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Database: UniProt
Entry: A0A0K9JQQ7_9BURK
LinkDB: A0A0K9JQQ7_9BURK
Original site: A0A0K9JQQ7_9BURK 
ID   A0A0K9JQQ7_9BURK        Unreviewed;       587 AA.
AC   A0A0K9JQQ7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-DEC-2017, entry version 17.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=BUMB_02175 {ECO:0000313|EMBL:KMY85629.1};
OS   Candidatus Paraburkholderia calva.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=242161 {ECO:0000313|EMBL:KMY85629.1, ECO:0000313|Proteomes:UP000053570};
RN   [1] {ECO:0000313|Proteomes:UP000053570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot6 {ECO:0000313|Proteomes:UP000053570};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMY85629.1}.
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DR   EMBL; LFLF01000072; KMY85629.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMY85629; KMY85629; BUMB_02175.
DR   PATRIC; fig|242161.4.peg.5878; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000053570; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053570};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053570};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KMY85629.1}.
FT   DOMAIN       23    188       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      211    347       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      410    558       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   587 AA;  64666 MW;  C5EC2C4F68B55079 CRC64;
     MNMPSAEFST SDTTTSHEAD SIGGTVLMRA LADENVEFIW GYPGGSVLYI YDELYKQDKI
     QHILVRHEQA AVHAADAYAR STGNVGVCLV TSGPGVTNAV TGIATAYMDS IPLVVISGQV
     PTAAIGLDAF QECDTVGITR PCMKHNVLVK DVRALAATIK KAFYIARTGR PGPVLIDIPK
     DVSKAPCKYE PIKSVSLRSY NPVTKGHSGQ IRKAVQLLLS AKRPYIYTGG GIILADASRE
     LNQFADLLGY PVTNTLMGLG GYRASDKKFL GMLGMHGTYE ANMAMQNCDV LIAIGARFDD
     RVIGDPKHFA SSPRKIIHID IDPSSISKRV KVDIPIVGDV KEVLKELIEQ LQHAEHGPDT
     QALNTWWDKI EGWRSKDCLA YDRKSDIITP QYVVEKLAEL TYGNAFVCSD VGQHQMWAAQ
     FYPFNKPRRW INSGGLGTMG FGLPAAMGVK MAYPDDEVVC ITGEGSIQMC IQELSTCKQY
     NTPVKIISLN NRYLGMVRQW QQIEYKKRYS SSYMDALPDF VKLAEAYGHV GIRVEKTADV
     EPALKEALRL KDRTVFLDFQ TDPTENVFPM VQAGKGITEM LLGSEDL
//
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