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Biliverdin reductase A (BVR A) (EC 1.3.1.24) (Biliverdin-IX alpha-reductase)

 BIEA_RAT                Reviewed;         295 AA.
P46844;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 134.
RecName: Full=Biliverdin reductase A;
Short=BVR A;
EC=1.3.1.24;
AltName: Full=Biliverdin-IX alpha-reductase;
Flags: Precursor;
Name=Blvra; Synonyms=Blvr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Kidney;
PubMed=1371282;
Fakhrai H., Maines M.D.;
"Expression and characterization of a cDNA for rat kidney biliverdin
reductase. Evidence suggesting the liver and kidney enzymes are the
same transcript product.";
J. Biol. Chem. 267:4023-4029(1992).
[2]
PROTEIN SEQUENCE OF 119-136, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[3]
MUTAGENESIS.
PubMed=8020496; DOI=10.1111/j.1432-1033.1994.tb18902.x;
McCoubrey W.K. Jr., Maines M.D.;
"Site-directed mutagenesis of cysteine residues in biliverdin
reductase. Roles in substrate and cofactor binding.";
Eur. J. Biochem. 222:597-603(1994).
[4]
CRYSTALLIZATION.
PubMed=10957639; DOI=10.1107/S0907444900008520;
Sun D., Sato M., Yoshida T., Shimizu H., Miyatake H., Adachi S.,
Shiro Y., Kikuchi A.;
"Crystallization and preliminary X-ray diffraction analysis of a rat
biliverdin reductase.";
Acta Crystallogr. D 56:1180-1182(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 8-291 IN COMPLEX WITH NAD.
PubMed=12079357; DOI=10.1016/S0022-2836(02)00383-2;
Whitby F.G., Phillips J.D., Hill C.P., McCoubrey W.K. Jr.,
Maines M.D.;
"Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor
complex.";
J. Mol. Biol. 319:1199-1210(2002).
-!- FUNCTION: Reduces the gamma-methene bridge of the open
tetrapyrrole, biliverdin IX alpha, to bilirubin with the
concomitant oxidation of a NADH or NADPH cofactor.
-!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
degradation.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the
pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the
alkaline range (8.5-8.7). NADPH, however, is the probable reactant
in biological systems.
-!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Biliverdin
reductase subfamily. {ECO:0000305}.
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EMBL; M81681; AAA40830.1; -; mRNA.
PIR; A42268; A42268.
RefSeq; NP_446302.1; NM_053850.1.
UniGene; Rn.9865; -.
PDB; 1GCU; X-ray; 1.40 A; A=1-295.
PDB; 1LC0; X-ray; 1.20 A; A=5-295.
PDB; 1LC3; X-ray; 1.50 A; A=5-295.
PDBsum; 1GCU; -.
PDBsum; 1LC0; -.
PDBsum; 1LC3; -.
ProteinModelPortal; P46844; -.
SMR; P46844; -.
STRING; 10116.ENSRNOP00000015843; -.
iPTMnet; P46844; -.
PhosphoSitePlus; P46844; -.
PaxDb; P46844; -.
PRIDE; P46844; -.
GeneID; 116599; -.
KEGG; rno:116599; -.
UCSC; RGD:620721; rat.
CTD; 644; -.
RGD; 620721; Blvra.
eggNOG; ENOG410IH7U; Eukaryota.
eggNOG; ENOG4111FZX; LUCA.
HOGENOM; HOG000231884; -.
HOVERGEN; HBG003218; -.
InParanoid; P46844; -.
KO; K00214; -.
PhylomeDB; P46844; -.
BRENDA; 1.3.1.24; 5301.
SABIO-RK; P46844; -.
UniPathway; UPA00684; -.
EvolutionaryTrace; P46844; -.
PRO; PR:P46844; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0004074; F:biliverdin reductase activity; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0042167; P:heme catabolic process; IEA:InterPro.
GO; GO:0055114; P:oxidation-reduction process; ISO:RGD.
InterPro; IPR017094; Biliverdin_Rdtase_A.
InterPro; IPR015249; Biliverdin_Rdtase_cat.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000683; Oxidoreductase_N.
Pfam; PF09166; Biliv-reduc_cat; 1.
Pfam; PF01408; GFO_IDH_MocA; 1.
PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
ProDom; PD040165; Biliverdin_Rdtase_cat; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Metal-binding; NAD; NADP; Oxidoreductase;
Phosphoprotein; Reference proteome; Zinc.
PROPEP 1 2
/FTId=PRO_0000010856.
CHAIN 3 295 Biliverdin reductase A.
/FTId=PRO_0000010857.
NP_BIND 15 20 NAD or NADP.
{ECO:0000269|PubMed:12079357}.
NP_BIND 76 79 NAD or NADP.
{ECO:0000269|PubMed:12079357}.
COMPBIAS 11 16 Poly-Val.
METAL 279 279 Zinc. {ECO:0000255}.
METAL 280 280 Zinc. {ECO:0000255}.
METAL 291 291 Zinc. {ECO:0000255}.
METAL 292 292 Zinc. {ECO:0000255}.
BINDING 97 97 NAD or NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:12079357}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 173 173 Phosphothreonine.
{ECO:0000250|UniProtKB:P53004}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:P53004}.
MOD_RES 247 247 N6-acetyllysine.
{ECO:0000250|UniProtKB:P53004}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:P53004}.
MUTAGEN 73 73 C->A: Loss of activity.
{ECO:0000269|PubMed:8020496}.
MUTAGEN 280 280 C->A: Reduced activity.
{ECO:0000269|PubMed:8020496}.
MUTAGEN 291 291 C->A: Reduced activity.
{ECO:0000269|PubMed:8020496}.
STRAND 8 14 {ECO:0000244|PDB:1LC0}.
HELIX 18 27 {ECO:0000244|PDB:1LC0}.
HELIX 30 33 {ECO:0000244|PDB:1LC0}.
STRAND 36 42 {ECO:0000244|PDB:1LC0}.
STRAND 53 55 {ECO:0000244|PDB:1LC0}.
HELIX 58 63 {ECO:0000244|PDB:1LC0}.
STRAND 65 72 {ECO:0000244|PDB:1LC0}.
HELIX 76 78 {ECO:0000244|PDB:1LC0}.
HELIX 79 88 {ECO:0000244|PDB:1LC0}.
STRAND 92 97 {ECO:0000244|PDB:1LC0}.
HELIX 103 115 {ECO:0000244|PDB:1LC0}.
STRAND 120 123 {ECO:0000244|PDB:1LC0}.
HELIX 125 128 {ECO:0000244|PDB:1LC0}.
HELIX 130 139 {ECO:0000244|PDB:1LC0}.
STRAND 144 154 {ECO:0000244|PDB:1LC0}.
HELIX 158 161 {ECO:0000244|PDB:1LC0}.
HELIX 164 167 {ECO:0000244|PDB:1LC0}.
HELIX 169 179 {ECO:0000244|PDB:1LC0}.
STRAND 183 192 {ECO:0000244|PDB:1LC0}.
HELIX 193 195 {ECO:0000244|PDB:1LC0}.
STRAND 197 205 {ECO:0000244|PDB:1LC0}.
STRAND 211 218 {ECO:0000244|PDB:1LC0}.
STRAND 225 234 {ECO:0000244|PDB:1LC0}.
STRAND 235 237 {ECO:0000244|PDB:1GCU}.
HELIX 249 261 {ECO:0000244|PDB:1LC0}.
HELIX 267 290 {ECO:0000244|PDB:1LC0}.
SEQUENCE 295 AA; 33566 MW; 219C8EA96C150588 CRC64;
MDAEPKRKFG VVVVGVGRAG SVRLRDLKDP RSAAFLNLIG FVSRRELGSL DEVRQISLED
ALRSQEIDVA YICSESSSHE DYIRQFLQAG KHVLVEYPMT LSFAAAQELW ELAAQKGRVL
HEEHVELLME EFEFLRREVL GKELLKGSLR FTASPLEEER FGFPAFSGIS RLTWLVSLFG
ELSLISATLE ERKEDQYMKM TVQLETQNKG LLSWIEEKGP GLKRNRYVNF QFTSGSLEEV
PSVGVNKNIF LKDQDIFVQK LLDQVSAEDL AAEKKRIMHC LGLASDIQKL CHQKK


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