UniProt: A0A0T7RYL1

Database: UniProt
Entry: A0A0T7RYL1_SALET

LinkDB:  A0A0T7RYL1_SALET 
Original site:  A0A0T7RYL1_SALET

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (15)   
   EMBL (15)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (37)   

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ID   A0A0T7RYL1_SALET        Unreviewed;       548 AA.
AC   A0A0T7RYL1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   Name=ilvG {ECO:0000313|EMBL:SUE49563.1};
GN   ORFNames=B7N00_20335 {ECO:0000313|EMBL:EDG5019295.1}, B7N01_17805
GN   {ECO:0000313|EMBL:EDG4996273.1}, B7N35_19545
GN   {ECO:0000313|EMBL:EDG5128216.1}, B7N72_16650
GN   {ECO:0000313|EMBL:EDG5371728.1}, B7N78_20655
GN   {ECO:0000313|EMBL:EDG5282170.1}, B7N80_16080
GN   {ECO:0000313|EMBL:EDG5289893.1}, B7N84_20645
GN   {ECO:0000313|EMBL:EDG5268738.1}, DRU31_19770
GN   {ECO:0000313|EMBL:EBS2454517.1}, E0916_20805
GN   {ECO:0000313|EMBL:ECF1448372.1}, EJV93_21080
GN   {ECO:0000313|EMBL:ECA2723670.1}, EWC73_19380
GN   {ECO:0000313|EMBL:ECE8538342.1}, G0B02_21860
GN   {ECO:0000313|EMBL:HAC6381706.1}, G0D18_24260
GN   {ECO:0000313|EMBL:HAC6683704.1}, G2206_17625
GN   {ECO:0000313|EMBL:HAE0436564.1}, NCTC5754_04598
GN   {ECO:0000313|EMBL:SUE49563.1};
OS   Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE49563.1, ECO:0000313|Proteomes:UP000254190};
RN   [1] {ECO:0000313|EMBL:HAC6381706.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381706.1}, M123
RC   {ECO:0000313|EMBL:HAC6683704.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0436564.1};
RX   PubMed=30286803;
RA   Souvorov A., Agarwala R., Lipman D.J.;
RT   "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL   Genome Biol. 19:153-153(2018).
RN   [2] {ECO:0000313|EMBL:SUE49563.1, ECO:0000313|Proteomes:UP000254190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE49563.1,
RC   ECO:0000313|Proteomes:UP000254190};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:HAC6683704.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381706.1}, M123
RC   {ECO:0000313|EMBL:HAC6683704.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0436564.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ECE8538342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=136768 {ECO:0000313|EMBL:EDG4996273.1}, 138330
RC   {ECO:0000313|EMBL:EDG5289893.1}, 143652
RC   {ECO:0000313|EMBL:EDG5371728.1}, 273631
RC   {ECO:0000313|EMBL:EDG5019295.1}, 330535
RC   {ECO:0000313|EMBL:EDG5268738.1}, 333944
RC   {ECO:0000313|EMBL:EDG5282170.1}, 337042
RC   {ECO:0000313|EMBL:EDG5128216.1}, 387147
RC   {ECO:0000313|EMBL:EBS2454517.1}, 470200
RC   {ECO:0000313|EMBL:ECE8538342.1}, 598023
RC   {ECO:0000313|EMBL:ECA2723670.1}, and 692616
RC   {ECO:0000313|EMBL:ECF1448372.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (FEB-2019) 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; AAGUWJ010000019; EBS2454517.1; -; Genomic_DNA.
DR   EMBL; AAHTVM010000016; ECA2723670.1; -; Genomic_DNA.
DR   EMBL; AAIJHK010000021; ECE8538342.1; -; Genomic_DNA.
DR   EMBL; AAIKGE010000018; ECF1448372.1; -; Genomic_DNA.
DR   EMBL; AAMEJW010000020; EDG4996273.1; -; Genomic_DNA.
DR   EMBL; AAMEJY010000018; EDG5019295.1; -; Genomic_DNA.
DR   EMBL; AAMEKY010000020; EDG5128216.1; -; Genomic_DNA.
DR   EMBL; AAMEMC010000016; EDG5268738.1; -; Genomic_DNA.
DR   EMBL; AAMEMH010000019; EDG5282170.1; -; Genomic_DNA.
DR   EMBL; AAMEML010000018; EDG5289893.1; -; Genomic_DNA.
DR   EMBL; AAMEMP010000019; EDG5371728.1; -; Genomic_DNA.
DR   EMBL; DAAMEZ010000020; HAC6381706.1; -; Genomic_DNA.
DR   EMBL; DAAMHM010000039; HAC6683704.1; -; Genomic_DNA.
DR   EMBL; DAAQQK010000020; HAE0436564.1; -; Genomic_DNA.
DR   EMBL; UGVQ01000002; SUE49563.1; -; Genomic_DNA.
DR   RefSeq; WP_021000939.1; NZ_WFIN01000012.1.
DR   AlphaFoldDB; A0A0T7RYL1; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000254190; Unassembled WGS sequence.
DR   Proteomes; UP000839929; 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:SF142; ACETOLACTATE SYNTHASE; 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:SUE49563.1}.
FT   DOMAIN          1..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          374..522
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   548 AA;  59182 MW;  6A7A807A010B12FB CRC64;
     MNGAQWVVHA LRAQGVKTVF GYPGGAIMPV YDALYDGGVE HLLCRHEQGA AMAAIGYARS
     TGKTGVCIAT SGPGATNLIT GLADALLDSV PVVAITGQVS APFIGTDAFQ EVDVLGLSLA
     CTKHSFLVQS LAELPRIMAE AFEVANAGRP GPVLVDIPKD IQLASGELEP WFTTVDNEAT
     FPQADAEQAR QMLEQAKKPM LYVGGGVGMA QAVPALRKFI AVTQMPVTCT LKGLGAVEAD
     YPYYLGMLGM HGTKAANFAV QECDLLIAVG ARFDDRVTGK LNTFAPNASV IHMDIDPAEM
     NKLRQAHVAL QGDLNSLLPA LQQPLKIDAW RQSCAELRAE HAWRYDHPGE TIYAPLLLKQ
     LSERKPADSV VTTDVGQHQM WSAQHMTYTR PENFITSSGL GTMGFGLPAA VGAQVARPND
     TVICISGDGS FMMNVQELGT VKRKQLPLKI VLLDNQRLGM VRQWQQLFFQ ERYSETTLTD
     NPDFLMLASA FGIPGQHITR KDQVEAALDT MLASEGPYLL HVSIDELENV WPLVPPGASN
     SEMLEKLS
//

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