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Database: UniProt
Entry: A5U0P1
LinkDB: A5U0P1
Original site: A5U0P1 
ID   KDC_MYCTA               Reviewed;         560 AA.
AC   A5U0P1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-APR-2014, entry version 43.
DE   RecName: Full=Alpha-keto-acid decarboxylase;
DE            Short=KDC;
DE            EC=4.1.1.-;
GN   Name=kdc; OrderedLocusNames=MRA_0861;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RA   Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y.,
RA   Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.;
RT   "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra,
RT   a non-pathogenic variant closely related to the well-characterized
RT   pathogenic strain H37Rv.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decarboxylates branched-chain and aromatic alpha-keto
CC       acids to aldehydes.
CC   -!- COFACTOR: Binds 1 metal ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
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DR   EMBL; CP000611; ABQ72591.1; -; Genomic_DNA.
DR   RefSeq; YP_001282153.1; NC_009525.1.
DR   ProteinModelPortal; A5U0P1; -.
DR   SMR; A5U0P1; 14-557.
DR   STRING; 419947.MRA_0861; -.
DR   EnsemblBacteria; ABQ72591; ABQ72591; MRA_0861.
DR   GeneID; 5214646; -.
DR   KEGG; mra:MRA_0861; -.
DR   PATRIC; 18141483; VBIMycTub106795_0953.
DR   eggNOG; COG3961; -.
DR   HOGENOM; HOG000061334; -.
DR   KO; K04103; -.
DR   OMA; DYNLEFL; -.
DR   OrthoDB; EOG62ZHQW; -.
DR   ProtClustDB; CLSK790786; -.
DR   BioCyc; MTUB419947:GJ8N-886-MONOMER; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968:SF4; PTHR18968:SF4; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    560       Alpha-keto-acid decarboxylase.
FT                                /FTId=PRO_0000333752.
FT   REGION      396    478       Thiamine pyrophosphate binding (By
FT                                similarity).
FT   METAL       446    446       Magnesium (By similarity).
FT   METAL       473    473       Magnesium (By similarity).
FT   METAL       475    475       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING      61     61       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   560 AA;  59783 MW;  F0430F720D57B7C4 CRC64;
     MTPQKSDACS DPVYTVGDYL LDRLAELGVS EIFGVPGDYN LQFLDHIVAH PTIRWVGSAN
     ELNAGYAADG YGRLRGMSAV VTTFGVGELS VTNAIAGSYA EHVPVVHIVG GPTKDAQGTR
     RALHHSLGDG DFEHFLRISR EITCAQANLM PATAGREIDR VLSEVREQKR PGYILLSSDV
     ARFPTEPPAA PLPRYPGGTS PRALSLFTKA AIELIADHQL TVLADLLVHR LQAVKELEAL
     LAADVVPHAT LMWGKSLLDE SSPNFLGIYA GAASAERVRA AIEGAPVLVT AGVVFTDMVS
     GFFSQRIDPA RTIDIGQYQS SVADQVFAPL EMSAALQALA TILTGRGISS PPVVPPPAEP
     PPAMPARDEP LTQQMVWDRV CSALTPGNVV LADQGTSFYG MADHRLPQGV TFIGQPLWGS
     IGYTLPAAVG AAVAHPDRRT VLLIGDGAAQ LTVQELGTFS REGLSPVIVV VNNDGYTVER
     AIHGETAPYN DIVSWNWTEL PSALGVTNHL AFRAQTYGQL DDALTVAAAR RDRMVLVEVV
     LPRLEIPRLL GQLVGSMAPQ
//
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