MCR1_ASPCL
ID MCR1_ASPCL Reviewed; 322 AA.
AC A1CRK9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ACLA_030130;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027059; EAW08280.1; -; Genomic_DNA.
DR RefSeq; XP_001269706.1; XM_001269705.1.
DR AlphaFoldDB; A1CRK9; -.
DR SMR; A1CRK9; -.
DR STRING; 5057.CADACLAP00001774; -.
DR EnsemblFungi; EAW08280; EAW08280; ACLA_030130.
DR GeneID; 4701749; -.
DR KEGG; act:ACLA_030130; -.
DR VEuPathDB; FungiDB:ACLA_030130; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_9_1_1; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR Proteomes; UP000006701; 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..322
FT /note="NADH-cytochrome b5 reductase 2"
FT /id="PRO_0000330170"
FT TRANSMEM 32..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 72..176
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 179..214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 36040 MW; 78259A75EFB29258 CRC64;
MFARQPLRFA QPLKQGFRKY STEAPAKGKS SLAPIYISVG LAGLGVGLYR YSTASAETPV
VDRPKVFTGG EQGWVDLKLS EIENLSHNTK RLRFEFADKE AVSGLQVASA LLTKFKPAEG
KPVIRPYTPV SDEDQPGYLD LVVKVYPNGP MSEHLHSMNV DQRLEFKGPI PKYPWETNKH
KHICLIAGGT GITPMYQLAR QIFKNPEDQT KVTLVFGNVS EEDILLKKEL QELENTHPRR
FKAFYVLDNP PKEWTGGKGY VTKELLKTVL PEPKEEDIKI FVCGPPGMYK AISGPKVSPK
DQGELTGLLA ELGYNKDQVY KF
