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Database: UniProt
Entry: A0A1V6TGI6_9EURO
LinkDB: A0A1V6TGI6_9EURO
Original site: A0A1V6TGI6_9EURO 
ID   A0A1V6TGI6_9EURO        Unreviewed;       474 AA.
AC   A0A1V6TGI6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSTE_c006G05897 {ECO:0000313|EMBL:OQE25455.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE25455.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
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=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OQE25455.1}.
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DR   EMBL; MLKD01000006; OQE25455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6TGI6; -.
DR   STRING; 303698.A0A1V6TGI6; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02922; FCB2_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF104; CYTOCHROME B2-LIKE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07020)-RELATED; 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT   DOMAIN          1..56
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          108..464
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          82..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  51888 MW;  7ABDD25DB8903DF1 CRC64;
     MPLTRAEIQQ HNNRQSCWVA IHGSVYDVTD EHPGGAKVIL RCAGRDATRD FDSVHSLELL
     AETLPETTLR GHIESDELVD SAKAKTTKAN DHTSSPAQTN SNDVPPPPPL NTLINLHDFE
     RVAEQYLAPN AWAYYTSAAD DELSKRNNSK AYQQVALRPR VLRKIPRVDT VTSILGHSVA
     LPVYMSPVGI AKYAHPDGEC ALARAAGEEG LAQVLANGSS MSVEKVRQSR VTEDQPLFFQ
     LYVNRDISKS VESVKRAVKA GARGIWITVD SPVVGKREMD ERMNLDISAT DSNAQGEGVA
     KVMASSISPF IDWDILNWIR DLTDLPVVIK GIQCVEDAVL AYEYGVQGIV LSNHGGRSQD
     TAQSPLLTLL EIRKFAPHIL DGKMQIFIDG GIRRGTDVLK AIALGATAVG LGRPFLYSLS
     AGYGENGVRR MVQILRQEIE ANMTFLGATC LKDLRPEMVN TSRLERDLVG SVKL
//
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