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Database: UniProt
Entry: W7LZR1_GIBM7
LinkDB: W7LZR1_GIBM7
Original site: W7LZR1_GIBM7 
ID   W7LZR1_GIBM7            Unreviewed;       489 AA.
AC   W7LZR1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=L-lactate dehydrogenase (Cytochrome) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FVEG_05790 {ECO:0000313|EMBL:EWG44803.1};
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG44803.1, ECO:0000313|Proteomes:UP000009096};
RN   [1] {ECO:0000313|EMBL:EWG44803.1, ECO:0000313|Proteomes:UP000009096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; DS022247; EWG44803.1; -; Genomic_DNA.
DR   RefSeq; XP_018750994.1; XM_018894023.1.
DR   AlphaFoldDB; W7LZR1; -.
DR   STRING; 334819.W7LZR1; -.
DR   GeneID; 30063752; -.
DR   KEGG; fvr:FVEG_05790; -.
DR   VEuPathDB; FungiDB:FVEG_05790; -.
DR   eggNOG; KOG0538; Eukaryota.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000009096; Chromosome 3.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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   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; 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:UP000009096}.
FT   DOMAIN          2..79
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          113..466
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          466..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  53260 MW;  AB697AF62095139F CRC64;
     MAKKVSVVEI RQHGTQEDLW IVVNGEVYDM TEFAPEHPGG EEIIYQHAGR DASMSYNEIH
     SSSLIKKSLP TTCHIGTLDT TTIDAAWKDQ ENDDANSDAD TPVDIVSEHK SKPDLSEIIN
     LHDFERAAEK FLATKPWAVI HTGSNDNITR DANNTFLNRI WLRPEIMRKV GKINTRQTLF
     GCDLSVPIYI SPTGGSKLGG AEGEITLARA AAKAGIVQCF ATPSSYPHLE ILEATEKHAF
     FQLYVNKDRS KSKAAIRDAI ATGKIKALFV TVDVPVISKR EEDERASSTS GPGQARDKKG
     AGFARLASSF IDPNVCWDDI QWLRSILGSI PIVVKGIQRA SDAQMALAVG CDGIVISNHG
     GRAADGVAPA ILTLLEVNRI CPEVFQSMKV LIDGGFRRGS DVVKAICLGA SAVGFGRPLL
     YSLGYGQEGV EHAINIIKDE IETAMRLCGI SDLMRDAHPG YVNTRDLDHL VPGPQDDLPS
     RRLLPESKL
//
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