ID C3PJ72_CORA7 Unreviewed; 557 AA.
AC C3PJ72;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alpha-keto-acid decarboxylase {ECO:0000256|ARBA:ARBA00020054};
GN Name=pdc {ECO:0000313|EMBL:ACP31730.1};
GN OrderedLocusNames=cauri_0131 {ECO:0000313|EMBL:ACP31730.1};
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP31730.1, ECO:0000313|Proteomes:UP000002077};
RN [1] {ECO:0000313|EMBL:ACP31730.1, ECO:0000313|Proteomes:UP000002077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1
RC {ECO:0000313|Proteomes:UP000002077};
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001601; ACP31730.1; -; Genomic_DNA.
DR RefSeq; WP_010188354.1; NZ_ACLH01000037.1.
DR AlphaFoldDB; C3PJ72; -.
DR STRING; 548476.cauri_0131; -.
DR GeneID; 31922751; -.
DR KEGG; car:cauri_0131; -.
DR eggNOG; COG3961; Bacteria.
DR HOGENOM; CLU_013748_0_2_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000002077; 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; IPR012000; Thiamin_PyroP_enz_cen_dom.
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; PF00205; TPP_enzyme_M; 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:ACP31730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002077};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..109
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..292
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 557 AA; 61260 MW; 04B4856B53573780 CRC64;
MQTTIGDFIL DRLKAIGITE IIGVPGDFNL SFLEQIEASE GIRFVGACNE LNAAYAADGY
ARQRGVGCLL TTYGVGELSA LNGIAGARAE HVPLVSLAGA PPQYATEFRW NLHHSLADGD
FANMLDSFAP FTEVATRVSP MNVVEEFDRA LHTCLREKRP VHIQIPSDIT HLSIEVPDEP
FSTELAPSDP ERLNAAADYV LEHLAKAKDP IILIDQDTNR HGFTEKFRAI IDKAQLPYSQ
LSSGKAILSE RHPLFIGTYN GAASAPGVQE RIEKSDFLVT TNPRFIEVNS GSFTHNLADA
RVYNFGDQHL NADGEYFVGI NTLELLDVLL DRIPEAGAST SAAFEPEPFE PNPDAPLTQE
RIWPQMLGFI QEDDVVIAEA GTSNIGLGQQ RMPEGVQYIN STIWGSIGFT LPCVLGSQLA
NPKRRHVLFI GDGSFQLTAQ ELSTILRQDL KPIIVLVNND GYTIERYILG MEREYNEIQM
WDYTALPKAF MKDTTMESYV ASTESELAKA LDDIAAHPER GAFLEVRLDA FDAPKGLQAF
GPQTADFDFG PRGPRNA
//
