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Database: UniProt
Entry: A0A0K1XFG8_9GAMM
LinkDB: A0A0K1XFG8_9GAMM
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ID   A0A0K1XFG8_9GAMM        Unreviewed;       574 AA.
AC   A0A0K1XFG8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN   ORFNames=AKN88_09430 {ECO:0000313|EMBL:AKX60125.1};
OS   Thiopseudomonas alkaliphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Thiopseudomonas.
OX   NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX60125.1, ECO:0000313|Proteomes:UP000063953};
RN   [1] {ECO:0000313|EMBL:AKX60125.1, ECO:0000313|Proteomes:UP000063953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E5571 {ECO:0000313|EMBL:AKX60125.1,
RC   ECO:0000313|Proteomes:UP000063953};
RX   PubMed=26679585;
RA   Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA   Juieng P., Loparev V., McQuiston J.R.;
RT   "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT   a Novel Bacterium of the Pseudomonadaceae Family.";
RL   Genome Announc. 3:e01474-15(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673,
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. {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|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; CP012365; AKX60125.1; -; Genomic_DNA.
DR   RefSeq; WP_053101426.1; NZ_JACANE010000002.1.
DR   AlphaFoldDB; A0A0K1XFG8; -.
DR   STRING; 1697053.AKN87_11950; -.
DR   GeneID; 82261157; -.
DR   KEGG; pbb:AKN87_11950; -.
DR   PATRIC; fig|1697053.3.peg.2418; -.
DR   OrthoDB; 9785953at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000063953; Chromosome.
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   CDD; cd02015; TPP_AHAS; 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; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
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   NCBIfam; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU003591}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063953};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:AKX60125.1}.
FT   DOMAIN          5..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          396..545
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  62956 MW;  751A5CD63B1FD7C7 CRC64;
     MELLSGAEMV VRSLRDEGVK YIYGYPGGAL LHVYDALFKE PELTHILVRH EQAATHMADA
     YGRATGKAGV VLVTSGPGAT NAVTGIATAY MDSIPMVVIA GQVASDMVGT DAFQETDMIG
     ISRPIVKHSF IVKDPAEIPE IIKKAFYIAE SGRPGPVVID IPKDMTNPVD KFEYSYPKKA
     KLRSYAPATR GHSGQIRKAV EMLLSAKRPI LYSGGGVILG NGSGPLTELA KQLNLPVTNT
     LMGLGGYPGT DRQFLGMLGM HGSYLANVAM HHSDVILAVG ARFDDRVING AAKFCPNAKI
     IHVDIDPASI SKLIKADIPI VGPVDNVLTE MLSVLKELGN TQDQQAMASW WKQIDEWRGN
     GRLFPFDEGD GVIIKPQRAI EVLCEVTKGD AFITSDVGQH QMFAAQHYRF NKPNRWINSG
     GLGTMGFGLP AAMGVKLNFP DEDVACVTGE GSIQMNIQEL STCLQYDLPV KIINLNNGVL
     GMVRQWQDMQ YNSRYSHSYM ESLPDFMKLA EAYGHVGMTV SKLDDLKPAM EEAFAMKNRL
     VFMDIYVDTS EHVYPMQIRD GAMRDMWLSK TERT
//
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