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Database: UniProt
Entry: F4GNV5_PUSST
LinkDB: F4GNV5_PUSST
Original site: F4GNV5_PUSST 
ID   F4GNV5_PUSST            Unreviewed;       573 AA.
AC   F4GNV5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-APR-2018, entry version 44.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   OrderedLocusNames=PT7_1894 {ECO:0000313|EMBL:AEC20434.1};
OS   Pusillimonas sp. (strain T7-7).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC20434.1, ECO:0000313|Proteomes:UP000008737};
RN   [1] {ECO:0000313|EMBL:AEC20434.1, ECO:0000313|Proteomes:UP000008737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T7-7 {ECO:0000313|EMBL:AEC20434.1,
RC   ECO:0000313|Proteomes:UP000008737};
RX   PubMed=21622753; DOI=10.1128/JB.05242-11;
RA   Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT   "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant
RT   diesel oil-degrading bacterium isolated from the Bohai Sea in China.";
RL   J. Bacteriol. 193:4021-4022(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T7-7;
RA   Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT   "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-
RT   7, a novel species isolated from the Bohai Sea, China.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002663; AEC20434.1; -; Genomic_DNA.
DR   RefSeq; WP_013742970.1; NC_015458.1.
DR   STRING; 1007105.PT7_1894; -.
DR   EnsemblBacteria; AEC20434; AEC20434; PT7_1894.
DR   KEGG; put:PT7_1894; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   KO; K01652; -.
DR   OMA; QGMVRQW; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; PSP1007105:G1GWE-1860-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000008737; 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   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; 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.
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:UP000008737};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008737};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN        4    168       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      194    329       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      395    544       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   573 AA;  63321 MW;  ACBFF819BCADFD37 CRC64;
     MELNGADIVV RCLAEQGVDH VFGYPGGAVL YIYDAIYKQD NFKHILVRHE QAAVHAADAY
     SRSSDKIGVA LVTSGPGLTN AVTGIATAYM DSIPMVIISG QVPTAAIGED AFQECDTVGI
     TRPCVKHNFL VRDVKDLAET MRRAFFIAKT GRPGPVLVDI PKDITVATCK FTPKRGEVKM
     RSYAPVVKGH QGQIKKAVQM LLTAERPMIY SGGGVVLSDA SAELRELVEL TGAPCTNTLM
     GLGAFPADDD KFVGMPGMHG TYEANMAMQN CDVLIAVGAR FDDRVIGNTK HFSQTPRKIV
     HIDIDPSSIS KRVRVDVPIV GNVKDVLQEM NSLYAQATVD TPVNKDALAK WWQQINTWRG
     KQCLVYENSD TLIKPQFVVE KLWEVTGGNA FVTSDVGQHQ MWAAQYYRFR QPRRWINSGG
     LGTMGVGLPY AMGVQMANPD SDIAVITGEA SIQMNIQELS TCSQYRLTPK VLCLNNRYLG
     MVRQWQQIDY GSRYSESYVD ALPDFVKLVE SYGHVGMRIE KPADVEPAIR EAFVKYKDRL
     VFLDFITDQT ENVWPMVKAG RGLTEMLLGS EDL
//
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