ID   KDC_MYCPA               Reviewed;         563 AA.
AC   Q742Q2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Alpha-keto-acid decarboxylase;
DE            Short=KDC;
DE            EC=4.1.1.-;
GN   Name=kdc; OrderedLocusNames=MAP_0783c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03100.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q742Q2; -.
DR   SMR; Q742Q2; -.
DR   STRING; 262316.MAP_0783c; -.
DR   EnsemblBacteria; AAS03100; AAS03100; MAP_0783c.
DR   KEGG; mpa:MAP_0783c; -.
DR   eggNOG; COG3961; Bacteria.
DR   HOGENOM; CLU_013748_0_2_11; -.
DR   OMA; EQRYNDI; -.
DR   Proteomes; UP000000580; 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; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..563
FT                   /note="Alpha-keto-acid decarboxylase"
FT                   /id="PRO_0000333749"
FT   REGION          347..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..476
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        351..367
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
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"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  60417 MW;  6CAD667541FAD37D CRC64;
     MPVTDAATEP AYTVGDYLLD RLAELGVSEI FGVPGDYNLE FLDHIVAHPR LRWVGNANEL
     NAGYAADGYG RLRGMSALVT TFGVGELSAA NAVAGSYAEQ VPVVHIVGGP SKDAQGTRRA
     LHHSLGDGDF EHFFRVSREI TCAQANLMPA TARREIDRVL SEVREQKRPG YILLSTDVAR
     FPTEPPEAAL PRYTGGTSPR ALAMFTEAAA ALIGEHRITV LADLLVHRLQ AIKELEALLA
     ADVVPHATLM WGKSLLDESS PNFLGIYAGS ASAPAVRTAI EEAPVLVTAG VVFTDMVSGF
     FSQRIDPART IDVGQYQSSV AGEVFAPLEM GEALQALTAI LTRRGVSSPP VASPPAEPLP
     PPPPREQPLT QKMVWDRVCT ALTPGNVVLA DQGTSFYGMA DHRLPQGVTF IGQPLWGSIG
     YTLPAALGAA VAHPDRRTVL LIGDGAAQLT VQELGTFARE GLSPVIVVVN NDGYTVERAI
     HGETAPYNDI VGWKWTEVPN ALGVTEHLAF RVQTYGELDD ALTAAARHQD RMVLVEVVLP
     RLEIPRLLVE LVRPTSPDGS PRR