ID A0A135V0E4_9PEZI Unreviewed; 561 AA.
AC A0A135V0E4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KXH66135.1};
GN ORFNames=CSAL01_06314 {ECO:0000313|EMBL:KXH66135.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH66135.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH66135.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH66135.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH66135.1}.
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DR EMBL; JFFI01000751; KXH66135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135V0E4; -.
DR STRING; 1209931.A0A135V0E4; -.
DR OrthoDB; 2089851at2759; -.
DR Proteomes; UP000070121; 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:UP000070121};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..113
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; 60278 MW; 36B301EDCB2B5F20 CRC64;
MSSETVDVVI DSLVAAGVKH IFGVPGAKID SVFNALIDRP EIQLVVCRHE QNAAFIAGAI
GRITGRPGVC IATSGPGTSN LVTGLVTAND EGAPVVAIVG DVKRVQAAKK THQSLRGVQL
LEPVTKKTTG AVHPDQISEI MLDAFRTATA YPQGATAISL PIDIMTVGTK TSIPALPQSA
FTPPQYGTSP SASLSRAAAM IQNAKFPVLF LGSRAATPDA VEAVHGFLRK HPIPVVETFQ
AAGSISQELA HLFYGRIGLF RNQPGDKLLS QADLVIVAGY DQSEYDADAW HKSQCLEILH
LDWIPADYGA FYNPKLELVG AIAANVKALS DILANVSRPQ ESEVAKTIFT EFHDWEQSPQ
ALGQTGDGPV HPLYFIKLMQ GLLPPSTTLA SDVGSMYIWL SRFYFAYSPK SFLVSNVQQT
LGVALPWAIG ASLAQEPPCS KKVVSISGDG GFLYSGQELV TAVKQGCNIT HFVWNDGKYN
MVEFQEVDKY GRSSGVDLGG VDFVKYAEAF GARGLRVSRS SELEAVMKEA LSYQGVCIVD
VEIDYSHNHE LMKNIIQDNI S
//
