ID   KDC_MYCLE               Reviewed;         569 AA.
AC   Q9CBD6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Alpha-keto-acid decarboxylase;
DE            Short=KDC;
DE            EC=4.1.1.-;
GN   Name=kdc; OrderedLocusNames=ML2167;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583924; CAC31122.1; -; Genomic_DNA.
DR   PIR; B87180; B87180.
DR   RefSeq; NP_302424.1; NC_002677.1.
DR   RefSeq; WP_010908744.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBD6; -.
DR   SMR; Q9CBD6; -.
DR   EnsemblBacteria; CAC31122; CAC31122; CAC31122.
DR   KEGG; mle:ML2167; -.
DR   PATRIC; fig|272631.5.peg.4107; -.
DR   Leproma; ML2167; -.
DR   eggNOG; COG3961; Bacteria.
DR   HOGENOM; CLU_013748_0_2_11; -.
DR   OMA; EQRYNDI; -.
DR   Proteomes; UP000000806; 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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..569
FT                   /note="Alpha-keto-acid decarboxylase"
FT                   /id="PRO_0000333748"
FT   REGION          392..474
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  61146 MW;  5F791EC735254165 CRC64;
     MTAPKIEAVY TVGAYLLDRL AELGVTEIFG VPGDYTLEFL DHIVAHPTIR WVGNANELNA
     GYAADGYGRL RGISALVTTF GVGELSAANA IAGSYAEHVP VVHIVGAPPK DAQSTHRALH
     HSLGDGDFEH FIRISSEITC SQANLTTATA CKEIDRVLSE VRKHKRPGYI LLSTDVARFP
     TEPPAAPLPG HTDGTSPRAL SLFIDAATKL IADKRMTVLA DLLVHRLQVV KELETLLTAD
     VVPYATLMWG KSLLDESSPN FLGIYAGAAS TEAVRAAIEQ APVLVTAGVV FTDMVSGFFS
     QRIDPARTID VGQYQSSVAD KVFTPLEMGD ALEALASILV RRGVSSPPVE LPPGNPTADT
     PSPTQRLTQQ ILWDRLCAAL TPGNVVLADQ GTAFYGMVEH RLPRGVTFIG QPLWGSIGYT
     LPAALGAGLA HRNRRTVLLL GDGAAQLTIQ ELGSFYREGL SPVIVVVNND GYTIERAIHG
     ATAPYNNIAR WRWTDIPGAL GVANHSSFRA ETYGELDEAF AVAAELKDQM VFVEVIVPKL
     DLPSLLTALT RPAQDSNRIF QLPNPGWDN