ID A0A0W0ZP64_9GAMM Unreviewed; 559 AA.
AC A0A0W0ZP64;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=Ltuc_2837 {ECO:0000313|EMBL:KTD70826.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD70826.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD70826.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD70826.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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=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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD70826.1}.
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DR EMBL; LNZA01000012; KTD70826.1; -; Genomic_DNA.
DR RefSeq; WP_058522034.1; NZ_LNZA01000012.1.
DR AlphaFoldDB; A0A0W0ZP64; -.
DR STRING; 40335.Ltuc_2837; -.
DR PATRIC; fig|40335.7.peg.3033; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000054693; Unassembled WGS sequence.
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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; 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:SF6; PYRUVATE DECARBOXYLASE C186.09-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.
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:KTD70826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 408..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 559 AA; 60907 MW; 4869BBDEA14F4248 CRC64;
MATVGTYLAQ RLQELGMSDY FAIPGDYNLG LLDELLKNTS LKMINCCNEL NAGYAADGYA
RIKGVSALVV TFSVGGLSAV NAIAGAYAEN LPVIVISGGP NTNSVQDAEI LHHTLATENY
SYVREIFAKI TAHSVFIHRP SDAPMQIDTA IAIALEKKKP VYIEIACNIA GLTVSPPTQR
ALNVKRLSDT SSLTAAIEDA AEKLNAAVKP VLVAGSKSRP CEATAMIEAL SQSCGYALAA
MPDAKGFVSE QHPNYIGIYW GPVSSPGCGE IVESSDLYFF IGPNFNDYTT VGHVCNIQPK
KLIVIADGSV SVAGKVYTDV YMNEFLRGLQ DKLKFNDASL KAYKRIAGSA PLYNEPDDLN
SPLTTRFLFG QIQKLLSSDY GVLAETGDSW FNGMRLNLPE KCPFEIQMQY GSIGWSVGAL
LGMQAALHNK KRVIALIGDG SFQMSAQELS TLIRYGFKPI IFLMNNASYT IEVQIHDGPY
NVINNWRYAD LVDVFNGDQA NVRAFRAPTH QALLDAIKEV KKTDALCFIE VILDKDDCNK
NLLEWGARVA SYNGRPPRM
//