ID B2HFC5_MYCMM Unreviewed; 566 AA.
AC B2HFC5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN Name=pdc {ECO:0000313|EMBL:ACC43087.1};
GN OrderedLocusNames=MMAR_4683 {ECO:0000313|EMBL:ACC43087.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43087.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC43087.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- FUNCTION: Decarboxylates branched-chain and aromatic alpha-keto acids
CC to aldehydes. {ECO:0000256|ARBA:ARBA00002938}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000256|ARBA:ARBA00001920};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP000854; ACC43087.1; -; Genomic_DNA.
DR RefSeq; WP_012396223.1; NC_010612.1.
DR AlphaFoldDB; B2HFC5; -.
DR STRING; 216594.MMAR_4683; -.
DR KEGG; mmi:MMAR_4683; -.
DR eggNOG; COG3961; Bacteria.
DR HOGENOM; CLU_013748_0_2_11; -.
DR OMA; EQRYNDI; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000001190; 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 CDD; cd02005; TPP_PDC_IPDC; 1.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:ACC43087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 15..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 403..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 566 AA; 60161 MW; 5454FBE2BD1AF84A CRC64;
MTLLENDAAT DPVYTVGDYL LDRLAELGVS EIFGVPGDYN LEFLDHIVAH PTIRWVGSAN
ELNAGYAADG YGRLRGMSAV VTTFGVGELS ATNAIAGSYA EHVPVVHIVG GPSKDAQGAR
RALHHSLGDG DFEHFFRISR EITCAQANLM PATACREIDR VLCEVREQKR PGYLLLSTDV
ARFPTEPPGA PLPPLAGGTS PRALSLFTRA AADLIGDHQL TVLADLLVHR LQAVKELEAV
LSADVVPHAT LMWGKSLLDE SSANFLGIYA GAASAEPVRT AIECAPVLVT AGVVFTDMVS
GFFSQRIDPA RTIDIGQYQS SVADQVFAPL EMGAALQAVA TILTKRGINS PPVAVPPAEP
GPPTPGRDEP LNQEMLWNRL CEALTPGNVV LADQGTSFYG MADHRLPQGV TFIGQPLWGS
IGYTLPAALG AAVAHPDRRT VLLIGDGAAQ LTVQELGIFS REGLSPVIVV VNNDGYTVER
AIHGETATYN DIVSWRWTDV PGALGVTNHL AMRAENYGEL DDALTAAAEQ QDRMVVVEAV
LPRLDVPPLL DELVGSLSPP ECGGRS
//