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Database: UniProt
Entry: B2HFC5_MYCMM
LinkDB: B2HFC5_MYCMM
Original site: B2HFC5_MYCMM 
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
//
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