ID W5Q633_SHEEP Unreviewed; 296 AA.
AC W5Q633; A0A6P3E8Z7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Biliverdin reductase A {ECO:0000256|PIRNR:PIRNR037032};
DE Short=BVR A {ECO:0000256|PIRNR:PIRNR037032};
DE EC=1.3.1.24 {ECO:0000256|PIRNR:PIRNR037032};
GN Name=BLVRA {ECO:0000313|Ensembl:ENSOARP00000018173.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000018173.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000018173.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000018173.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000018173.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR037032}.
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:0000256|PIRNR:PIRNR037032};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR037032};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC degradation. {ECO:0000256|PIRNR:PIRNR037032}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|PIRNR:PIRNR037032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|PIRNR:PIRNR037032}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Biliverdin reductase
CC subfamily. {ECO:0000256|PIRNR:PIRNR037032}.
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DR EMBL; AMGL01088295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004008040.1; XM_004007991.2.
DR AlphaFoldDB; W5Q633; -.
DR SMR; W5Q633; -.
DR STRING; 9940.ENSOARP00000018173; -.
DR PaxDb; 9940-ENSOARP00000018173; -.
DR Ensembl; ENSOART00000018430.1; ENSOARP00000018173.1; ENSOARG00000016920.1.
DR GeneID; 101118353; -.
DR KEGG; oas:101118353; -.
DR CTD; 644; -.
DR eggNOG; ENOG502QTSZ; Eukaryota.
DR HOGENOM; CLU_053157_0_0_1; -.
DR OrthoDB; 2906063at2759; -.
DR UniPathway; UPA00684; -.
DR Proteomes; UP000002356; Chromosome 4.
DR Bgee; ENSOARG00000016920; Expressed in epididymis and 54 other cell types or tissues.
DR ExpressionAtlas; W5Q633; baseline.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0106276; F:biliberdin reductase NAD+ activity; IEA:UniProtKB-EC.
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:UniProtKB-UniRule.
DR GO; GO:0042167; P:heme catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 PANTHER; PTHR43377; BILIVERDIN REDUCTASE A; 1.
DR PANTHER; PTHR43377:SF1; BILIVERDIN REDUCTASE A; 1.
DR Pfam; PF09166; Biliv-reduc_cat; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037032};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037032};
KW NAD {ECO:0000256|PIRNR:PIRNR037032};
KW NADP {ECO:0000256|PIRNR:PIRNR037032, ECO:0000256|PIRSR:PIRSR037032-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR037032};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Zinc {ECO:0000256|PIRNR:PIRNR037032}.
FT DOMAIN 9..125
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 133..243
FT /note="Biliverdin reductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF09166"
FT BINDING 16..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR037032-1"
FT BINDING 44..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR037032-1"
FT BINDING 77..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR037032-1"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR037032-1"
SQ SEQUENCE 296 AA; 33613 MW; 0E1895E60330431E CRC64;
MNTEPERKFG VVVVGVGRAG SVRIRDLRSP HASSAFLNLI GFVSRRELGS IDEVPQISLE
EALSSQEVEV AFICSESSSH EDYIRQFLNA GKHVLVEYPM TLSWVAAKDL WELAEQKGKV
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAAPLEEE RFGFPAFSGI SRLTWLVSLF
GELSLVSATL EERKEDQYMK MTVCLETENK SPLTWIEEKA PGLKRNRRLS FHFRSGSLEN
MPNVGINKNI FLKDQNIFVQ KLLGQFSEEE LAAEKKRILH CLWLAGEIQK HCCSKQ
//