ID   E6ZJL1_SPORE            Unreviewed;       586 AA.
AC   E6ZJL1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Related to L-lactate dehydrogenase (Cytochrome b2) {ECO:0000313|EMBL:CBQ67514.1};
GN   ORFNames=sr11464 {ECO:0000313|EMBL:CBQ67514.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ67514.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ67514.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; FQ311430; CBQ67514.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZJL1; -.
DR   EnsemblFungi; CBQ67514; CBQ67514; sr11464.
DR   VEuPathDB; FungiDB:sr11464; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG0538; Eukaryota.
DR   HOGENOM; CLU_020639_1_1_1; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000008867; Chromosome 1.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF101; DEHYDROGENASE, PUTATIVE-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   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          97..179
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          206..570
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  63176 MW;  C9F7D4212457C61B CRC64;
     MFSNAVKASV RSRASGSTLL RSSAPRRLPQ RTLHTSSSSG AASRSSSTAS SNAKGLVAGL
     VGLALLASAL PTRSVHNDQA RAPPKQVSPA AASDPDGKLI SMDEVATYNK LPLEGGKGLW
     VVIKGEVYDV TEFVDNHPGG RNIILKNAGK DVTELYEPIH PPTALEENLE ASKHIGQVDP
     STVKIVQAGE ESEKDRKRRL ARENLPSLGT VLNLDDFERI AESILSDQAW AYYASAADDE
     ITKAQNRASF NRIVFRPRIL RAIGQVDSSV KLIDSHGTGV DCALPIYVSP AAMAKLGHPD
     GELNLTRGAG KAAIIQGISA NASVGLDEML DARQKDQPVI YQLYVNKDRA ASERILRKVE
     ARGVSAVMLT VDAPVMGKRE RDRRVKGDEV EMGVDHGKDV KAQGGGVAQA ISGYIDPNLT
     WDDIAWFRNT CKLPLYLKGI QTVEDVELAA QHGVEGVVLS NHGGRSLEYS PAPLDVLVEL
     RQRRPDLFDK VEVFLDGGVR RGTDVLKAVA LGAKAVGLGR PFLYAQSGYG EAGVTRAIHI
     LQDEIHRGMQ LLGVTSLDQL TPEMIDILPR QFFYAVPKAE QPTSSD
//