ID A0A1V6PB79_PENDC Unreviewed; 629 AA.
AC A0A1V6PB79;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=PENDEC_c013G05678 {ECO:0000313|EMBL:OQD73786.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD73786.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD73786.1}.
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DR EMBL; MDYL01000013; OQD73786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PB79; -.
DR STRING; 69771.A0A1V6PB79; -.
DR OMA; EDLWVVV; -.
DR OrthoDB; 1605658at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR PANTHER; PTHR43400:SF8; HYPOTHETICAL FUMARATE REDUCTASE (EUROFUNG); 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522}.
FT DOMAIN 545..621
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 518..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 67501 MW; 4F64249AF6EBDF8E CRC64;
MAAPQVIVVG GGLSGLSAAH TVYLNGGNVL VLDKQAFFGG NSTKATSGIN GALTRTQTEL
GIQDSVKQFY EDTLKSARDK ARPDLIKVLT YKSASAVEWL QDVFNLDLTL VSRLGGHSQP
RTHRGHDAKF PGMAITYALM QRLEELADAE PGRVQIVKKA NVTGINRNGN NVTGVTYTLN
GEPKSVDGIV ILATGGYAAD FGDTSLLKKH RPDTFGLSST NGTHATGDGQ KMLMEIGANG
IDMDKVQVHP TGLVDPKDPD AKFKFLAAEA LRGEGGLLLN SDGQRFSDEL GHRDYVSGQM
WKEKEKGKWP IRLVLNSKAS KVLDFHTRHY SGRGLMKKMT GKELAKEIGC GDAALKNTFD
EYNLIADGKK KDPWNKRFFH NVPFDVNDEF HVALMEPVLH FTMGGIEINE HSQVLNSEKQ
PFDGLYACGE LAGGVHGANR LGGSSLLGCV VYGRVAGDSA SQHLFQKLIA GGSTAQQRLG
QISLHIDPST PGKISVEWGG AADGSLPTVA AAPGASSVAV DSPASSASPA APQSKPDPAN
FKIPEKEYSM EEVAKHNKKD DLWIAVKGVV LDVTNWLDEH PGGANALFNF MGRDATEEFA
MLHDDEVIPK YAGHIVIGRV QGQTPSLEL
//
