray; 1.55 A; A=1-316.
DR PDB; 2INE; X-ray; 1.90 A; A=2-316.
DR PDB; 2INZ; X-ray; 1.95 A; A=2-316.
DR PDB; 2IPW; X-ray; 2.00 A; A=2-316.
DR PDB; 2IQ0; X-ray; 1.95 A; A=2-316.
DR PDB; 2IQD; X-ray; 2.00 A; A=2-316.
DR PDB; 2IS7; X-ray; 1.70 A; A=2-316.
DR PDB; 2ISF; X-ray; 2.00 A; A=2-316.
DR PDB; 2J8T; X-ray; 0.82 A; A=6-316.
DR PDB; 2NVC; X-ray; 1.65 A; A=1-316.
DR PDB; 2NVD; X-ray; 1.55 A; A=1-316.
DR PDB; 2PD5; X-ray; 1.60 A; A=1-316.
DR PDB; 2PD9; X-ray; 1.55 A; A=1-316.
DR PDB; 2PDB; X-ray; 1.60 A; A=1-316.
DR PDB; 2PDC; X-ray; 1.65 A; A=1-316.
DR PDB; 2PDF; X-ray; 1.56 A; A=1-316.
DR PDB; 2PDG; X-ray; 1.42 A; A=1-316.
DR PDB; 2PDH; X-ray; 1.45 A; A=1-316.
DR PDB; 2PDI; X-ray; 1.55 A; A=1-316.
DR PDB; 2PDJ; X-ray; 1.57 A; A=1-316.
DR PDB; 2PDK; X-ray; 1.55 A; A=1-316.
DR PDB; 2PDL; X-ray; 1.47 A; A=1-316.
DR PDB; 2PDM; X-ray; 1.75 A; A=1-316.
DR PDB; 2PDN; X-ray; 1.70 A; A=1-316.
DR PDB; 2PDP; X-ray; 1.65 A; A=1-316.
DR PDB; 2PDQ; X-ray; 1.73 A; A=1-316.
DR PDB; 2PDU; X-ray; 1.55 A; A=1-316.
DR PDB; 2PDW; X-ray; 1.55 A; A=1-316.
DR PDB; 2PDX; X-ray; 1.65 A; A=1-316.
DR PDB; 2PDY; X-ray; 1.65 A; A=1-316.
DR PDB; 2PEV; X-ray; 0.90 A; A=1-316.
DR PDB; 2PF8; X-ray; 0.85 A; A=1-316.
DR PDB; 2PFH; X-ray; 0.85 A; A=1-316.
DR PDB; 2PZN; X-ray; 1.00 A; A=1-316.
DR PDB; 2QXW; X-ray; 0.80 A; A=1-316.
DR PDB; 2R24; X-ray; 1.75 A; A=1-316.
DR PDB; 3BCJ; X-ray; 0.78 A; A=1-316.
DR PDB; 3DN5; X-ray; 1.45 A; A=1-316.
DR PDB; 3G5E; X-ray; 1.80 A; A=1-316.
DR PDB; 3GHR; X-ray; 1.00 A; A=1-316.
DR PDB; 3GHS; X-ray; 1.00 A; A=1-316.
DR PDB; 3GHT; X-ray; 1.10 A; A=1-316.
DR PDB; 3GHU; X-ray; 1.20 A; A=1-316.
DR PDB; 3LBO; X-ray; 1.10 A; A=1-316.
DR PDB; 3LD5; X-ray; 1.27 A; A=1-316.
DR PDB; 3LEN; X-ray; 1.21 A; A=1-316.
DR PDB; 3LEP; X-ray; 0.99 A; A=1-316.
DR PDB; 3LQG; X-ray; 1.35 A; A=1-316.
DR PDB; 3LQL; X-ray; 1.13 A; A=1-316.
DR PDB; 3LZ3; X-ray; 1.03 A; A=1-316.
DR PDB; 3LZ5; X-ray; 0.95 A; A=1-316.
DR PDB; 3M0I; X-ray; 1.07 A; A=1-316.
DR PDB; 3M4H; X-ray; 0.94 A; A=1-316.
DR PDB; 3M64; X-ray; 1.30 A; A=1-316.
DR PDB; 3MB9; X-ray; 1.65 A; A=1-316.
DR PDB; 3MC5; X-ray; 1.14 A; A=1-316.
DR PDB; 3ONB; X-ray; 1.45 A; A=2-316.
DR PDB; 3ONC; X-ray; 1.06 A; A=2-316.
DR PDB; 3P2V; X-ray; 1.69 A; A=1-316.
DR PDB; 3Q65; X-ray; 2.09 A; A/B=1-316.
DR PDB; 3Q67; X-ray; 1.55 A; A/B=1-316.
DR PDB; 3RX2; X-ray; 1.90 A; A=1-316.
DR PDB; 3RX3; X-ray; 1.90 A; A=1-316.
DR PDB; 3RX4; X-ray; 2.00 A; A=1-316.
DR PDB; 3S3G; X-ray; 1.80 A; A=1-316.
DR PDB; 3T42; X-ray; 1.28 A; A=1-316.
DR PDB; 3U2C; X-ray; 1.00 A; A=1-316.
DR PDB; 3V35; X-ray; 1.90 A; A=1-316.
DR PDB; 3V36; X-ray; 2.00 A; A=1-316.
DR PDB; 4GCA; X-ray; 0.90 A; A=2-316.
DR PDB; 4GQ0; X-ray; 2.10 A; A=1-316.
DR PDB; 4IGS; X-ray; 0.85 A; A=1-316.
DR PDB; 4JIR; X-ray; 2.00 A; A=1-316.
DR PDB; 4LAU; X-ray; 0.84 A; A=1-316.
DR PDB; 4LAZ; X-ray; 0.85 A; A=1-316.
DR PDB; 4LB3; X-ray; 0.80 A; A=1-316.
DR PDB; 4LB4; X-ray; 0.80 A; A=1-316.
DR PDB; 4LBR; X-ray; 0.80 A; A=1-316.
DR PDB; 4LBS; X-ray; 0.76 A; A=1-316.
DR PDB; 4NKC; X-ray; 1.12 A; A=2-316.
DR PDB; 4PR4; X-ray; 1.06 A; A=2-316.
DR PDB; 4PRR; X-ray; 1.01 A; A=2-316.
DR PDB; 4PRT; X-ray; 0.96 A; A=1-316.
DR PDB; 4PUU; X-ray; 1.14 A; A=1-316.
DR PDB; 4PUW; X-ray; 1.12 A; A=1-316.
DR PDB; 4Q7B; X-ray; 1.19 A; A=2-316.
DR PDB; 4QBX; X-ray; 0.98 A; A=1-316.
DR PDB; 4QR6; X-ray; 1.05 A; A=1-316.
DR PDB; 4QX4; X-ray; 1.26 A; A=1-316.
DR PDB; 4QXI; X-ray; 0.87 A; A=1-316.
DR PDB; 4RPQ; X-ray; 1.20 A; A=2-316.
DR PDB; 4XZH; X-ray; 1.00 A; A/B=1-316.
DR PDB; 4XZI; X-ray; 2.45 A; A=1-316.
DR PDB; 4YS1; X-ray; 1.07 A; A=1-316.
DR PDB; 4YU1; X-ray; 1.02 A; A=1-316.
DR PDB; 5HA7; X-ray; 1.65 A; A/B=1-316.
DR PDB; 5OU0; X-ray; 0.94 A; A=1-316.
DR PDB; 5OUJ; X-ray; 0.96 A; A=1-316.
DR PDB; 5OUK; X-ray; 0.96 A; A=1-316.
DR PDB; 6F7R; X-ray; 0.92 A; A=1-316.
DR PDB; 6F81; X-ray; 0.97 A; A=1-316.
DR PDB; 6F82; X-ray; 1.03 A; A=1-316.
DR PDB; 6F84; X-ray; 1.09 A; A=1-316.
DR PDB; 6F8O; X-ray; 1.17 A; A=1-316.
DR PDB; 6SYW; X-ray; 0.93 A; A=1-316.
DR PDB; 6T27; X-ray; 1.11 A; A=1-316.
DR PDB; 6T3P; X-ray; 0.97 A; A=1-316.
DR PDB; 6T5G; X-ray; 1.28 A; A=1-316.
DR PDB; 6T7Q; X-ray; 1.01 A; A=1-316.
DR PDB; 6TD8; X-ray; 0.97 A; A=1-316.
DR PDB; 6TUC; X-ray; 1.06 A; A=1-316.
DR PDB; 6TUF; X-ray; 1.15 A; A=1-316.
DR PDB; 6TXP; X-ray; 0.95 A; A=1-316.
DR PDB; 6XUM; X-ray; 0.97 A; A=1-316.
DR PDB; 6Y03; X-ray; 1.69 A; A=1-316.
DR PDB; 6Y1P; X-ray; 0.94 A; A=1-316.
DR PDBsum; 1ABN; -.
DR PDBsum; 1ADS; -.
DR PDBsum; 1AZ1; -.
DR PDBsum; 1AZ2; -.
DR PDBsum; 1EF3; -.
DR PDBsum; 1EL3; -.
DR PDBsum; 1IEI; -.
DR PDBsum; 1MAR; -.
DR PDBsum; 1PWL; -.
DR PDBsum; 1PWM; -.
DR PDBsum; 1T40; -.
DR PDBsum; 1T41; -.
DR PDBsum; 1US0; -.
DR PDBsum; 1X96; -.
DR PDBsum; 1X97; -.
DR PDBsum; 1X98; -.
DR PDBsum; 1XGD; -.
DR PDBsum; 1Z3N; -.
DR PDBsum; 1Z89; -.
DR PDBsum; 1Z8A; -.
DR PDBsum; 2ACQ; -.
DR PDBsum; 2ACR; -.
DR PDBsum; 2ACS; -.
DR PDBsum; 2ACU; -.
DR PDBsum; 2AGT; -.
DR PDBsum; 2DUX; -.
DR PDBsum; 2DUZ; -.
DR PDBsum; 2DV0; -.
DR PDBsum; 2F2K; -.
DR PDBsum; 2FZ8; -.
DR PDBsum; 2FZ9; -.
DR PDBsum; 2FZB; -.
DR PDBsum; 2FZD; -.
DR PDBsum; 2HV5; -.
DR PDBsum; 2HVN; -.
DR PDBsum; 2HVO; -.
DR PDBsum; 2I16; -.
DR PDBsum; 2I17; -.
DR PDBsum; 2IKG; -.
DR PDBsum; 2IKH; -.
DR PDBsum; 2IKI; -.
DR PDBsum; 2IKJ; -.
DR PDBsum; 2INE; -.
DR PDBsum; 2INZ; -.
DR PDBsum; 2IPW; -.
DR PDBsum; 2IQ0; -.
DR PDBsum; 2IQD; -.
DR PDBsum; 2IS7; -.
DR PDBsum; 2ISF; -.
DR PDBsum; 2J8T; -.
DR PDBsum; 2NVC; -.
DR PDBsum; 2NVD; -.
DR PDBsum; 2PD5; -.
DR PDBsum; 2PD9; -.
DR PDBsum; 2PDB; -.
DR PDBsum; 2PDC; -.
DR PDBsum; 2PDF; -.
DR PDBsum; 2PDG; -.
DR PDBsum; 2PDH; -.
DR PDBsum; 2PDI; -.
DR PDBsum; 2PDJ; -.
DR PDBsum; 2PDK; -.
DR PDBsum; 2PDL; -.
DR PDBsum; 2PDM; -.
DR PDBsum; 2PDN; -.
DR PDBsum; 2PDP; -.
DR PDBsum; 2PDQ; -.
DR PDBsum; 2PDU; -.
DR PDBsum; 2PDW; -.
DR PDBsum; 2PDX; -.
DR PDBsum; 2PDY; -.
DR PDBsum; 2PEV; -.
DR PDBsum; 2PF8; -.
DR PDBsum; 2PFH; -.
DR PDBsum; 2PZN; -.
DR PDBsum; 2QXW; -.
DR PDBsum; 2R24; -.
DR PDBsum; 3BCJ; -.
DR PDBsum; 3DN5; -.
DR PDBsum; 3G5E; -.
DR PDBsum; 3GHR; -.
DR PDBsum; 3GHS; -.
DR PDBsum; 3GHT; -.
DR PDBsum; 3GHU; -.
DR PDBsum; 3LBO; -.
DR PDBsum; 3LD5; -.
DR PDBsum; 3LEN; -.
DR PDBsum; 3LEP; -.
DR PDBsum; 3LQG; -.
DR PDBsum; 3LQL; -.
DR PDBsum; 3LZ3; -.
DR PDBsum; 3LZ5; -.
DR PDBsum; 3M0I; -.
DR PDBsum; 3M4H; -.
DR PDBsum; 3M64; -.
DR PDBsum; 3MB9; -.
DR PDBsum; 3MC5; -.
DR PDBsum; 3ONB; -.
DR PDBsum; 3ONC; -.
DR PDBsum; 3P2V; -.
DR PDBsum; 3Q65; -.
DR PDBsum; 3Q67; -.
DR PDBsum; 3RX2; -.
DR PDBsum; 3RX3; -.
DR PDBsum; 3RX4; -.
DR PDBsum; 3S3G; -.
DR PDBsum; 3T42; -.
DR PDBsum; 3U2C; -.
DR PDBsum; 3V35; -.
DR PDBsum; 3V36; -.
DR PDBsum; 4GCA; -.
DR PDBsum; 4GQ0; -.
DR PDBsum; 4IGS; -.
DR PDBsum; 4JIR; -.
DR PDBsum; 4LAU; -.
DR PDBsum; 4LAZ; -.
DR PDBsum; 4LB3; -.
DR PDBsum; 4LB4; -.
DR PDBsum; 4LBR; -.
DR PDBsum; 4LBS; -.
DR PDBsum; 4NKC; -.
DR PDBsum; 4PR4; -.
DR PDBsum; 4PRR; -.
DR PDBsum; 4PRT; -.
DR PDBsum; 4PUU; -.
DR PDBsum; 4PUW; -.
DR PDBsum; 4Q7B; -.
DR PDBsum; 4QBX; -.
DR PDBsum; 4QR6; -.
DR PDBsum; 4QX4; -.
DR PDBsum; 4QXI; -.
DR PDBsum; 4RPQ; -.
DR PDBsum; 4XZH; -.
DR PDBsum; 4XZI; -.
DR PDBsum; 4YS1; -.
DR PDBsum; 4YU1; -.
DR PDBsum; 5HA7; -.
DR PDBsum; 5OU0; -.
DR PDBsum; 5OUJ; -.
DR PDBsum; 5OUK; -.
DR PDBsum; 6F7R; -.
DR PDBsum; 6F81; -.
DR PDBsum; 6F82; -.
DR PDBsum; 6F84; -.
DR PDBsum; 6F8O; -.
DR PDBsum; 6SYW; -.
DR PDBsum; 6T27; -.
DR PDBsum; 6T3P; -.
DR PDBsum; 6T5G; -.
DR PDBsum; 6T7Q; -.
DR PDBsum; 6TD8; -.
DR PDBsum; 6TUC; -.
DR PDBsum; 6TUF; -.
DR PDBsum; 6TXP; -.
DR PDBsum; 6XUM; -.
DR PDBsum; 6Y03; -.
DR PDBsum; 6Y1P; -.
DR AlphaFoldDB; P15121; -.
DR SASBDB; P15121; -.
DR SMR; P15121; -.
DR BioGRID; 106732; 66.
DR IntAct; P15121; 12.
DR MINT; P15121; -.
DR STRING; 9606.ENSP00000285930; -.
DR BindingDB; P15121; -.
DR ChEMBL; CHEMBL1900; -.
DR DrugBank; DB07028; (2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACID.
DR DrugBank; DB07030; (5-CHLORO-2-{[(3-NITROBENZYL)AMINO]CARBONYL}PHENOXY)ACETIC ACID.
DR DrugBank; DB07450; (R)-minalrestat.
DR DrugBank; DB02101; (S,R)-fidarestat.
DR DrugBank; DB08449; 2-(3-((4,5,7-trifluorobenzo[d]thiazol-2-yl)methyl)-1H-pyrrolo[2,3-b]pyridin-1-yl)acetic acid.
DR DrugBank; DB08000; 2-(CARBOXYMETHYL)-1-OXO-1,2-DIHYDRONAPHTHO[1,2-D]ISOTHIAZOLE-4-CARBOXYLIC ACID 3,3-DIOXIDE.
DR DrugBank; DB07139; 3-[5-(3-nitrophenyl)thiophen-2-yl]propanoic acid.
DR DrugBank; DB07498; 4-[3-(3-NITROPHENYL)-1,2,4-OXADIAZOL-5-YL]BUTANOIC ACID.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR DrugBank; DB02020; Alrestatin.
DR DrugBank; DB11859; Brexanolone.
DR DrugBank; DB02994; Cacodylic acid.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB07187; CP-744809.
DR DrugBank; DB00694; Daunorubicin.
DR DrugBank; DB06246; Exisulind.
DR DrugBank; DB01039; Fenofibrate.
DR DrugBank; DB02021; Fidarestat.
DR DrugBank; DB16707; Gavorestat.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB02834; IDD552.
DR DrugBank; DB08084; IDD594.
DR DrugBank; DB01689; Inhibitor Idd 384.
DR DrugBank; DB07063; Lidorestat.
DR DrugBank; DB06077; Lumateperone.
DR DrugBank; DB02518; N-Acetylalanine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR DrugBank; DB05383; Pimagedine.
DR DrugBank; DB05533; QR-333.
DR DrugBank; DB05327; Ranirestat.
DR DrugBank; DB02712; Sorbinil.
DR DrugBank; DB00605; Sulindac.
DR DrugBank; DB02383; Tolrestat.
DR DrugBank; DB02132; Zenarestat.
DR DrugBank; DB08772; Zopolrestat.
DR DrugBank; DB07093; {3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACID.
DR DrugBank; DB07999; {4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACID.
DR DrugBank; DB08098; {[5-(5-nitro-2-furyl)-1,3,4-oxadiazol-2-yl]thio}acetic acid.
DR DrugCentral; P15121; -.
DR GuidetoPHARMACOLOGY; 2768; -.
DR SwissLipids; SLP:000001112; -.
DR GlyGen; P15121; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P15121; -.
DR PhosphoSitePlus; P15121; -.
DR SwissPalm; P15121; -.
DR BioMuta; AKR1B1; -.
DR DMDM; 113596; -.
DR DOSAC-COBS-2DPAGE; P15121; -.
DR REPRODUCTION-2DPAGE; IPI00413641; -.
DR REPRODUCTION-2DPAGE; P15121; -.
DR UCD-2DPAGE; P15121; -.
DR EPD; P15121; -.
DR jPOST; P15121; -.
DR MassIVE; P15121; -.
DR MaxQB; P15121; -.
DR PaxDb; P15121; -.
DR PeptideAtlas; P15121; -.
DR PRIDE; P15121; -.
DR ProteomicsDB; 53108; -.
DR TopDownProteomics; P15121; -.
DR Antibodypedia; 4365; 592 antibodies from 42 providers.
DR CPTC; P15121; 3 antibodies.
DR DNASU; 231; -.
DR Ensembl; ENST00000285930.9; ENSP00000285930.3; ENSG00000085662.14.
DR GeneID; 231; -.
DR KEGG; hsa:231; -.
DR MANE-Select; ENST00000285930.9; ENSP00000285930.3; NM_001628.4; NP_001619.1.
DR UCSC; uc003vrp.2; human.
DR CTD; 231; -.
DR DisGeNET; 231; -.
DR GeneCards; AKR1B1; -.
DR HGNC; HGNC:381; AKR1B1.
DR HPA; ENSG00000085662; Tissue enriched (adrenal).
DR MIM; 103880; gene.
DR neXtProt; NX_P15121; -.
DR OpenTargets; ENSG00000085662; -.
DR PharmGKB; PA24675; -.
DR VEuPathDB; HostDB:ENSG00000085662; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000153272; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P15121; -.
DR OMA; HCRFVNM; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; P15121; -.
DR TreeFam; TF106492; -.
DR BioCyc; MetaCyc:HS01502-MON; -.
DR BRENDA; 1.1.1.188; 2681.
DR BRENDA; 1.1.1.21; 2681.
DR PathwayCommons; P15121; -.
DR Reactome; R-HSA-196108; Pregnenolone biosynthesis.
DR Reactome; R-HSA-5652227; Fructose biosynthesis.
DR SABIO-RK; P15121; -.
DR SignaLink; P15121; -.
DR BioGRID-ORCS; 231; 16 hits in 1091 CRISPR screens.
DR ChiTaRS; AKR1B1; human.
DR EvolutionaryTrace; P15121; -.
DR GeneWiki; AKR1B1; -.
DR GenomeRNAi; 231; -.
DR Pharos; P15121; Tclin.
DR PRO; PR:P15121; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P15121; protein.
DR Bgee; ENSG00000085662; Expressed in right adrenal gland cortex and 209 other tissues.
DR ExpressionAtlas; P15121; baseline and differential.
DR Genevisible; P15121; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0047956; F:glycerol dehydrogenase [NADP+] activity; IEA:RHEA.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; TAS:Reactome.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IDA:UniProtKB.
DR GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
DR GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0046370; P:fructose biosynthetic process; TAS:Reactome.
DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0035809; P:regulation of urine volume; IEA:Ensembl.
DR GO; GO:0003091; P:renal water homeostasis; IEA:Ensembl.
DR GO; GO:0001523; P:retinoid metabolic process; IMP:UniProtKB.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8281941,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..316
FT /note="Aldo-keto reductase family 1 member B1"
FT /id="PRO_0000124623"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:15272156"
FT BINDING 10..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="substrate"
FT BINDING 211..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15146478,
FT ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231,
FT ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233,
FT ECO:0000269|PubMed:17505104"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8281941,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07943"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 15
FT /note="I -> F (in dbSNP:rs5054)"
FT /id="VAR_014743"
FT VARIANT 42
FT /note="H -> L (in dbSNP:rs5056)"
FT /id="VAR_014744"
FT VARIANT 73
FT /note="L -> V (in dbSNP:rs5057)"
FT /id="VAR_014745"
FT VARIANT 90
FT /note="K -> E (in dbSNP:rs2229542)"
FT /id="VAR_048213"
FT VARIANT 204
FT /note="G -> S (in dbSNP:rs5061)"
FT /id="VAR_014746"
FT VARIANT 288
FT /note="T -> I (in dbSNP:rs5062)"
FT /id="VAR_014747"
FT MUTAGEN 44
FT /note="D->N: Reduced glyceraldehyde oxidoreductase
FT activity."
FT /evidence="ECO:0000269|PubMed:8245005"
FT MUTAGEN 49
FT /note="Y->F: Complete loss of glyceraldehyde oxidoreductase
FT activity."
FT /evidence="ECO:0000269|PubMed:8245005"
FT MUTAGEN 78
FT /note="K->M: Reduced glyceraldehyde oxidoreductase
FT activity."
FT /evidence="ECO:0000269|PubMed:8245005"
FT MUTAGEN 111
FT /note="H->N: Reduced glyceraldehyde oxidoreductase
FT activity."
FT /evidence="ECO:0000269|PubMed:8245005"
FT CONFLICT 5
FT /note="L -> I (in Ref. 2; AAA51714)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="T -> I (in Ref. 10; CAG47000)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="K -> R (in Ref. 10; CAG29347)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="W -> R (in Ref. 14; AAH05387)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="N -> S (in Ref. 10; CAG29347)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..272
FT /note="IAE -> EAA (in Ref. 16; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="H -> M (in Ref. 18; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1US0"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2PDC"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3U2C"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2ACQ"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1XGD"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:1US0"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1US0"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1IEI"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3U2C"
SQ SEQUENCE 316 AA; 35853 MW; 1852E8616B5DCEAE CRC64;
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ
EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK
EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP
AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK
HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA
LLSCTSHKDY PFHEEF
