NB5R4_XENTR
ID NB5R4_XENTR Reviewed; 523 AA.
AC Q28CZ9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome b5 reductase 4;
DE EC=1.6.2.2;
DE AltName: Full=Flavohemoprotein b5/b5R;
DE Short=b5+b5R;
DE AltName: Full=cb5/cb5R;
GN Name=cyb5r4; ORFNames=TGas070l21.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic
CC reticulum stress response pathway. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Soluble protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; CR855785; CAJ83762.1; -; mRNA.
DR RefSeq; NP_001016756.1; NM_001016756.2.
DR AlphaFoldDB; Q28CZ9; -.
DR SMR; Q28CZ9; -.
DR STRING; 8364.ENSXETP00000048892; -.
DR PaxDb; Q28CZ9; -.
DR GeneID; 549510; -.
DR KEGG; xtr:549510; -.
DR CTD; 51167; -.
DR Xenbase; XB-GENE-984179; cyb5r4.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0536; Eukaryota.
DR HOGENOM; CLU_003827_0_2_1; -.
DR InParanoid; Q28CZ9; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q28CZ9; -.
DR Reactome; R-XTR-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IBA:GO_Central.
DR CDD; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 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; PTHR19370; 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; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF63380; SSF63380; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..523
FT /note="Cytochrome b5 reductase 4"
FT /id="PRO_0000287560"
FT DOMAIN 54..130
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 167..258
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 275..387
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 89
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 367..382
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 394..426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 523 AA; 59216 MW; BF4CEECC9085903C CRC64;
MLNVPSQSFP APSSQQRVAA IGRSKVPLKP GRSLMDWIRL TKSGKDLTGL KGRLIDVTEE
ELAQHNKKED CWICIRGMVY NITPYMEYHP GGEEELMKAA GRDGTDLFDQ VHRWVNYESM
LKECLIGRMA IKHVSISKEV TSVENKMNKH LNGSVASSKM SRTSSKESHP WYDWFQTESL
VTVAVYTKMK NVCSELVIVD HLENVLRGEI IIGDYSYLLH SELSHPVQKD IEVKVSATAG
KIEIKMKKKE PVSWKSLGQP MDGHNSFLKH SQRGLYYRKC RLASKTDINY NTKLFCVQLP
QGCHLQVPVG HHIYLKMNIS GVDIVKPYTP VASCLLPDAQ YSTFCNKQCL YLMIKIYPNG
SITPHLENLT VGDYISISNP QGTFSSFQIE NVMDVFLVAA GTGITPMIRL LQHVLTCVSS
LRKAKLIFFN KKEEDILWKE QVEELSLADK RFEAQLILSE PSVKWTGYRG QISYSLLNES
ILRTEEGSKI LICICGPNAF VDQGISFLQD LGFSKEEVFA FRE
