ID A0A077LFA5_9PSED Unreviewed; 566 AA.
AC A0A077LFA5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=PSCI_0961 {ECO:0000313|EMBL:BAP41663.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP41663.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP41663.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP41663.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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|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; AP014637; BAP41663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077LFA5; -.
DR STRING; 1028989.PSCI_0961; -.
DR KEGG; pses:PSCI_0961; -.
DR HOGENOM; CLU_013748_1_2_6; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000031652; 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 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 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}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 2..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 61961 MW; B9208D7627143AA6 CRC64;
MVVRFLRDEG VKHIYGYPGG ALLHVYDALF KEPEVSHILV RHEQAATHMA DGYARATGKA
GVVLVTSGPG ATNAITGIAT AYMDSIPMVV ISGQVPSTLV GTDAFQETDM IGISRPIVKH
SFMIKHPSEI PDVLKKAFYL AQSGRPGPVV VDLPKDMTNP AEKFEYVYPK KVKLRSYSPA
VRGHSGQIRK AVEMLLAAKR PVIYSGGGVV MGNGASPLTE LARLLDAPVT NTLMGLGGYP
GTDRQFVGML GMHGSYTANM VMHNTDVILA VGARFDDRVI NGAAKFCPNA KIIHIDIDPA
SISKTIKADV PIVGPVESVL TDMVATFKEI GQTPDQQAVG SWWKQIDEWR AGGDLFPYDR
GDGSIIKPQK VIETLHEVTK GDAYVTSDVG QHQMFAAQYY RFDKPNRWIN SGGLGTMGFG
FPAAMGIKLN FPDADVACVT GEGSIQMNIQ ELSTCLQYDL PVKIILLNNG VLGMVRQWQD
MSYGGRHSHS YVESLPDFVK LVESYGHVGI RITDLKDLKP KLEEAFAMKD RLVFVDIQVD
VSEHVYPMQI KDGSMRDMWL SKTERT
//
