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Database: UniProt
Entry: A0A0J5MCK9_PLUGE
LinkDB: A0A0J5MCK9_PLUGE
Original site: A0A0J5MCK9_PLUGE 
ID   A0A0J5MCK9_PLUGE        Unreviewed;       548 AA.
AC   A0A0J5MCK9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-APR-2018, entry version 22.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=ABW06_19730 {ECO:0000313|EMBL:KMK11708.1}, AZ034_000884
GN   {ECO:0000313|EMBL:OUF46398.1};
OS   Pluralibacter gergoviae (Enterobacter gergoviae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK11708.1, ECO:0000313|Proteomes:UP000036196};
RN   [1] {ECO:0000313|EMBL:KMK11708.1, ECO:0000313|Proteomes:UP000036196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS81F13 {ECO:0000313|EMBL:KMK11708.1,
RC   ECO:0000313|Proteomes:UP000036196};
RA   Greninger A.L., Miller S.;
RT   "Genome sequences of Pluralibacter gergoviae.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OUF46398.1, ECO:0000313|Proteomes:UP000195081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGH173 {ECO:0000313|EMBL:OUF46398.1};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Cerqueira G., Kirby J., Ferraro M., Onderdonk A., Delaney M.,
RA   Kim D., Gussin G., Young S., Abouelleil A., Cao P., Chapman S.,
RA   Cusick C., Shea T., Neafsey D., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterobacter gergoviae MGH173.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {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.
CC       {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|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMK11708.1}.
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DR   EMBL; LDZF01000025; KMK11708.1; -; Genomic_DNA.
DR   EMBL; NGRT01000001; OUF46398.1; -; Genomic_DNA.
DR   RefSeq; WP_048275886.1; NZ_NGRU01000002.1.
DR   EnsemblBacteria; KMK11708; KMK11708; ABW06_19730.
DR   PATRIC; fig|61647.15.peg.2506; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000036196; Unassembled WGS sequence.
DR   Proteomes; UP000195081; 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   InterPro; IPR012846; Acetolactate_synth_lsu.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036196,
KW   ECO:0000313|Proteomes:UP000195081};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036196};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KMK11708.1}.
FT   DOMAIN        1    164       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      186    321       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      374    522       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   548 AA;  58967 MW;  078EDA27276C170D CRC64;
     MNGAQWVVHA LRAQGVDTVF GYPGGAIMPI YDALYDGGVE HLLCRHEQGA AMAAIGYARA
     TGKTGVCMAT SGPGATNLIT GLADALLDSV PVVAITGQVA SPFIGTDAFQ EVDVLGLSLA
     CTKHSFLVQS SEELPRILAE AFEVANSGRP GPVLVDIPKD IQVASASFEP WFSTVSADEA
     LPQAEIAQAR QMIAGAQKPV LYVGGGVGMA QAVPALREFV SVTQMPVTCT LKGLGAVAAE
     YPYYLAMLGM HGTKAANLAV QQCDLLIAVG ARFDDRVTGK LNTFAPHAKV IHLDIDPAEL
     NKLRQAHVGL QGDLNALLPA LQQPLEIDPW RQYAADLRRE HAWRYDHPGD AIYAPLLLRQ
     LSERKPADAV VTTDVGQHQM WSAQHMDYTR PENFITSSGL GTMGFGLPAA VGAQVARPDD
     TVICISGDGS FMMNVQELGT VKRKQLPLKI VLLDNQRLGM VRQWQQLFFE ERYSETTLTD
     NPDFLTLASA FGIPGQHITR KDQVEAALDA MLNSKGPYLL HVSIDELENV WPLVPPGASN
     AEMLEKLS
//
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