BDH2_HUMAN
ID BDH2_HUMAN Reviewed; 245 AA.
AC Q9BUT1; A8K295; B4DUF6; Q503A0; Q6IA46; Q6UWD3; Q9H8S8; Q9NRX8;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=3-hydroxybutyrate dehydrogenase type 2;
DE EC=1.1.1.30 {ECO:0000269|PubMed:16380372};
DE AltName: Full=4-oxo-L-proline reductase {ECO:0000303|PubMed:35150746};
DE EC=1.1.1.104 {ECO:0000269|PubMed:35150746};
DE AltName: Full=Dehydrogenase/reductase SDR family member 6;
DE AltName: Full=Oxidoreductase UCPA;
DE AltName: Full=R-beta-hydroxybutyrate dehydrogenase;
DE AltName: Full=Short chain dehydrogenase/reductase family 15C member 1;
GN Name=BDH2; Synonyms=DHRS6 {ECO:0000303|PubMed:16380372}, SDR15C1;
GN ORFNames=UNQ6308/PRO20933;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-70.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-70.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-70.
RC TISSUE=Ovary, and Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP SER-70.
RC TISSUE=Brain, and Skin;
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 [7]
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 [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY IRON.
RX PubMed=22527885; DOI=10.1007/s00109-012-0899-7;
RA Liu Z., Lanford R., Mueller S., Gerhard G.S., Luscieti S., Sanchez M.,
RA Devireddy L.;
RT "Siderophore-mediated iron trafficking in humans is regulated by iron.";
RL J. Mol. Med. 90:1209-1221(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=35150746; DOI=10.1016/j.jbc.2022.101708;
RA Kwiatkowski S., Bozko M., Zarod M., Witecka A., Kocdemir K.,
RA Jagielski A.K., Drozak J.;
RT "Recharacterization of the Mammalian Cytosolic Type 2 (R)-beta-
RT Hydroxybutyrate Dehydrogenase (BDH2) as 4-Oxo-L-Proline Reductase (EC
RT 1.1.1.104).";
RL J. Biol. Chem. 298:101708-101708(2022).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16380372; DOI=10.1074/jbc.m511346200;
RA Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J.,
RA Oppermann U.;
RT "Characterization of human DHRS6, an orphan short chain
RT dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-
RT hydroxybutyrate dehydrogenase.";
RL J. Biol. Chem. 281:10291-10297(2006).
CC -!- FUNCTION: NAD(H)-dependent dehydrogenase/reductase with a preference
CC for cyclic substrates (PubMed:35150746) (By similarity). Catalyzes
CC stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-
CC proline, likely a detoxification mechanism for ketoprolines
CC (PubMed:35150746). Mediates the formation of 2,5-dihydroxybenzoate
CC (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and
CC associates with LCN2, thereby regulating iron transport and homeostasis
CC while protecting cells against free radical-induced oxidative stress.
CC The iron-siderophore complex is imported into mitochondria, providing
CC an iron source for mitochondrial metabolic processes in particular heme
CC synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase
CC (PubMed:16380372). {ECO:0000250|UniProtKB:Q8JZV9,
CC ECO:0000269|PubMed:16380372, ECO:0000269|PubMed:35150746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-4-hydroxy-L-proline + NAD(+) = 4-oxo-L-proline + H(+) +
CC NADH; Xref=Rhea:RHEA:13601, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:63727, ChEBI:CHEBI:84813;
CC EC=1.1.1.104; Evidence={ECO:0000269|PubMed:35150746};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13603;
CC Evidence={ECO:0000269|PubMed:35150746};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH;
CC Xref=Rhea:RHEA:20521, ChEBI:CHEBI:10983, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.30;
CC Evidence={ECO:0000269|PubMed:16380372};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=483 uM for 4-oxo-L-proline {ECO:0000269|PubMed:35150746};
CC KM=6152 uM for (R)-3-hydroxybutanoate {ECO:0000269|PubMed:35150746};
CC KM=60 uM for NAD {ECO:0000269|PubMed:16380372};
CC KM=9.1 mM for (R)-3-hydroxybutanoate {ECO:0000269|PubMed:16380372};
CC Vmax=41 umol/min/mg enzyme toward 4-oxo-L-proline
CC {ECO:0000269|PubMed:35150746};
CC Vmax=0.04 umol/min/mg enzyme toward (R)-3-hydroxybutanoate
CC {ECO:0000269|PubMed:35150746};
CC Vmax=82 nmol/min/mg enzyme toward (R)-3-hydroxybutanoate (at 30
CC degrees Celsius) {ECO:0000269|PubMed:16380372};
CC Note=kcat is 19 sec(-1) for the NADH-dependent reduction of 4-oxo-L-
CC proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of
CC (R)-3-hydroxybutanoate. {ECO:0000269|PubMed:35150746};
CC pH dependence:
CC Optimum pH is 7.5-9.0 with (R)-3-hydroxybutanoate and 6.5-7.0 with 4-
CC oxo-L-proline. {ECO:0000269|PubMed:16380372,
CC ECO:0000269|PubMed:35150746};
CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000305|PubMed:35150746}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:Q8JZV9}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16380372}.
CC -!- INTERACTION:
CC Q9BUT1; Q13952-2: NFYC; NbExp=3; IntAct=EBI-6137689, EBI-11956831;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16380372}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BUT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BUT1-2; Sequence=VSP_015859;
CC Name=3;
CC IsoId=Q9BUT1-3; Sequence=VSP_039781;
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22527885}.
CC -!- INDUCTION: Induced by low iron levels, and down-regulated by elevated
CC iron levels. {ECO:0000269|PubMed:22527885}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: Postulated to act as a 3-hydroxybutyrate dehydrogenase,
CC however its contribution to ketone body formation appears to be
CC physiologically irrelevant since it has very low affinity for the
CC substrate. {ECO:0000250|UniProtKB:Q8JZV9, ECO:0000269|PubMed:16380372,
CC ECO:0000269|PubMed:35150746}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF164790; AAF80754.1; -; mRNA.
DR EMBL; AY358841; AAQ89200.1; -; mRNA.
DR EMBL; CR457309; CAG33590.1; -; mRNA.
DR EMBL; AK023323; BAB14526.1; -; mRNA.
DR EMBL; AK290160; BAF82849.1; -; mRNA.
DR EMBL; AK300626; BAG62318.1; -; mRNA.
DR EMBL; AC097485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037277; AAH37277.1; -; mRNA.
DR EMBL; BC001953; AAH01953.1; -; mRNA.
DR EMBL; BC095414; AAH95414.1; -; mRNA.
DR CCDS; CCDS3663.1; -. [Q9BUT1-1]
DR RefSeq; NP_064524.3; NM_020139.3. [Q9BUT1-1]
DR RefSeq; XP_011530430.1; XM_011532128.2. [Q9BUT1-1]
DR RefSeq; XP_016863951.1; XM_017008462.1. [Q9BUT1-1]
DR PDB; 2AG5; X-ray; 1.84 A; A/B/C/D=1-245.
DR PDBsum; 2AG5; -.
DR AlphaFoldDB; Q9BUT1; -.
DR SMR; Q9BUT1; -.
DR BioGRID; 121228; 40.
DR IntAct; Q9BUT1; 9.
DR STRING; 9606.ENSP00000296424; -.
DR iPTMnet; Q9BUT1; -.
DR PhosphoSitePlus; Q9BUT1; -.
DR BioMuta; BDH2; -.
DR DMDM; 125987797; -.
DR EPD; Q9BUT1; -.
DR jPOST; Q9BUT1; -.
DR MassIVE; Q9BUT1; -.
DR MaxQB; Q9BUT1; -.
DR PaxDb; Q9BUT1; -.
DR PeptideAtlas; Q9BUT1; -.
DR PRIDE; Q9BUT1; -.
DR ProteomicsDB; 79125; -. [Q9BUT1-1]
DR ProteomicsDB; 79126; -. [Q9BUT1-2]
DR ProteomicsDB; 79127; -. [Q9BUT1-3]
DR Antibodypedia; 26090; 207 antibodies from 28 providers.
DR DNASU; 56898; -.
DR Ensembl; ENST00000296424.9; ENSP00000296424.4; ENSG00000164039.15. [Q9BUT1-1]
DR GeneID; 56898; -.
DR KEGG; hsa:56898; -.
DR MANE-Select; ENST00000296424.9; ENSP00000296424.4; NM_020139.4; NP_064524.3.
DR UCSC; uc003hwz.4; human. [Q9BUT1-1]
DR CTD; 56898; -.
DR DisGeNET; 56898; -.
DR GeneCards; BDH2; -.
DR HGNC; HGNC:32389; BDH2.
DR HPA; ENSG00000164039; Tissue enhanced (kidney).
DR neXtProt; NX_Q9BUT1; -.
DR OpenTargets; ENSG00000164039; -.
DR PharmGKB; PA142672559; -.
DR VEuPathDB; HostDB:ENSG00000164039; -.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000156721; -.
DR HOGENOM; CLU_010194_1_0_1; -.
DR InParanoid; Q9BUT1; -.
DR OMA; VYLCCKA; -.
DR OrthoDB; 1226147at2759; -.
DR PhylomeDB; Q9BUT1; -.
DR TreeFam; TF328795; -.
DR BioCyc; MetaCyc:HS08987-MON; -.
DR PathwayCommons; Q9BUT1; -.
DR Reactome; R-HSA-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; Q9BUT1; -.
DR SignaLink; Q9BUT1; -.
DR BioGRID-ORCS; 56898; 14 hits in 1066 CRISPR screens.
DR ChiTaRS; BDH2; human.
DR EvolutionaryTrace; Q9BUT1; -.
DR GenomeRNAi; 56898; -.
DR Pharos; Q9BUT1; Tbio.
DR PRO; PR:Q9BUT1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BUT1; protein.
DR Bgee; ENSG00000164039; Expressed in mucosa of stomach and 122 other tissues.
DR ExpressionAtlas; Q9BUT1; baseline and differential.
DR Genevisible; Q9BUT1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IDA:HGNC-UCL.
DR GO; GO:0051287; F:NAD binding; IDA:HGNC-UCL.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:HGNC-UCL.
DR GO; GO:0042168; P:heme metabolic process; ISS:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0019290; P:siderophore biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Lipid metabolism; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..245
FT /note="3-hydroxybutyrate dehydrogenase type 2"
FT /id="PRO_0000042580"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16380372,
FT ECO:0007744|PDB:2AG5"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16380372,
FT ECO:0007744|PDB:2AG5"
FT BINDING 58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16380372,
FT ECO:0007744|PDB:2AG5"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16380372,
FT ECO:0007744|PDB:2AG5"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:16380372,
FT ECO:0007744|PDB:2AG5"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039781"
FT VAR_SEQ 141..245
FT /note="VVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTVDTPSLQERIQAR
FT GNPEEARNDFLKRQKTGRFATAEEIAMLCVYLASDESAYVTGNPVIIDGGWSL -> GS
FT VSFRGLRCSYTHIIKSSAFGNRHSRDYNFKY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_015859"
FT VARIANT 70
FT /note="N -> S (in dbSNP:rs1054707)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_023602"
FT CONFLICT 95
FT /note="E -> V (in Ref. 4; BAF82849)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="V -> L (in Ref. 2; AAQ89200)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="L -> P (in Ref. 4; BAF82849)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> T (in Ref. 6; AAH95414)"
FT /evidence="ECO:0000305"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2AG5"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 145..165
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2AG5"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:2AG5"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2AG5"
SQ SEQUENCE 245 AA; 26724 MW; A6E10E9DF9304107 CRC64;
MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP GIQTRVLDVT
KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF SMNLNVRSMY LMIKAFLPKM
LAQKSGNIIN MSSVASSVKG VVNRCVYSTT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV
DTPSLQERIQ ARGNPEEARN DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID
GGWSL
