NCB5R_DICDI
ID NCB5R_DICDI Reviewed; 286 AA.
AC Q54NC1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NADH-cytochrome b5 reductase 1;
DE EC=1.6.2.2;
GN Name=cyb5r1; ORFNames=DDB_G0285399;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Electron donor reductase for cytochrome b5. The cytochrome
CC b5/NADH cytochrome b5 reductase electron transfer system supports the
CC catalytic activity of several sterol biosynthetic enzymes (By
CC similarity). {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Mitochondrion outer
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64774.1; -; Genomic_DNA.
DR RefSeq; XP_638259.1; XM_633167.1.
DR AlphaFoldDB; Q54NC1; -.
DR SMR; Q54NC1; -.
DR STRING; 44689.DDB0266821; -.
DR PaxDb; Q54NC1; -.
DR EnsemblProtists; EAL64774; EAL64774; DDB_G0285399.
DR GeneID; 8625067; -.
DR KEGG; ddi:DDB_G0285399; -.
DR dictyBase; DDB_G0285399; cyb5r1.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_2_1; -.
DR InParanoid; Q54NC1; -.
DR OMA; KDMRFSF; -.
DR PhylomeDB; Q54NC1; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-DDI-211945; Phase I - Functionalization of compounds.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54NC1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; NAD; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..286
FT /note="NADH-cytochrome b5 reductase 1"
FT /id="PRO_0000367255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 52..155
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 135..150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 161..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 31879 MW; C67113A496ECF406 CRC64;
MQISDFILVI IGSVALAAGV KYVFTLTSGS NKDKKGGEAE KGKQVEKALD PQEYRKFQLK
EKFIVNHNTR IFRFALPNED DILGLPIGQH ISLRAVVGGK EVYRPYTPIS SDEERGYFDL
LIKVYEKGAM SGYVDNMFIG DSIEVKGPKG KFNYQPNMRK SIGMLAGGTG ITPMLQVIKA
ILKNPSDKTE ISLVFGNITE EDILLKKELD ELAEKHPQFK VYYVLNNPPK GWTQGVGFVS
KEIIESRLPS PSDQTMVIMC GPPMMNKAMT GHLETIGFNE SNIFTF
