BIEA_HUMAN
ID BIEA_HUMAN Reviewed; 296 AA.
AC P53004; A8K747; O95019; Q86UX0; Q96QL4; Q9BRW8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Biliverdin reductase A {ECO:0000303|PubMed:8631357};
DE Short=BVR A {ECO:0000303|PubMed:8631357};
DE EC=1.3.1.24 {ECO:0000269|PubMed:7929092, ECO:0000269|PubMed:8424666, ECO:0000269|PubMed:8631357};
DE AltName: Full=Biliverdin-IX alpha-reductase {ECO:0000303|PubMed:8950184};
DE Flags: Precursor;
GN Name=BLVRA {ECO:0000312|HGNC:HGNC:1062};
GN Synonyms=BLVR, BVR {ECO:0000303|PubMed:8631357};
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 VARIANT THR-3.
RX PubMed=8950184; DOI=10.1016/s0167-4781(96)00099-1;
RA Komuro A., Tobe T., Nakano Y., Yamaguchi T., Tomita M.;
RT "Cloning and characterization of the cDNA encoding human biliverdin-IX
RT alpha reductase.";
RL Biochim. Biophys. Acta 1309:89-99(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC TISSUE=Placenta;
RX PubMed=8631357; DOI=10.1111/j.1432-1033.1996.00372.x;
RA Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr.;
RT "Human biliverdin IXalpha reductase is a zinc-metalloprotein.
RT Characterization of purified and Escherichia coli expressed enzymes.";
RL Eur. J. Biochem. 235:372-381(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-3; VAL-37 AND ARG-56.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-3.
RC TISSUE=Brain, and Prostate;
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 PROTEIN SEQUENCE OF 3-36; 48-74 AND 228-248, FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8424666; DOI=10.1006/abbi.1993.1044;
RA Maines M.D., Trakshel G.M.;
RT "Purification and characterization of human biliverdin reductase.";
RL Arch. Biochem. Biophys. 300:320-326(1993).
RN [8]
RP PROTEIN SEQUENCE OF 3-22, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7929092; DOI=10.1016/s0021-9258(19)51088-2;
RA Yamaguchi T., Komoda Y., Nakajima H.;
RT "Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human
RT liver. Purification and characterization.";
RL J. Biol. Chem. 269:24343-24348(1994).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP INVOLVEMENT IN HBLVD.
RX PubMed=19580635; DOI=10.1111/j.1478-3231.2009.02029.x;
RA Gafvels M., Holmstrom P., Somell A., Sjovall F., Svensson J.O., Stahle L.,
RA Broome U., Stal P.;
RT "A novel mutation in the biliverdin reductase-A gene combined with liver
RT cirrhosis results in hyperbiliverdinaemia (green jaundice).";
RL Liver Int. 29:1116-1124(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248 AND LYS-253, 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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18] {ECO:0007744|PDB:2H63}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-296 IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human biliverdin reductase A.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Reduces the gamma-methene bridge of the open tetrapyrrole,
CC biliverdin IX alpha, to bilirubin with the concomitant oxidation of a
CC NADH or NADPH cofactor (PubMed:8631357, PubMed:8424666,
CC PubMed:7929092). Uses the reactants NADH or NADPH depending on the pH;
CC NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline
CC range (8.5-8.7) (PubMed:8631357, PubMed:8424666, PubMed:7929092).
CC NADPH, however, is the probable reactant in biological systems
CC (PubMed:7929092). {ECO:0000269|PubMed:7929092,
CC ECO:0000269|PubMed:8424666, ECO:0000269|PubMed:8631357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bilirubin IXalpha + NAD(+) = biliverdin IXalpha + H(+) + NADH;
CC Xref=Rhea:RHEA:15797, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57977, ChEBI:CHEBI:57991; EC=1.3.1.24;
CC Evidence={ECO:0000269|PubMed:7929092, ECO:0000269|PubMed:8424666,
CC ECO:0000269|PubMed:8631357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bilirubin IXalpha + NADP(+) = biliverdin IXalpha + H(+) +
CC NADPH; Xref=Rhea:RHEA:15793, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57977, ChEBI:CHEBI:57991, ChEBI:CHEBI:58349; EC=1.3.1.24;
CC Evidence={ECO:0000269|PubMed:7929092, ECO:0000269|PubMed:8424666,
CC ECO:0000269|PubMed:8631357};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:8631357};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:8631357};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for NADPH {ECO:0000269|PubMed:8631357};
CC KM=50 uM for NADH {ECO:0000269|PubMed:8631357};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.18}.
CC -!- INTERACTION:
CC P53004; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-7410441, EBI-739832;
CC P53004; P28482: MAPK1; NbExp=2; IntAct=EBI-7410441, EBI-959949;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7929092,
CC ECO:0000269|PubMed:8424666}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:7929092,
CC ECO:0000269|PubMed:8424666}.
CC -!- DISEASE: Hyperbiliverdinemia (HBLVD) [MIM:614156]: A condition
CC characterized by a green discoloration of the skin, urine, serum, and
CC other bodily fluids. It is due to increased biliverdin resulting from
CC inefficient conversion to bilirubin. Affected individuals appear to
CC have symptoms only in the context of obstructive cholestasis and/or
CC liver failure. In some cases, green jaundice can resolve after
CC resolution of obstructive cholestasis. {ECO:0000269|PubMed:19580635}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Biliverdin reductase
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/blvra/";
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DR EMBL; U34877; AAC35588.1; -; mRNA.
DR EMBL; X93086; CAA63635.1; -; mRNA.
DR EMBL; AK291862; BAF84551.1; -; mRNA.
DR EMBL; AY616754; AAT11126.1; -; Genomic_DNA.
DR EMBL; AC005189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004939; AAD05025.1; -; Genomic_DNA.
DR EMBL; AC004985; AAP21879.1; -; Genomic_DNA.
DR EMBL; BC005902; AAH05902.1; -; mRNA.
DR EMBL; BC008456; AAH08456.1; -; mRNA.
DR CCDS; CCDS5472.1; -.
DR PIR; G02066; G02066.
DR PIR; S62624; S62624.
DR RefSeq; NP_000703.2; NM_000712.3.
DR RefSeq; NP_001240752.1; NM_001253823.1.
DR RefSeq; XP_011513776.1; XM_011515474.2.
DR RefSeq; XP_016868009.1; XM_017012520.1.
DR PDB; 2H63; X-ray; 2.70 A; A/B/C/D=7-296.
DR PDBsum; 2H63; -.
DR AlphaFoldDB; P53004; -.
DR SMR; P53004; -.
DR BioGRID; 107113; 70.
DR CORUM; P53004; -.
DR DIP; DIP-42180N; -.
DR IntAct; P53004; 26.
DR MINT; P53004; -.
DR STRING; 9606.ENSP00000385757; -.
DR DrugBank; DB00157; NADH.
DR GlyGen; P53004; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53004; -.
DR MetOSite; P53004; -.
DR PhosphoSitePlus; P53004; -.
DR SwissPalm; P53004; -.
DR BioMuta; BLVRA; -.
DR DMDM; 23830892; -.
DR OGP; P53004; -.
DR REPRODUCTION-2DPAGE; IPI00294158; -.
DR EPD; P53004; -.
DR jPOST; P53004; -.
DR MassIVE; P53004; -.
DR MaxQB; P53004; -.
DR PaxDb; P53004; -.
DR PeptideAtlas; P53004; -.
DR PRIDE; P53004; -.
DR ProteomicsDB; 56566; -.
DR Antibodypedia; 13185; 368 antibodies from 28 providers.
DR DNASU; 644; -.
DR Ensembl; ENST00000265523.9; ENSP00000265523.4; ENSG00000106605.11.
DR Ensembl; ENST00000402924.5; ENSP00000385757.1; ENSG00000106605.11.
DR GeneID; 644; -.
DR KEGG; hsa:644; -.
DR MANE-Select; ENST00000265523.9; ENSP00000265523.4; NM_000712.4; NP_000703.2.
DR UCSC; uc003tir.4; human.
DR CTD; 644; -.
DR DisGeNET; 644; -.
DR GeneCards; BLVRA; -.
DR HGNC; HGNC:1062; BLVRA.
DR HPA; ENSG00000106605; Low tissue specificity.
DR MalaCards; BLVRA; -.
DR MIM; 109750; gene.
DR MIM; 614156; phenotype.
DR neXtProt; NX_P53004; -.
DR OpenTargets; ENSG00000106605; -.
DR Orphanet; 276405; Hyperbiliverdinemia.
DR PharmGKB; PA25373; -.
DR VEuPathDB; HostDB:ENSG00000106605; -.
DR eggNOG; ENOG502QTSZ; Eukaryota.
DR GeneTree; ENSGT00390000011072; -.
DR HOGENOM; CLU_053157_0_0_1; -.
DR InParanoid; P53004; -.
DR OMA; HCEQPEK; -.
DR OrthoDB; 879838at2759; -.
DR PhylomeDB; P53004; -.
DR TreeFam; TF342889; -.
DR BioCyc; MetaCyc:HS02928-MON; -.
DR BRENDA; 1.3.1.24; 2681.
DR PathwayCommons; P53004; -.
DR Reactome; R-HSA-189483; Heme degradation.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SABIO-RK; P53004; -.
DR SignaLink; P53004; -.
DR SIGNOR; P53004; -.
DR UniPathway; UPA00684; -.
DR BioGRID-ORCS; 644; 11 hits in 1086 CRISPR screens.
DR ChiTaRS; BLVRA; human.
DR EvolutionaryTrace; P53004; -.
DR GenomeRNAi; 644; -.
DR Pharos; P53004; Tbio.
DR PRO; PR:P53004; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P53004; protein.
DR Bgee; ENSG00000106605; Expressed in monocyte and 203 other tissues.
DR ExpressionAtlas; P53004; baseline and differential.
DR Genevisible; P53004; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0106276; F:biliberdin reductase NAD+ activity; IDA:UniProtKB.
DR GO; GO:0004074; F:biliverdin reductase (NAD(P)+) activity; IDA:UniProtKB.
DR GO; GO:0106277; F:biliverdin reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042167; P:heme catabolic process; IDA:UniProtKB.
DR InterPro; IPR017094; Biliverdin_Rdtase_A.
DR InterPro; IPR015249; Biliverdin_Rdtase_cat.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF09166; Biliv-reduc_cat; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Metal-binding; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:7929092,
FT ECO:0000269|PubMed:8424666"
FT /id="PRO_0000010852"
FT CHAIN 3..296
FT /note="Biliverdin reductase A"
FT /evidence="ECO:0000269|PubMed:8631357"
FT /id="PRO_0000010853"
FT BINDING 16..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2H63"
FT BINDING 44..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2H63"
FT BINDING 77..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2H63"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2H63"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000303|PubMed:8631357"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000303|PubMed:8631357"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000303|PubMed:8631357"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000303|PubMed:8631357"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 3
FT /note="A -> T (in dbSNP:rs699512)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8950184, ECO:0000269|Ref.4"
FT /id="VAR_019230"
FT VARIANT 37
FT /note="L -> V (in dbSNP:rs17245918)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019231"
FT VARIANT 56
FT /note="Q -> R (in dbSNP:rs1050916)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014851"
FT CONFLICT 121
FT /note="L -> S (in Ref. 6; AAH05902)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="AG -> SD (in Ref. 2; CAA63635)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="E -> D (in Ref. 2; CAA63635)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 182..193
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2H63"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:2H63"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:2H63"
SQ SEQUENCE 296 AA; 33428 MW; 2CF2AA7F1CDDB707 CRC64;
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS IDGVQQISLE
DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF
GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN
VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK
