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Database: UniProt
Entry: A0A1L7WDI8_9HELO
LinkDB: A0A1L7WDI8_9HELO
Original site: A0A1L7WDI8_9HELO 
ID   A0A1L7WDI8_9HELO        Unreviewed;       490 AA.
AC   A0A1L7WDI8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Related to cytochrome b2, mitochondrial {ECO:0000313|EMBL:CZR50845.1};
GN   ORFNames=PAC_00719 {ECO:0000313|EMBL:CZR50845.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR50845.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR50845.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR50845.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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DR   EMBL; FJOG01000001; CZR50845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WDI8; -.
DR   STRING; 576137.A0A1L7WDI8; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000184330; 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; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF82; CYTOCHROME B2, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G07200)-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   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; 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:UP000184330}.
FT   DOMAIN          2..79
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          101..468
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          81..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  53295 MW;  3DCD8A331CA35FC8 CRC64;
     MAKIFDAAEV AKHNTPEDCW VCLYGDVWDV TEFLPGHPGG SKIILQLAGR DATEDYDPIH
     PPGTLEGNLK PEAKLGKIDP ATIPLAKPDD AEKEQEKEGP PDMQSLLNLD EIEEVATKQV
     SKKCWAYYYS AADDLISKSF NNLVYKQILL RPRVFVDCTR CDTSTSLLGH KVGIPLYVSP
     AAMARLAHPD GEHGIAQGIS TFGALQIVSN NASMTPEQIV EGSLPGQIFG WQLYVQNDRK
     KSEDMLVRIN KMSDKYKFIC LTLDAPVPGK REHDEKQQTV GASLPVSSSI KEAGGKPGGG
     GVGQQLFWGT AADLTWESTL PWLAKHTKLP IVLKGLQTHE DAYLAAQYAP QVKAIILSNH
     GGRALDTAPP AVHTLLEIRK YCPEVFSRIE VWVDGGIKRG TDVVKALCLG AKAVGVGRPA
     LFGLGAGGTE GVHRTFEILK AETETCMRLL GVEKVSKLGP KHINSRAVER DIYDGHAGLE
     KLGLWVKANL
//
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