UniProt: D3S0Q3

Database: UniProt
Entry: D3S0Q3_FERPA

LinkDB:  D3S0Q3_FERPA 
Original site:  D3S0Q3_FERPA

All links

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)   

Download RDF

ID   D3S0Q3_FERPA            Unreviewed;       554 AA.
AC   D3S0Q3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=Ferp_2163 {ECO:0000313|EMBL:ADC66294.1};
OS   Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Ferroglobus.
OX   NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC66294.1, ECO:0000313|Proteomes:UP000002613};
RN   [1] {ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA   Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT   "Complete sequence of Ferroglobus placidus DSM 10642.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC66294.1, ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX   PubMed=22180810; DOI=10.4056/sigs.2225018;
RA   Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA   Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA   Lovley D., Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL   Stand. Genomic Sci. 5:50-60(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001899; ADC66294.1; -; Genomic_DNA.
DR   RefSeq; WP_012966632.1; NC_013849.1.
DR   AlphaFoldDB; D3S0Q3; -.
DR   STRING; 589924.Ferp_2163; -.
DR   PaxDb; 589924-Ferp_2163; -.
DR   GeneID; 8779701; -.
DR   KEGG; fpl:Ferp_2163; -.
DR   eggNOG; arCOG01998; Archaea.
DR   HOGENOM; CLU_013748_1_2_2; -.
DR   OrthoDB; 6837at2157; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002613; 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   Reference proteome {ECO:0000313|Proteomes:UP000002613};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          1..115
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          380..528
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   554 AA;  60997 MW;  C79D07A80D70D7DB CRC64;
     MRAADAIVKA LEKEGVKHIF GIPGGAIIEV YDALFDSEIV HILTRHEQAA VHAADGYARA
     TGRVGVAFAT SGPGATNTVT GIATAYMDSS PVVVMTGQVP RSLIGNDAFQ EADITGITMP
     ITKHNYLVTD EKELLRIIKE AFYIARTGRP GPVLIDLPKD VTIADIEFDY PEKVDLPGYK
     PKYAGHPRQI KRAAELIMKA ERPIILAGGG VILSNASEEL VKLAETIPAF VVTSLMGKGA
     IPETHPLSLG FIGMHGAKYA NYAVQESDLI IAVGVRFSDR TTGKVSSFAP NAKIIHIDID
     PAEIGKNVRV DVPIVGDAKL VLRELIKHIQ YKRRKEWEDK VNEWRRKYPL RYKRDGKLKP
     QYVIEKLYEL APDAIVTTEV GQNQMWAAQY FKVKYPRQFI TSGGLGTMGF GFPAAIGVKT
     AFPDKTVVDI AGDGSFLMNI QELATCVDYG IDVKVFILNN AFLGMVRQWQ QLFYDERYSQ
     TCLLCKEMSF EKIAEGFGAV GMTVERESEV EDAIKEALSI DAPVVVDFRV DRLENVYPMV
     PAGAALNEII DEEV
//

DBGET integrated database retrieval system