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Database: UniProt
Entry: A0A0W0ZP64_9GAMM
LinkDB: A0A0W0ZP64_9GAMM
Original site: A0A0W0ZP64_9GAMM 
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
//
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