GenomeNet

Database: UniProt
Entry: F6DPI1_DESRL
LinkDB: F6DPI1_DESRL
Original site: F6DPI1_DESRL 
ID   F6DPI1_DESRL            Unreviewed;       553 AA.
AC   F6DPI1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-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=Desru_0357 {ECO:0000313|EMBL:AEG58654.1};
OS   Desulfotomaculum ruminis (strain ATCC 23193 / DSM 2154 / NCIB 8452 /
OS   DL).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG58654.1, ECO:0000313|Proteomes:UP000009234};
RN   [1] {ECO:0000313|Proteomes:UP000009234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC   {ECO:0000313|Proteomes:UP000009234};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Stams A.J.M.,
RA   Plugge C.M., Muyzer G., Kuever J., Parshina S.N., Ivanova A.E.,
RA   Nazina T.N., Brambilla E., Spring S., Klenk H.-P., Woyke T.;
RT   "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL   Submitted (MAY-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002780; AEG58654.1; -; Genomic_DNA.
DR   RefSeq; WP_013840429.1; NC_015589.1.
DR   EnsemblBacteria; AEG58654; AEG58654; Desru_0357.
DR   KEGG; dru:Desru_0357; -.
DR   KO; K01652; -.
DR   OMA; HEANMAI; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; DRUM696281:G1GY6-379-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000009234; 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; 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:UP000009234};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009234};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN        3    169       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      192    327       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      384    529       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   553 AA;  60317 MW;  011AF1A2974CFD78 CRC64;
     MKMSGAQILI DSLKEAGVET IFGYPGGQAL PIYDALYDSD LQHILVRHEQ GAAHAADGYA
     RASGKVGVCL ATSGPGATNL VTGIANAYMD SVPMVAITGQ VPTFLLGRDS FQEVDITGIT
     LPITKHNYIV KDIKDMGRIV KEAFYVASTG RPGPVLIDIP KDISSGEMDY ERNGCLNLPG
     YNPPREARED LVNQALRAIA ESRCPVIYAG GGVISSGAHQ ELKKLSETLL APVTVTLMGL
     GGFPGDHPLS LGMLGMHGSK YANYAVCECD LLIAVGVRFD DRVTGKIESF ASNAKIIHID
     IDPAEMGKNV QVDIPVTGDV KLVLNQLLER LEARIPTAWQ EKIAAWKKEY PFDYDRTGET
     LKPQQIIREI DRQTSGQARI TTEVGQHQMW AAQYYTYTKP RSFISSGGLG TMGYGFPAAI
     GVQVACPEET VFDIAGDGSI QMNIQELATA VNYELPVNVA IMNNGYLGMV RQWQEMLYNR
     RYSQSEMKSP DFVKLAESYG AEGYRITRKE EVTPVLQAAI QSRKPVLMDF VVEPEENVLP
     FVPPGKGLNE MLG
//
DBGET integrated database retrieval system