ID   KDC_MYCS2               Reviewed;         555 AA.
AC   A0R480; I7FT25;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alpha-keto-acid decarboxylase;
DE            Short=KDC;
DE            EC=4.1.1.-;
GN   Name=kdc; Synonyms=pdc; OrderedLocusNames=MSMEG_5735, MSMEI_5583;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK72950.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42023.1; -; Genomic_DNA.
DR   RefSeq; WP_011730751.1; NZ_SIJM01000007.1.
DR   RefSeq; YP_889968.1; NC_008596.1.
DR   AlphaFoldDB; A0R480; -.
DR   SMR; A0R480; -.
DR   STRING; 246196.MSMEI_5583; -.
DR   EnsemblBacteria; ABK72950; ABK72950; MSMEG_5735.
DR   EnsemblBacteria; AFP42023; AFP42023; MSMEI_5583.
DR   GeneID; 66737029; -.
DR   KEGG; msg:MSMEI_5583; -.
DR   KEGG; msm:MSMEG_5735; -.
DR   PATRIC; fig|246196.19.peg.5587; -.
DR   eggNOG; COG3961; Bacteria.
DR   OMA; EQRYNDI; -.
DR   OrthoDB; 391134at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..555
FT                   /note="Alpha-keto-acid decarboxylase"
FT                   /id="PRO_0000333750"
FT   REGION          388..470
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  58902 MW;  D734A5CD806222AE CRC64;
     MTDDGYTVGD YLLDRLAELG VTEVFGVPGD YQLEFLDHVV AHPRITWVGG ANELNAGYAA
     DGYGRLRGMA ALVTTFGVGE LSAANAIAGS YAEHVPVVHI VGAPSKDSQA ARRIVHHTLG
     DGDFEHFLRM SREITCAQAN LVPATATREI DRVLSEVHEQ KRPGYLLIAT DVARFPTEPP
     TAPLPRHSGG TSPRALSLFT EAATQLIGEH RLTVLADFLV HRMGCVEALN KLLTADTVPH
     ATLMWGKSLV DESSPNFLGI YAGAASEGSV REVIEDAPVL VTAGVLFTDM VSGFFSQRID
     PARTIDIGVN QSVVAGQVFA PLDMAAALDA LASILAERGI ESPALPPAPA PQRPAAPPRD
     AVLTQEALWD RLAEALTPGN VVLADQGTSF YGLAGHRLAS GVTFIGQPLW ASIGYTLPAA
     LGAGLADRDR RTVLLIGDGA AQLTVQELGA FGREGLTPVV VVVNNNGYTV ERAIHGVTAR
     YNDITAWRWT ELPAALGVPD ALTFRCATYG ELDDALTVAA ETQDRMVFVE VMLERMDIPP
     LLGELAQSAS AANAK