ID A0A672TRH1_STRHB Unreviewed; 559 AA.
AC A0A672TRH1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Cytochrome b5 reductase 4 {ECO:0000256|ARBA:ARBA00022339};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
DE AltName: Full=Flavohemoprotein b5/b5R {ECO:0000256|ARBA:ARBA00031842};
DE AltName: Full=cb5/cb5R {ECO:0000256|ARBA:ARBA00030883};
GN Name=CYB5R4 {ECO:0000313|Ensembl:ENSSHBP00005003556.1};
OS Strigops habroptila (Kakapo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Strigops.
OX NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005003556.1, ECO:0000313|Proteomes:UP000472266};
RN [1] {ECO:0000313|Ensembl:ENSSHBP00005003556.1, ECO:0000313|Proteomes:UP000472266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jarvis E.D., Howard J., Rhie A., Phillippy A., Korlach J., Digby A.,
RA Iorns D., Eason D., Robertson B., Raemaekers T., Howe K., Lewin H.,
RA Damas J., Hastie A., Tracey A., Chow W., Fedrigo O.;
RT "Strigops habroptila (kakapo) genome, bStrHab1, primary haplotype, v2.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSHBP00005003556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR AlphaFoldDB; A0A672TRH1; -.
DR Ensembl; ENSSHBT00005004330.1; ENSSHBP00005003556.1; ENSSHBG00005003211.1.
DR GeneTree; ENSGT00940000155536; -.
DR InParanoid; A0A672TRH1; -.
DR OMA; WIRLCNS; -.
DR OrthoDB; 163533at2759; -.
DR Proteomes; UP000472266; Chromosome 7.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR CDD; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR037908; p23_NCB5OR.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE 2; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000472266}.
FT DOMAIN 91..167
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 203..294
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 311..423
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 63402 MW; 0F2ECEF85E655F87 CRC64;
MLNVPPQAFP APSSQQRAAA GGRAKSLDQR GSQSMVMLKR KVLDTLKILH CQSGRPMAIT
SLVPLKPGRS LMDWIRLTKS GKDMTGLKGR LIEVTEDELA KHNKKEDCWI CIRGFVYNVT
PYMEYHPGGE DELMKAAGTD GTDLFDQVHR WVNYESMLKE CLVGRMAVKP IAAPKEITSV
CEEKKQLNGM LPEKKVLSGA SKDLTPSYDW FQTDSLITIV IYTKQKDMNA ELVILDHEDK
RLRGEIIVDD YSYLLEVDLD HAVEEDMAVN IAEKVGKVEI ILKKKDNVHW KILGQPLESH
NTFMKRTDRG LFYRKCKLVL KTEVTHDTKL FCLLLPESTH LRVPTGQHVY LKQIIAGTEV
VKPYTPVLPF LPLDFKEPSC HDSAHIYLMI KIYSCGLFTQ ALDHLQIGDC ISVSNPEGSF
KKSQVQTSED LFLLAAGTGF TPMVKLLNFA LTEVSCLRTV KLIFFNRTED DILWRNQLEQ
LALKDQRFEI QFILSQPKKD WVGKQGMISS SLLSEFVKRS RKDSKVLICI CGPTPFTEQG
VQYLKDLGYS QEEVHPFTA
//
