ID A0A0L8I3V4_OCTBM Unreviewed; 169 AA. AC A0A0L8I3V4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 29-MAY-2024, entry version 24. DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011}; DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011}; DE Flags: Fragment; GN ORFNames=OCBIM_22036559mg {ECO:0000313|EMBL:KOF96039.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda; OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF96039.1}; RN [1] {ECO:0000313|EMBL:KOF96039.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF96039.1}; RC TISSUE=Gonad {ECO:0000313|EMBL:KOF96039.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA- CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00029341}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|PIRSR:PIRSR601834-1}; CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome CC reductase family. {ECO:0000256|ARBA:ARBA00006105}. 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; KQ416645; KOF96039.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0L8I3V4; -. DR STRING; 37653.A0A0L8I3V4; -. DR EnsemblMetazoa; Ocbimv22036559m; Ocbimv22036559m.p; Ocbimv22036559m.g. DR EnsemblMetazoa; XM_014935653.1; XP_014791139.1; LOC106884323. DR OMA; FQCYQTG; -. DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC. DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:TreeGrafter. DR CDD; cd06183; cyt_b5_reduct_like; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR InterPro; IPR001834; CBR-like. DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1. DR PANTHER; PTHR19370:SF171; NADH-CYTOCHROME B5 REDUCTASE-LIKE; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR601834-1}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR601834- KW 1}; NAD {ECO:0000256|ARBA:ARBA00023027}. FT DOMAIN 2..29 FT /note="Flavoprotein pyridine nucleotide cytochrome FT reductase-like FAD-binding" FT /evidence="ECO:0000259|Pfam:PF00970" FT DOMAIN 42..152 FT /note="Oxidoreductase FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF00175" FT BINDING 7 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1" FT BINDING 8 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:KOF96039.1" SQ SEQUENCE 169 AA; 19435 MW; D4F27D9536E3BC48 CRC64; LYPTGLMSQH IKEWQLGTVA EFKGPFGSFS ENLLKKWSKL CLLASGTGIA PMSAIVKSIL NDEDNETVIQ LLFACRFYED ILLKEDIENW ADYWNFRVLY CLSQEQESSN LDPYEERLHF GRITKTLVES KVGDVASNFF LICGSRVFNK DMANFLTELG LSEEQYFVF //