ID A0A0D7KA18_9BURK Unreviewed; 565 AA.
AC A0A0D7KA18;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KJA10023.1};
GN ORFNames=RP29_13245 {ECO:0000313|EMBL:KJA10023.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA10023.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA10023.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA10023.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KJA10023.1}.
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DR EMBL; JXYQ01000042; KJA10023.1; -; Genomic_DNA.
DR RefSeq; WP_044399231.1; NZ_JXYQ01000042.1.
DR AlphaFoldDB; A0A0D7KA18; -.
DR STRING; 80878.RP29_13245; -.
DR PATRIC; fig|80878.5.peg.2425; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000032566; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule 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:SF169; 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:UP000032566};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..548
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 565 AA; 59683 MW; 5AC637D655C469DB CRC64;
MTTPFNGADA MVRMLQYNGV KHIFGLCGDT SLPFYDAMAR LDHGMDHILT RDERSAGYMA
DAYARVTGKV GVCEGPSGGG ATYLLPGLVE ANESSVAVLG ITSDVSVGAR GKFPLTELDQ
QALYKPLTKW NTTIDRVDQI PHAVRSAFRA MTTGRPGAAH ICLPYDVQKH AIDESDVWAQ
PGHDHFPAYR SAPDPAAVDE AAERLVAARS PVLICGGGVV IAGASAALDA LATLLNAPVC
TSVSGQGSLA DTHPLNAGVV GTNGGIEATR AVVAQADLVL FVGARAGSTT TEHWQMPSRK
VTILHLDVDA MTIGTNYRTD VALVGDALLG LQALHAEVQA RIGKRPADVA DGAALAARAR
AAKQAFFAPL AASLDRPIKP ERVVDVLNRL LPPRAIVVAD PGTPCPYFTA YFNAPQSGRH
FITNRAHGAL GFAMSAGVGA AVGQPDSVVV SVMGDGSFGF TCGELETIVR RNVPLKMIVF
SNSVYGWIKA SQKTGYDQRY FSVDFNRTHH ARVAEAFGVK AWQVENPADL EGAIKAALMH
DGPALVDVIS QELQDTAVPV SQWMG
//