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Database: UniProt
Entry: F7V5X5_CLOSS
LinkDB: F7V5X5_CLOSS
Original site: F7V5X5_CLOSS 
ID   F7V5X5_CLOSS            Unreviewed;       563 AA.
AC   F7V5X5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   25-APR-2018, entry version 46.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   OrderedLocusNames=CXIVA_21870 {ECO:0000313|EMBL:BAK48154.1};
OS   Clostridium sp. (strain SY8519).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48154.1, ECO:0000313|Proteomes:UP000008937};
RN   [1] {ECO:0000313|Proteomes:UP000008937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX   PubMed=21914882; DOI=10.1128/JB.05637-11;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genomic sequence of the O-desmethylangolensin-producing
RT   bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from
RT   adult human intestine.";
RL   J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK48154.1; -; Genomic_DNA.
DR   RefSeq; WP_013978111.1; NC_015737.1.
DR   STRING; 1042156.CXIVA_21870; -.
DR   EnsemblBacteria; BAK48154; BAK48154; CXIVA_21870.
DR   KEGG; cls:CXIVA_21870; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   KO; K01652; -.
DR   OMA; FRPLCKF; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; CSP1042156:G1H6I-2194-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000008937; 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:UP000008937};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008937};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN        4    170       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      193    327       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      382    529       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   563 AA;  61514 MW;  3F5CB05AFE8BF04B CRC64;
     MLLTGAEIVI ECLKEQGVDT VFGYPGGAIL NIYDELYKHA DEIHHVLTSH EQGASHAADG
     YARSTGRVGV CFATSGPGAT NLVTGIGTAY MDSVPVVAIT CNVGVPLLGK DSFQEVDIAG
     ITMPITKHNF IVKDVNRLAD TIRRAFRIAR SGRPGPVLVD IPKDVTGAKA EFIRRPVEIP
     PRSTERISNE SLHHAVSMIQ SSRKPFIFVG GGAVISEASS ELKEFVEKVQ APVCDSLMGK
     GAFSGTDPLY AGMLGMHGTK ASNLGVSRCD LLIAIGTRFS DRVIGNAKRF AADAQILHID
     VDPAEVNKNI HTDECIIGDV REVLARLNQL LTRQNHDPWI AEVEEYKQKY PMRYSEQGLC
     GPYMMEEIYR QTKGDAIIVA EVGQHQMWAA QYYKYSRPRT YLTSGGLGTM GFGLGAAIGA
     QMANPDKQVV NIAGDGCFRM NFNEILTAVR EQVPLIEVIV NNSVLGMVHQ WQKLFYGKRY
     SNTSFTDDVD FVRVAEALGA RGFRVSTREE FQEAFAAALK ENGPVVLDCR IGSDDNVWPM
     VAPGDSIGNA FDEADYSKKI QNK
//
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