ID A0A0D1YC20_9EURO Unreviewed; 558 AA.
AC A0A0D1YC20;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:KIV80497.1};
GN ORFNames=PV11_07994 {ECO:0000313|EMBL:KIV80497.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV80497.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV80497.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV80497.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KN846953; KIV80497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YC20; -.
DR STRING; 1016849.A0A0D1YC20; -.
DR HOGENOM; CLU_013748_3_2_1; -.
DR OrthoDB; 2089851at2759; -.
DR Proteomes; UP000053599; 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:UP000053599};
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 194..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 60574 MW; 265A6664222515E9 CRC64;
MAEDTVAQII VNSVYNAGVR YVFGVPGAKI DAIFDCLQDH EEIKLIVARH EQNAAFMAAA
VGRITGTPGV CIATSGPGAS NLATGLVTAN TECDPVVALI GSVPRAMALH RTHQSMRALD
ILGPTSKTAV SIDVEDQAAE VILNAFRTAS SSPKGVSVVS IPIDVSKGKT TILPFPSQAF
LPPTYGTAPT TRLDEVIKLI QNAKLPVLFL GLRASSPRVV DAVRTLLSKF PLPTVETFQA
AGAVSKELVH NFYGRVGIFR NQVGDRLLTK SDLVLSVGYD PVEYDPNAWN PKGDGRIIHI
DVSAADYGAH YRPLHELVGS IAENLKYITQ NLQKIPESSI SEQCKSLHDE YLSWQKLPDV
KRSSGLIHPL HFITVLQGLV SKDTTVCVDV GSVYIYFMRY FFAYEPRRLL CSDGQQTLGV
GLPWAIAASL VQDPPCSEKV ISVSGDGGFM FSSQEMSTAV QQGCNITHFI WNDQAYNMVE
FQEIMKYNRS SGVKLGGVDF VKFAESFGAK GFRISDSSQV ESVIKEALAH EGVSLVDVSI
DYSQNLDLAK TIAQDQWN
//
