ID A0A1P8UE08_9GAMM Unreviewed; 564 AA.
AC A0A1P8UE08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BW247_02325 {ECO:0000313|EMBL:APZ42075.1};
OS Acidihalobacter ferrooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ42075.1, ECO:0000313|Proteomes:UP000243807};
RN [1] {ECO:0000313|EMBL:APZ42075.1, ECO:0000313|Proteomes:UP000243807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V8 {ECO:0000313|EMBL:APZ42075.1,
RC ECO:0000313|Proteomes:UP000243807};
RA Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA Watkin E.L.J.;
RT "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT V8).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019434; APZ42075.1; -; Genomic_DNA.
DR RefSeq; WP_076835462.1; NZ_CP019434.1.
DR AlphaFoldDB; A0A1P8UE08; -.
DR STRING; 1765967.BW247_02325; -.
DR OrthoDB; 9785953at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000243807; 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:UP000243807};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 61752 MW; 16748877CAD74C47 CRC64;
MELTGAEIFV RCLREEGVDI LFGYPGGAVL HIYDVLYRQE EVSHVLVRHE QAAVHAAEGF
AKSTGRVGVA LVTSGPGATN AVTGIADAYM DSVPLVVFTG QVPTHVIGSD AFQETDSVGI
TRPIVKHNFL VKDVADMAET IKKAFYIAAS GRPGPVVVDL PKDVTAAKTN FKYPKSIRLR
SYKPTIKGHP GQIKRALEMI VKAEKPIVYA GGGVVLGGAS EELTTFTREL GYPITNTLMG
LGGYPASDTQ SLGMLGMHGT YEANMAMHHA DVVIAIGARF DDRVTGNIDK FCPHAKIVHM
DVDPASISKT VKVDVPIVGQ VKEILGDLIA ALRDSGKKPK ADALKAWWKQ IDEWRSMDCL
KYDRESELIK PQYVIERLHA LTGGDAYVTS DVGQHQMWAA QYYKFDKPNR WINSGGLGTM
GVGLPFAMGV QMAHPEATVA CITGEGSIQM CIQELSTCLQ YGLPLKIVLL NNRYLGMVRQ
WQEFFYQGRY AMSYMNALPD FVKLAEAYGH VGMQIERPQD VDGALQEALA MKDRLVFMNF
ITDDTENVYP MIPAGAGQNE MILI
//
