ID H8GHB4_METAL Unreviewed; 578 AA.
AC H8GHB4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Metal_1087 {ECO:0000313|EMBL:EIC28905.1};
OS Methylomicrobium album BG8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomicrobium.
OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC28905.1, ECO:0000313|Proteomes:UP000005090};
RN [1] {ECO:0000313|EMBL:EIC28905.1, ECO:0000313|Proteomes:UP000005090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG8 {ECO:0000313|EMBL:EIC28905.1,
RC ECO:0000313|Proteomes:UP000005090};
RX PubMed=23580712;
RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA Stein L.Y.;
RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT Methylomicrobium album Strain BG8.";
RL Genome Announc. 1:E0017013-E0017013(2013).
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; CM001475; EIC28905.1; -; Genomic_DNA.
DR RefSeq; WP_005370348.1; NZ_CM001475.1.
DR AlphaFoldDB; H8GHB4; -.
DR STRING; 686340.Metal_1087; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000005090; 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:UP000005090};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 64019 MW; 56100E833BBC00D8 CRC64;
MELNGAQILV QSLKDEGVEY IFGYPGGAVL HLYDALFQQQ DIKHILVRHE QGATHAADGY
ARATGKPGVV LVTSGPGATN AITGIATAYM DSIPLVVISG QVSMPVIGSD AFQEVDMIGI
SRPCVKHNFL VKDVNKIAET VKKAFYIATT GRPGPVVVDI PKDMTDPRIK VPYHYPKKVS
IRSYNPTVTG HKGQIKKAVD LLLSAERPVI YSGGGVVLGE ASQELTELAH LLGYPVTNTL
MGLGAYPATD QQFIGMLGMH GTYEANMAMH ESDLIIAIGA RFDDRVTGKL DRFCPHAKII
HIDVDPASIS KTVKVDIPIV GEVKPVLEQM IELIREHKKK PNKKALDDWW KQIAQWQAIQ
CLEYDRSSPL IKPQYVIEQL WEVTRGDAYI TSDVGQHQMW AAQYYKFDKP RHWINSGGLG
TMGFGLPAAI GVKIGHPEAE VACVTGEASI QMCIQELSTA LQYNTPIKIV NLNNRYMGMV
RQWQEFSYES RYSHSYMDTI PDFVKLAEAY GHVGMRIDRP DEVRPALEQA FALKDRTVFL
DIITDRTENV YPMIEAGKAH NDMKLRVAAS ASTDRELA
//
