ID A0A099L9P4_9GAMM Unreviewed; 580 AA.
AC A0A099L9P4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KGJ99614.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KGJ99614.1};
GN ORFNames=ND16A_3714 {ECO:0000313|EMBL:KGJ99614.1};
OS Thalassotalea sp. ND16A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ99614.1, ECO:0000313|Proteomes:UP000029848};
RN [1] {ECO:0000313|EMBL:KGJ99614.1, ECO:0000313|Proteomes:UP000029848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND16A {ECO:0000313|EMBL:KGJ99614.1,
RC ECO:0000313|Proteomes:UP000029848};
RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA Hazen T.C.;
RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT Eastern Mediterranean Deep Water.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KGJ99614.1}.
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DR EMBL; JQDZ01000030; KGJ99614.1; -; Genomic_DNA.
DR RefSeq; WP_033076592.1; NZ_JQDZ01000030.1.
DR AlphaFoldDB; A0A099L9P4; -.
DR STRING; 1535422.ND16A_3714; -.
DR PATRIC; fig|1535422.3.peg.941; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000029848; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd00568; TPP_enzymes; 1.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029848};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KGJ99614.1}.
FT DOMAIN 11..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 62266 MW; DB61B7EC65088F33 CRC64;
MKKTAAWLAK YALEQVGVEY TFGIPGVHNT ELYDELNNSD LITPYLVMHE GHGGFMADAI
SRTTDAIGAM VIVPAAGVTH AASGIAEAYL DGIPMLVISG GIRNDSKFNY QLHQLDQLKL
VEGITKAAFR VDTHEQVIDT IYKAYNIAIS GEPGPVFVEI PVNLQLDKAQ ITEIKPYQPA
EQQPLTTKTI AQIKAAAQLL AEADNPVIFA GWGALKASAA LVSIAEQIGA AVSTTLQGIS
AFPANHPLHA GFSFGPAAAP AAQNAFAKAD CVLAIGTRFA EIATGSFGGT LPENLIHIDI
NPDVFDCNFN TKLAITGDAT QVCAQLSEEL EKFDSLSSQN NSALSAQLAQ DKQAHRQDWY
NHDSKARVNP ALYFDELRKQ LSDDGFVVVD DGNHTFLTAE LMPIHNARGF ISPTDFNCMG
YAVPAAIATK LAAPDKEVVA VVGDGAFMMT CMELATAVAN NIGCIIGVFN DGELSQISQA
QQIPYNRKTC TVLPQTKLQG IATATGAEYI RIQGNDDIKA GISKARTLSA NNKPVILDIN
IDYSKPTSFT QGIVKTNLKR MPLPTKMRLV GRAIYRKITD
//
