ID A0A135TID5_9PEZI Unreviewed; 561 AA.
AC A0A135TID5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KXH47887.1};
GN ORFNames=CNYM01_01405 {ECO:0000313|EMBL:KXH47887.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH47887.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH47887.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH47887.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
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:KXH47887.1}.
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DR EMBL; JEMN01001107; KXH47887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TID5; -.
DR Proteomes; UP000070054; 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 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; 60155 MW; 1F1499DB1E47866D CRC64;
MSSETVDVVI DSLVAAGVKH IFGVPGAKID SVFNALIDRP EIQLVVCRHE QNAAFIAGAI
GRITGRPGVC IATSGPGTSN LVTGLVTAND EGAPVVAIVG DVKRVQAAKK THQSLRGVQL
LEPVTKKTTG AVHPDQISEI MLDAFRTATA YPQGATAISL PIDIMTVGTK TSIPALPPSA
FTPPQYGTSP SASLSRAAAM IQNAKFPVLF LGSRAATPDA VEAVHGFLRK HPIPVVETFQ
AAGSISQELA HLFYGRIGLF RNQPGDKLLS QADLVIVAGY DQSEYDADAW HKSQSLEILH
LDWIPADYGA FYNPKLELVG AIAANVKALG DILANVSRPQ ESEIAKSIFT EFHAWEQSPQ
ALGQTGDGPV HPLYFIKLMQ GLLPPSTTLA SDVGSMYIWL SRFYFAYSPK SFLISNVQQT
LGVALPWAIG ASLAQEPPCS KKVVSISGDG GFLYSGQELV TAVKQGCNIT HFIWNDGKYN
MVEFQEVDKY GRSSGVDLGG VDFVKYAEAF GAKGLRVSRS LELEAVMNEA LSYQGVCIVD
VEIDYSHNHE LMKNVIQDNI S
//
