ID F7SWY6_9BURK Unreviewed; 595 AA.
AC F7SWY6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXXA_06208 {ECO:0000313|EMBL:EGP47323.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP47323.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP47323.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP47323.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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:EGP47323.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFRQ01000031; EGP47323.1; -; Genomic_DNA.
DR RefSeq; WP_006391299.1; NZ_GL982453.1.
DR AlphaFoldDB; F7SWY6; -.
DR PATRIC; fig|1003200.3.peg.1217; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_4_0_4; -.
DR OrthoDB; 9773408at2; -.
DR Proteomes; UP000004853; 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 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:SF164; PYRUVATE DECARBOXYLASE; 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 19..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 217..299
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 428..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 63673 MW; 79F1E5E08694649F CRC64;
MSTPTHAPSH QETPPPEWGS DYLAALLRHL GLEYVALNPG ASYRGLHDSL VNYLGDESPK
MLTVLHEEHA VAIAHGYAKV TGRPMGAILH ANVGLMHGSM AIFDAYCDRV PVMVFGATGP
VDSARRRPWI DWLHTSKDQG ALVRSFVKWD AEPYSLEGAR DAVLRARQIA TTQPQGPVYV
CFDSALQEAP CADAPPLLPL ARHAPPPRPG IADRLAREAA QRLHAARRPV ILIGRVSRDE
ADWDRRVALA EHCAATVLTD FKVGAAFPTR HPLHGTTPSF FMADEGLQAL READVVLSLD
WVDLAGTLRT AWGPAHTPAH VMQVSLDQVL HNGFGGEHQG LVGADTYLMC DPDEFVAQTL
EALRDLGDAR MAAADLPPEP DMAPQESGDA AEGMSLAVFS GTVSQHLRRH APACLIRANL
GWPGDAHPLA HPLDYLGYDG GGGIGSGPGM AVGAALGLRG TPRLPVAVLG DGDYLMGATA
LWTAVSYGIP LLVIVANNRS FFNDEVHQEK VAQMRSRPVE NKWIGQRIEG PEIDLAGLAR
AQGALGWGPV QTADQLARAL DEAIAAVKAG KVAVIDARVA REYAKTMAKA LGRGH
//
