ID E3QTN6_COLGM Unreviewed; 561 AA.
AC E3QTN6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EFQ34311.1};
GN ORFNames=GLRG_09455 {ECO:0000313|EMBL:EFQ34311.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; GG697378; EFQ34311.1; -; Genomic_DNA.
DR RefSeq; XP_008098331.1; XM_008100140.1.
DR AlphaFoldDB; E3QTN6; -.
DR STRING; 645133.E3QTN6; -.
DR EnsemblFungi; EFQ34311; EFQ34311; GLRG_09455.
DR GeneID; 24414820; -.
DR VEuPathDB; FungiDB:GLRG_09455; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_3_2_1; -.
DR OrthoDB; 2089851at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
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 GO; GO:0034077; P:butanediol metabolic process; 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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
DR PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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:UP000008782};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 561 AA; 60349 MW; 5E0E040BEC94DC1D CRC64;
MSTETVDVVI DSLVNAGVTH IFGVPGAKID SVFNALIDRP EIKLVVCRHE QNAAFIAGAI
GRITGRPGVC IATSGPGTSN LVTGLVTAND EGAPVVALVG DVKRIQAAKK THQSLHGVQL
LKPVTKKVTG AVHPDQISEI MLDAFRTAAA YPQGATAVSL PIDIMTVGTK TFIPALPSNA
FIPPQYGTSP SASLSRAASM IQNAKFPVLF LGTRAATPEA VLAVQGFLRK HPIPVVETFQ
AAGSISRELA HLFFGRIGLF RNQPGDKLLA QADLVIVAGY DQSEYDADAW HKNQSLEILH
LDWIPADYGT FYNPKLELVG SIAANVKALS DMLANVSRPQ ESEVAKAIFT EFHAWEQSPE
ALGRTGDSPV HPLYFIKLMQ GMLPPSPTVA SDVGSMYIWL SRFYFAYSPK SFLVSNVQQT
LGVALPWAIG ASMAQDPPCS RKVISISGDG GFLYSGQELV TAVQHGCNIT HFIWNDGKYN
MVEFQEVDKY GRSSGVDLGG VDFVKYAEAF GAKGLRVSRS SELEAVMKEA LSHQGVCVVD
IEIDYSHNSE LMKNVIHDNI S
//
