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Database: UniProt
Entry: N2AM50_9CLOT
LinkDB: N2AM50_9CLOT
Original site: N2AM50_9CLOT 
ID   N2AM50_9CLOT            Unreviewed;       559 AA.
AC   N2AM50;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   20-DEC-2017, entry version 26.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=C824_03063 {ECO:0000313|EMBL:EMZ25549.1};
OS   Clostridium sp. ASF502.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=97139 {ECO:0000313|EMBL:EMZ25549.1, ECO:0000313|Proteomes:UP000012582};
RN   [1] {ECO:0000313|EMBL:EMZ25549.1, ECO:0000313|Proteomes:UP000012582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF502 {ECO:0000313|EMBL:EMZ25549.1,
RC   ECO:0000313|Proteomes:UP000012582};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined
RT   bacterial community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-14(2014).
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:EMZ25549.1}.
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DR   EMBL; AQFU01000051; EMZ25549.1; -; Genomic_DNA.
DR   RefSeq; WP_004080792.1; NZ_KB822467.1.
DR   EnsemblBacteria; EMZ25549; EMZ25549; C824_03063.
DR   PATRIC; fig|97139.3.peg.3323; -.
DR   OrthoDB; POG091H02KO; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000012582; 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:UP000012582};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012582};
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      192    326       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      382    529       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   559 AA;  61032 MW;  C8E95606F598894A CRC64;
     MYLTGADIVI ECLKEQGVDM VFGYPGGAIL NVYDALYQHS DEIKHILTSH EQGAAHAADG
     YARATGKVGV CFATSGPGAT NLVTGIATAY MDSIPIVAIT CNVGVSLLGK DSFQEVDITG
     ITMPITKHNY IVKDVDSLAG TIRKAFQIAR SGRPGPVLID IPKDVTANKA EYIKEEIRPF
     MPDGEQILEE EIDRAVAMIE EAKQPYIFVG GGAVLSDASE ELTEFVNKVD APVTDSLMGK
     GAFPGTDERY TGMLGMHGTK TSNFGVSECD LLIVLGARFS DRVTGNTQTF AKHAKILQFD
     VDPAEMNKNV LITAGVTGDI REALKKVNRK LSRQSHPDWM EKIREYKQQY PMKYHPDGLT
     GPFVVEEIYR QTKGDALIVT EVGQHQMWAA QYYRYSRPRT FLTSGGLGTM GYGLGASLGA
     KMGCPEKTVV NIAGDGCFRM NMNEIATAAR YQIPVIEVVI NNHVLGMVRQ WQNLFYGQRY
     SATVLNDGVD FAKLAEAMGA VGVRVTTQEE FREAFADALK SDQPVLIDCQ IDSDDKVWPM
     VAPGAAISDA FDEDDLKNK
//
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