UniProt: F6D6Y1

Database: UniProt
Entry: F6D6Y1_METPW

LinkDB:  F6D6Y1_METPW 
Original site:  F6D6Y1_METPW

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   F6D6Y1_METPW            Unreviewed;       581 AA.
AC   F6D6Y1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
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   OrderedLocusNames=MSWAN_2435 {ECO:0000313|EMBL:AEG19436.1};
OS   Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG19436.1, ECO:0000313|Proteomes:UP000009231};
RN   [1] {ECO:0000313|Proteomes:UP000009231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC   {ECO:0000313|Proteomes:UP000009231};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA   Imachi H., Zinder S., Liu W., Woyke T.;
RT   "Complete sequence of Methanobacterium sp. SWAN-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG19436.1, ECO:0000313|Proteomes:UP000009231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC   {ECO:0000313|Proteomes:UP000009231};
RX   PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA   Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT   "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT   lacus isolated from northern peatlands.";
RL   Int. J. Syst. Evol. Microbiol. 64:1473-1480(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; CP002772; AEG19436.1; -; Genomic_DNA.
DR   RefSeq; WP_013826935.1; NC_015574.1.
DR   AlphaFoldDB; F6D6Y1; -.
DR   STRING; 868131.MSWAN_2435; -.
DR   GeneID; 10669968; -.
DR   KEGG; mew:MSWAN_2435; -.
DR   eggNOG; arCOG01998; Archaea.
DR   HOGENOM; CLU_013748_1_2_2; -.
DR   OrthoDB; 6837at2157; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000009231; 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:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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: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.
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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:AEG19436.1}.
FT   DOMAIN          1..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          190..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          387..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   581 AA;  62546 MW;  D56C4E851B0E800E CRC64;
     MKGGEAIIKS LTDQGVDVVF GYPGGVLLPL YDVIYDSDMK HILVRHEQCA AHAADGYARA
     SGKVGVCIGT SGPGATNLVT GIATAYMDSS PIIAIAGQVS TPLIGNDAFQ EVDTLGMTMP
     ITKHNFQAMH ADEIPGLIKS AFYIANTGRP GPVVLDLPKD VQQEDFDFEK AEPMELPGYK
     PTKKGHPLQV KRATDLILSC KKPVILAGGG VILSGSSSEL LRLSEILGAP VATSLMGKGS
     FPEDHPLSLG MLGMHGKQVA NFTVDDCDCL IAIGCRFSDR TTGSLSKFAK DAKIVHIDVD
     PAEIGKNVDV DVPIVGDAKI VMQSLLQTIS QKKVSAAVNT AAWTKHVSAF RKRSIPRVSF
     DEIPLKPQQV IKEISEAITD DTIVTTDVGQ NQMWMAHYFT SRIPRTFLSS GGLGTMGFGF
     PAAIGAKVAK PETDVVAVCG DGGFLMVCQD LATIKDYDIP IVICVLDNRY LGMVAQWQKL
     FYNNRISHTK LGNVPDFVKL AESFDIKGEK VEKPGELKES LKRALNSGEP TLLDIVIDPD
     EILPMVPPGR GLTEIVGEYK VETEYPGEIP YKSKAREMEG D
//

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