MCR1B_VANPO
ID MCR1B_VANPO Reviewed; 306 AA.
AC A7TM72;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=NADH-cytochrome b5 reductase 2-B;
DE EC=1.6.2.2;
DE AltName: Full=Mitochondrial cytochrome b reductase B;
GN Name=MCR1B; ORFNames=Kpol_529p19;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: May mediate the reduction of outer membrane cytochrome b5.
CC {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: Mitochondrion outer membrane {ECO:0000250};
CC 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; DS480420; EDO16639.1; -; Genomic_DNA.
DR RefSeq; XP_001644497.1; XM_001644447.1.
DR AlphaFoldDB; A7TM72; -.
DR SMR; A7TM72; -.
DR STRING; 436907.A7TM72; -.
DR EnsemblFungi; EDO16639; EDO16639; Kpol_529p19.
DR GeneID; 5544798; -.
DR KEGG; vpo:Kpol_529p19; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_1_1; -.
DR InParanoid; A7TM72; -.
DR OMA; LPVIRPY; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; A7TM72; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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 FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..306
FT /note="NADH-cytochrome b5 reductase 2-B"
FT /id="PRO_0000330193"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..157
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 160..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 306 AA; 33628 MW; 82800A04590324D5 CRC64;
MISSFTSLGS RPLLLSSGIA VTAAAAVYFS TGSRLANEAL HNKTFKGFKG PASTWVDLPL
VKFEDLSHDT RKFTFKLPND DDVSGISPLS FLLARPHGTW SLRGIRPYTP VSLPETQGVI
EFVIKHVPNG GMSSHMFSLK PNDTVSFTGP IVKYEWKQNK FDSVTLLGAG SGITPLYQLM
GSILSNPEDK TKINLFYANK TSDDILLKKE LDEFQQKFSD RVKIHYYLSQ PKTKDIASTG
AKKGFIAKED IESLAPASNE NTHVFVCGPE PFVKAYAGQQ GPLFFQGSFG GILKELGYTK
SQVFKV