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   03-AUG-2022, entry version 75.
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; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: Decarboxylates branched-chain and aromatic alpha-keto acids
CC       to aldehydes.
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213; Evidence={ECO:0000250};
CC       Note=Binds 1 metal ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; CP000611; ABQ72591.1; -; Genomic_DNA.
DR   RefSeq; WP_003900222.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U0P1; -.
DR   SMR; A5U0P1; -.
DR   STRING; 419947.MRA_0861; -.
DR   EnsemblBacteria; ABQ72591; ABQ72591; MRA_0861.
DR   KEGG; mra:MRA_0861; -.
DR   eggNOG; COG3961; Bacteria.
DR   HOGENOM; CLU_013748_0_2_11; -.
DR   OMA; EQRYNDI; -.
DR   OrthoDB; 391134at2; -.
DR   Proteomes; UP000001988; Chromosome.
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; 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; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR43452; PTHR43452; 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   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Thiamine pyrophosphate.
FT   CHAIN           1..560
FT                   /note="Alpha-keto-acid decarboxylase"
FT                   /id="PRO_0000333752"
FT   REGION          396..478
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         446
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
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