UniProt: D3PT83

Database: UniProt
Entry: D3PT83_MEIRD

LinkDB:  D3PT83_MEIRD 
Original site:  D3PT83_MEIRD

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (2)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (26)   

Download RDF

ID   D3PT83_MEIRD            Unreviewed;       561 AA.
AC   D3PT83;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Mrub_1909 {ECO:0000313|EMBL:ADD28666.1};
GN   ORFNames=K649_13015 {ECO:0000313|EMBL:AGK05889.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS   ruber).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05889.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:ADD28666.1, ECO:0000313|Proteomes:UP000006655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC   {ECO:0000313|EMBL:ADD28666.1};
RX   PubMed=21304689; DOI=10.4056/sigs.1032748;
RA   Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Meiothermus ruber type strain (21).";
RL   Stand. Genomic Sci. 3:26-36(2010).
RN   [2] {ECO:0000313|EMBL:AGK05889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK05889.1};
RA   Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA   Eichler E., Turner S.W.;
RT   "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT   Sequencing Data.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGK05889.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC   {ECO:0000313|EMBL:AGK05889.1};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-2013) 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}.
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; CP001743; ADD28666.1; -; Genomic_DNA.
DR   EMBL; CP005385; AGK05889.1; -; Genomic_DNA.
DR   RefSeq; WP_013014165.1; NC_021081.1.
DR   AlphaFoldDB; D3PT83; -.
DR   STRING; 504728.K649_13015; -.
DR   KEGG; mrb:Mrub_1909; -.
DR   KEGG; mre:K649_13015; -.
DR   PATRIC; fig|504728.9.peg.2677; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000006655; Chromosome.
DR   Proteomes; UP000013026; 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; 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:ADD28666.1}.
FT   DOMAIN          1..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          190..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          379..527
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   561 AA;  60557 MW;  1EB39FC43D4206B9 CRC64;
     MNGAAAILKA LEMQGVDTIF GHPGGTIMPT YDALYDSPIR HILVRHEQAG VHAATAYARA
     SGRVGVCMAT SGPGALNLVT GLQDALMDST PVVALTGNVP QHLIGTDAFQ EADVVGITQP
     VTKHNFQVRN VNDIPRIIAE AFYIASTGRP GPVLIDFPKD VQQAEFTGSF DVEINLPGYK
     PTYKGHPRQI ERALEALQKA ERPVLMVGGG ALNAAPEIVA LAEKTGMPVI PTLMGLGVFP
     GTHPQCLGMP GMHGSVAANR AIHHADTILA IGLRFDDRVT GKVSRFAPHA HTVIHVDIDP
     AEIGKLVKTT IPVVGDAKWV AAELVKGAKK LHLSKWWAQL EDWKTKYPFA WKPKPHLQSQ
     EVIQAFWEAT KGKAVVTAGV GQHQMFTAQF YKFDAPRSWI NSGGLGTMGV GLPFAIGAAL
     ARPGELVIDF DGDGSFQMTL QELATLKKHN LNVKIVILNN GFLGMVRQWQ DLFHAKRYSE
     VYLADSNPDF AKLAEAYGIR GITLTDKAKL HETVKEVLAH PGPVLLEARV YHEEGVFPMI
     PSGGAAEDMI IENPRETVAG D
//

DBGET integrated database retrieval system