ID W6QTY9_PENRF Unreviewed; 381 AA.
AC W6QTY9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=NADH:cytochrome b5 reductase (CBR) {ECO:0000313|EMBL:CDM37609.1};
GN ORFNames=PROQFM164_S06g000571 {ECO:0000313|EMBL:CDM37609.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37609.1};
RN [1] {ECO:0000313|EMBL:CDM37609.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM37609.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR601834-1};
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR EMBL; HG792020; CDM37609.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QTY9; -.
DR STRING; 1365484.W6QTY9; -.
DR OMA; GCLRFFI; -.
DR OrthoDB; 1387364at2759; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370:SF189; CYTOCHROME C MITOCHONDRIAL IMPORT FACTOR CYC2; 1.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR601834-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR601834-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 74..191
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT BINDING 167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ SEQUENCE 381 AA; 41981 MW; 8A862021D611A6BB CRC64;
MNNLSSLCCR SSQGLRAVAR PVRYASTSAT PTSPKSPRSN SRRWLSIAFV GATAAGAGAY
IQSQNTSSAT LNPETFTKYS IVSREPVSAT SSLFTLRPRI PSDSNYDVYE EAWQTGVWSV
MFKQPQLQIG RDYTPLPTTA ATSLSVDDEN EGCLRFFIRK DPFGEVSRYL HNIAVGADVE
IRGPKIECAI PKETSDIVFI AGGTGIAPAL QAAYSLLNRK NTEHRPTIHI LWANRIKDDC
AGGHSDSLKP QSRRGWFSGW FGSKSRDNTS EKPVDVVRTE ETSIIVRELE ALKAQYPGQV
IVDYYLDEEN TFIGKEDIRG AIAPASKGNS RRSNLILVSG PEGFISYMAG PKLWAQGQEL
QGPLKGIIKE LDLKEWAVWK L
//
