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 01-MAY-2013, entry version 40.
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; LEWIGNC; -.
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 GO; GO:0008152; P:metabolic process; IEA:GOC.
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
//
