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Database: UniProt
Entry: A0A0M9GRQ4_9BACI
LinkDB: A0A0M9GRQ4_9BACI
Original site: A0A0M9GRQ4_9BACI 
ID   A0A0M9GRQ4_9BACI        Unreviewed;       571 AA.
AC   A0A0M9GRQ4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-APR-2018, entry version 19.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=AAV98_13045 {ECO:0000313|EMBL:KPB04180.1};
OS   Bacillus sp. CHD6a.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04180.1, ECO:0000313|Proteomes:UP000037908};
RN   [1] {ECO:0000313|EMBL:KPB04180.1, ECO:0000313|Proteomes:UP000037908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHD6a {ECO:0000313|EMBL:KPB04180.1,
RC   ECO:0000313|Proteomes:UP000037908};
RA   Lin W., Liu Y., Zheng Q., Jiao N.;
RT   "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT   hydrothermal environment.";
RL   Submitted (APR-2015) 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   -!- 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:KPB04180.1}.
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DR   EMBL; LBMD01000016; KPB04180.1; -; Genomic_DNA.
DR   RefSeq; WP_060666009.1; NZ_LBMD01000016.1.
DR   EnsemblBacteria; KPB04180; KPB04180; AAV98_13045.
DR   PATRIC; fig|1643452.3.peg.1468; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000037908; 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   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:UP000037908};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037908};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KPB04180.1}.
FT   DOMAIN       17    177       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      205    340       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      397    545       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   571 AA;  62049 MW;  326B6B0B69F921A1 CRC64;
     MSTVEKSGTK VAQKLLTGSR MIVEALKEEK VEVIFGYPGG AVLNIYDALY DGGIPHLLTR
     HEQGAIHAAE GYARVTGKPG VVIATSGPGA TNIVTGLADA MIDSLPLVVI TGQVNSQVLG
     SDAFQEAPIL GISMPITKHN FQVQDVKDLP RIFKEAFHIA STGRPGPVLI DIPKDITATS
     GIYDYSKEVH LPGYKLQIEP DPQAVKKVAQ ALKKAEKPVI LAGAGVLHSK ATDELKELVA
     KTTIPVANTL LGLGSFPADH PLFLGMAGMH GTYTANMALY EADLIINIGA RFDDRLTGNL
     QEFAKFAKVV HFDIDPSEIG KNVKTDYPVI GDAAKSLQLL IKELTETANT SSWLEQLLQS
     KEDYPLWYVE DGETFKPQKL VELVHELTKG EAIVTTDVGQ HQMWAAQFHG FQKPDRWVTS
     GGLGTMGFGL PAAIGAQVAE RPSTVVAVLG DAGFQMTLQE LAVLKEYKLP VKVVLVNNQS
     MGMVRQWQQL FYKERYSESL LPNQPDYVKL SDAFGIKAAV VQSEEEFRVA FAEALATDEP
     YLLDCRVTPM ENVYPMIAPG KGIQQMEGVK P
//
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