MCR1_PICGU
ID MCR1_PICGU Reviewed; 294 AA.
AC A5DQE4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=NADH-cytochrome b5 reductase 2;
DE EC=1.6.2.2;
DE AltName: Full=Mitochondrial cytochrome b reductase;
GN Name=MCR1; ORFNames=PGUG_05495;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408161; EDK41397.2; -; Genomic_DNA.
DR RefSeq; XP_001482475.1; XM_001482425.1.
DR AlphaFoldDB; A5DQE4; -.
DR SMR; A5DQE4; -.
DR STRING; 4929.XP_001482475.1; -.
DR EnsemblFungi; EDK41397; EDK41397; PGUG_05495.
DR GeneID; 5124220; -.
DR KEGG; pgu:PGUG_05495; -.
DR VEuPathDB; FungiDB:PGUG_05495; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_1_1; -.
DR InParanoid; A5DQE4; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR Proteomes; UP000001997; 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..294
FT /note="NADH-cytochrome b5 reductase 2"
FT /id="PRO_0000330188"
FT TRANSMEM 11..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..149
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 152..187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 32570 MW; 83D98BB5338749AE CRC64;
MSLARFTQPR VLLPVVAAAT SIGLVYHYSS LSIQNDTAKT FKGGDEWIDL KLKKSWDVSS
NTRHFVFELK SPEDVSGLVT ASCLMTKFVT AKGNNVIRPY TPVSDVDQKG TIDFVIKKYD
GGKMSTHFHG LKEGDTVSFK GPIVKWKWEP NQFQSIALIG GGTGITPLYQ LLHEITKNPE
DKTKVKLFYG NLTEEDILIK KELDDIAEKH KDQVSITYFV DKASANWKGE TGHIDKEFLQ
SNLPGPSKDS KVFVCGPPGL YKALSGVKVS PTDQGEVTGV LAELGYTKEN VYKF
