ID A0A2I3GM60_NOMLE Unreviewed; 296 AA.
AC A0A2I3GM60;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSNLEP00000032401.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000032401.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000032401.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000032401.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ADFV01046816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01046817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01046818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01046819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003268882.1; XM_003268834.2.
DR AlphaFoldDB; A0A2I3GM60; -.
DR STRING; 61853.ENSNLEP00000032401; -.
DR Ensembl; ENSNLET00000034967.1; ENSNLEP00000032401.1; ENSNLEG00000003333.3.
DR GeneTree; ENSGT00390000011072; -.
DR InParanoid; A0A2I3GM60; -.
DR OMA; HEGHIRQ; -.
DR OrthoDB; 2906063at2759; -.
DR UniPathway; UPA00684; -.
DR Proteomes; UP000001073; Chromosome 17.
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|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037032};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
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; 33444 MW; EE3D287D9D459862 CRC64;
MNTEPKRKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS VDGVQQISLE
DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF
GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN
VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK
//
