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Database: UniProt
Entry: A0A0S8DP78_9BACT
LinkDB: A0A0S8DP78_9BACT
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ID   A0A0S8DP78_9BACT        Unreviewed;       557 AA.
AC   A0A0S8DP78;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   20-DEC-2017, entry version 15.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=AMJ78_10535 {ECO:0000313|EMBL:KPK38083.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophica.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK38083.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK38083.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK38083.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK38083.1}.
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DR   EMBL; LJUB01000162; KPK38083.1; -; Genomic_DNA.
DR   PATRIC; fig|1703776.3.peg.1992; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000050824; 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   Gene3D; 3.40.50.1220; -; 1.
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:UP000050824};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050824};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KPK38083.1}.
FT   DOMAIN        5    169       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      194    329       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      384    530       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   557 AA;  60674 MW;  C7DD378DC2EF39C8 CRC64;
     MTTKMTGAQI LVESLKKEGV EVIFGIPGGA VLPLFDVLYD APIRFILTRH EQGAVHAADG
     YTRATGKVGV CIATSGPGAT NLVTGIATAY MDSIPIVAIT GQVKTFLIGN DAFQEADVTG
     VTRPITKHNY LVKDIKDLAC IVKEAFHIAS TGRPGPVLID LPVDVSIAEA EFHYPKELCI
     RGYKPTYNGH PGQIKRAAKV IADSKRPVIY AGGGVILSGG SHLLKELATK IQAPVTTTLL
     GLGSFPETDE LSLGMLGMHG TAYANYAIQN SDLIIAIGAR FDDRVTGKID EFAPHAKIIH
     IDIDPAAISK NVKVDVPIVG DVKNVLTELL KIVHKPATKE WLERVMQWRQ KHPLDYKADE
     KLRPQYVIQQ IYEATKGEAI ISTDVGQNQM WAAQWFTYTR PRSFISSGGL GTMGFGLPAA
     IGAKVGKPDE YVFVLAGDGS IQMNIQELAT AVVNNIHVKV AILNNGYLGM VRQWQELFYK
     RRYSYTRLVN PDFVKIAEAY GAVGIRVAKK EEVRPAIEKA LHTKNVVVMD FIIEEEENVF
     PMVPAGKAID QMIGSMA
//
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