ID A0A1Y5RQ28_9RHOB Unreviewed; 568 AA.
AC A0A1Y5RQ28;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:SLN22738.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:SLN22738.1};
GN Name=ilvB {ECO:0000313|EMBL:SLN22738.1};
GN ORFNames=AQS8620_00625 {ECO:0000313|EMBL:SLN22738.1};
OS Aquimixticola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aquimixticola.
OX NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN22738.1, ECO:0000313|Proteomes:UP000193862};
RN [1] {ECO:0000313|EMBL:SLN22738.1, ECO:0000313|Proteomes:UP000193862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN22738.1,
RC ECO:0000313|Proteomes:UP000193862};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFS01000002; SLN22738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RQ28; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000193862; 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 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193862};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:SLN22738.1}.
FT DOMAIN 7..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 568 AA; 60392 MW; 59324C4424E442C3 CRC64;
MSSLDNTVAH QIVRALKRHR IDCFFGQSLP SALVLACEDN GIRQISYRQE NSGGAMADAY
ARVSRRIGMV VAQNGPAATL LVPPMAEAKQ AGIPMIAFVQ EVETPTVDRN AFQELDHFAL
FHGVTKFVRR IDDPDRVDDY IDMALTAATT GKPGPVVLLL PADVLRGPQG KAPYKRTQSL
GHFPLDRPAA ASAAVAQAAR LIAGAKHPVV IAGGGVNISD ASAILGEVMD LAHLPVFTTN
MGKGAVDETH PLAGGVQGAL NGPASLARET KPLLETADVV LLIGTRTNQN GTDNWKIYPQ
GATFIHIDID PMEIGRTYEA LRLQGDARET LTALKAALAA QDLAARKAAR AGLEAKIATA
WADFESARAK YAASDETPMR PERLMAELQR LLTPETVVVA DASYSSMWVV GQLRNATTGA
RFITPRGLAG LGWGMPMGLG AAMARKGAPV IALVGDGGFA HNWAELETAM RHNIPLVTIV
LNNGILGFQK DAETVKFGKY TTSCHFGEVD HTQVAKAVGM QALRIDRVDQ IAPALREALA
ARAPRMIEVV TSPAAHPALS LFAGSLDT
//
