ID W7MBB3_GIBM7 Unreviewed; 597 AA.
AC W7MBB3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EWG44809.1};
GN ORFNames=FVEG_05795 {ECO:0000313|EMBL:EWG44809.1};
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:EWG44809.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG44809.1, 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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; DS022247; EWG44809.1; -; Genomic_DNA.
DR RefSeq; XP_018751000.1; XM_018894028.1.
DR AlphaFoldDB; W7MBB3; -.
DR STRING; 334819.W7MBB3; -.
DR EnsemblFungi; FVEG_05795T0; FVEG_05795T0; FVEG_05795.
DR GeneID; 30063757; -.
DR KEGG; fvr:FVEG_05795; -.
DR VEuPathDB; FungiDB:FVEG_05795; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OMA; VCFPYSH; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..139
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 215..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 426..581
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 65114 MW; 876DFA8819C04B95 CRC64;
MARLTTYSAS FAFFEALYEA GVRYVFANLG SDHPAIMEAL AKARELDDVK FPTVITCPHE
FVAMSMADGF ARVTGTPQCV LVHVDVGTQM LGCAMHNASC SRTPVFVFAG LSPFTLEGEM
RGSRTEHIHW LQDAHDQRAI VAQYCRYAGE FKTGKNIKQL TSRALQFATS DVPGPVYMVG
AREVMEEDIP AYSLKQEEWQ PVVPAAIPQT ELEIIIKTLA EAESPLILVG YSGRNPSTVP
ELVTLVESIP GVRVLDAMGS SLSFPFGHRA SVGVRIGGHP AIETADVILI LDCDVTWIPT
KCKPREDAKI LHIDLDPLKS NMPLYYIPAT RRYRADVGVA LKQLNEYVRT SDKYSKLTSQ
EPYISRWSKL AEEHKELLDQ AAKAAARPED TTSSPSTSYL CAQLRRLCPK DTIWCHETIT
NAPFIHEQLQ VDEPGHILGN GGGGLGWSGG ASLGVKLASD YLAGGEGKGN FVTQIVGDGT
YLFGVPGTVY WVASRYRIAT LTIVLSNKGW NAPRVSMELI HPTGYGSRIN NKDLNISFDP
TPDFSGIAKA ASGNKAWAAV IDSVDDLDRL LPAAVQQVKS GVSAILEVRL KGSWDKP
//
