ID Q5ZUA2_LEGPH Unreviewed; 393 AA. AC Q5ZUA2; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 96. DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase I {ECO:0000313|EMBL:AAU27975.1}; GN OrderedLocusNames=lpg1905 {ECO:0000313|EMBL:AAU27975.1}; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC OS 33152 / DSM 7513). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU27975.1, ECO:0000313|Proteomes:UP000000609}; RN [1] {ECO:0000313|EMBL:AAU27975.1, ECO:0000313|Proteomes:UP000000609} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513 RC {ECO:0000313|Proteomes:UP000000609}; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A., RA Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., RA Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella pneumophila."; RL Science 305:1966-1968(2004). RN [2] {ECO:0007829|PDB:3AAP, ECO:0007829|PDB:3AAQ} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 41-393 IN COMPLEX WITH ATP RP ANALOG, AND DISULFIDE BONDS. RX PubMed=20159467; DOI=10.1016/j.str.2009.11.014; RA Vivian J.P., Riedmaier P., Ge H., Le Nours J., Sansom F.M., Wilce M.C., RA Byres E., Dias M., Schmidberger J.W., Cowan P.J., d'Apice A.J., RA Hartland E.L., Rossjohn J., Beddoe T.; RT "Crystal structure of a Legionella pneumophila ecto -triphosphate RT diphosphohydrolase, a structural and functional homolog of the eukaryotic RT NTPDases."; RL Structure 18:228-238(2010). RN [3] {ECO:0007829|PDB:4BR4, ECO:0007829|PDB:4BR7} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-393 IN COMPLEX WITH AMP; ATP RP ANALOG AND MAGNESIUM, AND DISULFIDE BONDS. RX PubMed=23830739; DOI=10.1016/j.str.2013.05.016; RA Zebisch M., Krauss M., Schafer P., Lauble P., Strater N.; RT "Crystallographic snapshots along the reaction pathway of nucleoside RT triphosphate diphosphohydrolases."; RL Structure 21:1460-1475(2013). RN [4] {ECO:0007829|PDB:4BVO, ECO:0007829|PDB:4BVP} RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 35-393, AND DISULFIDE BONDS. RX PubMed=24699658; DOI=10.1107/S1399004714001916; RA Zebisch M., Krauss M., Schafer P., Strater N.; RT "Structures of Legionella pneumophila NTPDase1 in complex with RT polyoxometallates."; RL Acta Crystallogr. D 70:1147-1154(2014). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017354; AAU27975.1; -; Genomic_DNA. DR RefSeq; YP_095922.1; NC_002942.5. DR PDB; 3AAP; X-ray; 1.60 A; A=41-393. DR PDB; 3AAQ; X-ray; 2.00 A; A=41-393. DR PDB; 3AAR; X-ray; 1.65 A; A=41-393. DR PDB; 4BR4; X-ray; 1.45 A; A=37-393. DR PDB; 4BR7; X-ray; 1.80 A; A=37-393. DR PDB; 4BR9; X-ray; 1.40 A; A/B=35-393. DR PDB; 4BRA; X-ray; 1.60 A; A/B=35-393. DR PDB; 4BRC; X-ray; 1.30 A; A/B=35-393. DR PDB; 4BRD; X-ray; 1.50 A; A/B=35-393. DR PDB; 4BRE; X-ray; 1.60 A; A/B=35-393. DR PDB; 4BRF; X-ray; 1.60 A; A/B=35-393. DR PDB; 4BRG; X-ray; 1.45 A; A/B=35-393. DR PDB; 4BRH; X-ray; 1.69 A; A/B=35-393. DR PDB; 4BRI; X-ray; 1.75 A; A/B=35-393. DR PDB; 4BRK; X-ray; 1.50 A; A/B=35-393. DR PDB; 4BRL; X-ray; 1.60 A; A/B=35-393. DR PDB; 4BRM; X-ray; 2.02 A; A/B=35-393. DR PDB; 4BRN; X-ray; 1.69 A; A/B=35-393. DR PDB; 4BRO; X-ray; 1.99 A; A/B=35-393. DR PDB; 4BRP; X-ray; 2.50 A; A/B/C/D=35-393. DR PDB; 4BRQ; X-ray; 1.45 A; A/B=35-393. DR PDB; 4BVO; X-ray; 1.70 A; A=37-393. DR PDB; 4BVP; X-ray; 1.49 A; A/B=35-393. DR PDBsum; 3AAP; -. DR PDBsum; 3AAQ; -. DR PDBsum; 3AAR; -. DR PDBsum; 4BR4; -. DR PDBsum; 4BR7; -. DR PDBsum; 4BR9; -. DR PDBsum; 4BRA; -. DR PDBsum; 4BRC; -. DR PDBsum; 4BRD; -. DR PDBsum; 4BRE; -. DR PDBsum; 4BRF; -. DR PDBsum; 4BRG; -. DR PDBsum; 4BRH; -. DR PDBsum; 4BRI; -. DR PDBsum; 4BRK; -. DR PDBsum; 4BRL; -. DR PDBsum; 4BRM; -. DR PDBsum; 4BRN; -. DR PDBsum; 4BRO; -. DR PDBsum; 4BRP; -. DR PDBsum; 4BRQ; -. DR PDBsum; 4BVO; -. DR PDBsum; 4BVP; -. DR AlphaFoldDB; Q5ZUA2; -. DR SMR; Q5ZUA2; -. DR STRING; 272624.lpg1905; -. DR PaxDb; 272624-lpg1905; -. DR KEGG; lpn:lpg1905; -. DR PATRIC; fig|272624.6.peg.1990; -. DR eggNOG; COG5371; Bacteria. DR HOGENOM; CLU_727216_0_0_6; -. DR OrthoDB; 5640341at2; -. DR EvolutionaryTrace; Q5ZUA2; -. DR Proteomes; UP000000609; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1. DR InterPro; IPR000407; GDA1_CD39_NTPase. DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1. DR Pfam; PF01150; GDA1_CD39; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3AAP, ECO:0007829|PDB:3AAQ}; KW Hydrolase {ECO:0000313|EMBL:AAU27975.1}; KW Metal-binding {ECO:0007829|PDB:4BR7, ECO:0007829|PDB:4BRD}; KW Nucleotide-binding {ECO:0007829|PDB:4BRF, ECO:0007829|PDB:4BRN}; KW Reference proteome {ECO:0000313|Proteomes:UP000000609}. FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 52 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 53 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 53 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 56 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 56 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRQ" FT BINDING 80 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 80 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRQ" FT BINDING 82 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 140 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 143 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 189 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 274 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 302 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:4BVP" FT BINDING 346 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4BRN" FT BINDING 346 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4BRF" FT BINDING 346 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRQ" FT BINDING 350 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4BRQ" FT DISULFID 39..44 FT /evidence="ECO:0007829|PDB:4BR4, ECO:0007829|PDB:4BR7" FT DISULFID 244..264 FT /evidence="ECO:0007829|PDB:3AAP, ECO:0007829|PDB:3AAQ" FT DISULFID 330..351 FT /evidence="ECO:0007829|PDB:3AAP, ECO:0007829|PDB:3AAQ" SQ SEQUENCE 393 AA; 44531 MW; 71635FBA5EA6E876 CRC64; MYHSKTSILA LYQLMFRVLI FLSCLVILTP NTIADTNPCE KHSCIAVIDA GSTGSRLHIY SYDTDDTNTP IHIEEIWNKK IKPGFASIQP NSVTIDAYLT MLLADAPIHN IPVYFYATAG MRLLPQSQQK KYYDELEYWF RQQSQWQLAE AKTITGNDEA LFDWLAVNYK LDTLKSVQNK SVGVMDMGGA SVQIVFPMPK NAEISKHNQV ELNIYGQNIN LYVHSFLGLG QTEMSHQFLN SPSCFANDYP LPDGESGQGN APSCKEEVTS LMNSVHKVNQ QIQPLLALNP VNEWYSIGGI SNLASSQLFH FENSELTNQS LLQQGDNQIC HQQWDILNGQ YPDDEYLYQY CLLSSYYYAL MVDGYGINPN QTIHYIPPEQ NLDWTIGVVL HRA //