ID B5JFV2_9BACT Unreviewed; 562 AA.
AC B5JFV2;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
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=VDG1235_1755 {ECO:0000313|EMBL:EDY82135.1};
OS Verrucomicrobiae bacterium DG1235.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY82135.1, ECO:0000313|Proteomes:UP000003839};
RN [1] {ECO:0000313|EMBL:EDY82135.1, ECO:0000313|Proteomes:UP000003839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY82135.1,
RC ECO:0000313|Proteomes:UP000003839};
RA Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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; DS990592; EDY82135.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JFV2; -.
DR STRING; 382464.VDG1235_1755; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_0; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000003839; 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 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF169; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
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:UP000003839};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:EDY82135.1}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 60525 MW; BA6D08160BDA5EDD CRC64;
MNYTGAEILI KLLEQQGIQR IAGIPGGANL PMYDALSRSE SIRHILARHE QGAGFIAQGQ
ARVTGEAAVF FATSGPGATN TVTALADAKL DSIPIICITG QVPQSLIGTD AFQEIDTYGL
SVPVTKHSYL VRSAAELLEV IPDAFRVAVS GRPGPVLIDI PKDVQMERIR IEEWPAVGER
DQSPEFDAKE IELAAAMING SERPIIYVGG GAIHGSAERR ILELAERIHA PVTTTLMGLG
AFPASHEQSI GMLGMHAARY TNMALEECDL LIALGARFDD RATGKVAQFC PDAKIVHIDI
DAAELHKIKT AHIGIQADLN EALECLMPLT QERRREAWLQ RIAELKREFA LEMPDSDSPT
SAYGIVRQTQ SICPPDTIVT TDVGQHQMRA AQAFTFEEPR RWLTSGGLGT MGFGVPAAIG
AALEAPDQQV VCFSGDGSLM MNIQEFATAA EEGVNLKIVL CNNNSLGLVH QQQTLFYGKN
IFASNFSSHL DFCMIARGFG VAAYDLAGSE DPKAMLEEAL KAPGCVLINV PIDVTHKVFP
MVPPGGANSE AIHEQAEREV AI
//