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Database: UniProt
Entry: I0RD80_MYCXE
LinkDB: I0RD80_MYCXE
Original site: I0RD80_MYCXE 
ID   I0RD80_MYCXE            Unreviewed;       514 AA.
AC   I0RD80;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN   ORFNames=MXEN_20625 {ECO:0000313|EMBL:EID09083.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID09083.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID09083.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID09083.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EID09083.1}.
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DR   EMBL; AJFI01000109; EID09083.1; -; Genomic_DNA.
DR   RefSeq; WP_003923155.1; NZ_AJFI01000109.1.
DR   AlphaFoldDB; I0RD80; -.
DR   PATRIC; fig|1150591.3.peg.4148; -.
DR   OrthoDB; 2443624at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000003584; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003584}.
FT   DOMAIN          1..108
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          369..506
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   514 AA;  52575 MW;  C9DE90EBB909825A CRC64;
     MNGAHALINT LVDGGVEVCF ANPGTSEMHF VAALDSVPRM RGVLTLFEGV ATGAADGYAR
     IAGRPAAVLV HLGPGLANGL ANLHNARRAR VPMVVVVGDH ATYHKKYDAP LESDIDALAA
     SVSGWVRRSR STGELAADAA EAIATSQANQ HISTLILPAD VSWSDGATTA KAVSARRTPV
     VDVARAATVL RSGEPTVILV GGDATRESGL TAAARIATIT GARWYCETFP TRVQRGAGLP
     VVERLAYFAE AVAAQLDGAK HLVLAGAKSP VSFFAYPGKP SNLVPEGCEV HHLAGGVGAA
     DALVALAEEV APGIAAPLAA PSRPVLPTGA LTAASAADVV GALMPENVIV VDESNTSGLL
     LAQATAGAPA HDWLTLTGGA IGYGIPAATG AAIAAPDRPV LCLESDGSAM YTLSGLWTQA
     RENLDVTTVV YNNGAYDILR LELQRVGVEN NPGPKARGLL DLTRPAIDFV KLAEGMGVPA
     RRVTTAEEFA DALQAGFAAP GPHLIEAVVP SMLG
//
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