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Database: UniProt
Entry: A0A179HVQ7_PURLI
LinkDB: A0A179HVQ7_PURLI
Original site: A0A179HVQ7_PURLI 
ID   A0A179HVQ7_PURLI        Unreviewed;       500 AA.
AC   A0A179HVQ7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Cytochrome b2, mitochondrial {ECO:0000313|EMBL:OAQ94585.1};
GN   ORFNames=VFPFJ_00694 {ECO:0000313|EMBL:OAQ94585.1};
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ94585.1, ECO:0000313|Proteomes:UP000078340};
RN   [1] {ECO:0000313|EMBL:OAQ94585.1, ECO:0000313|Proteomes:UP000078340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ94585.1};
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT   Phytophthora in bio-control Purpureocillium lilacinum.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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:OAQ94585.1}.
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DR   EMBL; LSBI01000001; OAQ94585.1; -; Genomic_DNA.
DR   RefSeq; XP_018183304.1; XM_018317779.1.
DR   AlphaFoldDB; A0A179HVQ7; -.
DR   STRING; 33203.A0A179HVQ7; -.
DR   GeneID; 28882828; -.
DR   KEGG; plj:VFPFJ_00694; -.
DR   OMA; RIWFRPK; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
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; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT   DOMAIN          1..77
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          103..464
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          274..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  55324 MW;  73A77FC3DDD87C68 CRC64;
     MALKGSDVAA HDNAKSCWVI IHGKAYDVTE FLPEHPGGQK IILKYAGKDA TEEFDPIHPP
     DTLDKYLDRS KHLGAVDMGT VAKEVKEEDP DEADRLERVA QKPLLSQCYN LFDFEAVARR
     VMKRTAWGYY SSAADDEITM RENHSAIHRI WFRPQILVDV ENVDFSTTML GTKCSVPFYV
     TATALGKLGN PEGEVVLTRA ARTHNVVQMI PTLASCSFDE IVDARQGDQV QWLQLYVNKD
     REITRKIVQH AEARGCKGLF ITVDAPQLGR REKDMRSKFT DQGSNVQSGQ DTDTSQGAAR
     AISSFIDPSL SWKDIPWFRS ITSMPIILKG VQRVEDVLCA VDAGVQGVVL SNHGGRQLDF
     ARSGIEVLAE TMPVLRERGV DPERFQVFVD GGFRRASDIL KALCLGATGV GIGRPFLYAM
     SAYGQDGVER AMQLLKDEME MNMRLIGCAS VRDLHPGLLD TRGLFIHSNS TPPDALSATV
     YDPLVVPPQR PKGPPVKAKL
//
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