ID A0AA91Z3U5_WOLPI Unreviewed; 884 AA. AC A0AA91Z3U5; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 02-OCT-2024, entry version 4. DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853}; DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853}; GN ORFNames=BTO27_01675 {ECO:0000313|EMBL:PBQ28258.1}; OS Wolbachia pipientis wAus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=2049495 {ECO:0000313|EMBL:PBQ28258.1, ECO:0000313|Proteomes:UP000218032}; RN [1] {ECO:0000313|EMBL:PBQ28258.1, ECO:0000313|Proteomes:UP000218032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wAus {ECO:0000313|Proteomes:UP000218032}; RA Ward C.M., Baxter S.W.; RT "Wolbachia endosymbiont of Plutella Australiana."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and CC phosphate. {ECO:0000256|ARBA:ARBA00003144}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1; CC Evidence={ECO:0000256|PIRNR:PIRNR000853}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}. 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:PBQ28258.1}. 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; MRWX01000010; PBQ28258.1; -; Genomic_DNA. DR RefSeq; WP_052265055.1; NZ_MRWX01000010.1. DR Proteomes; UP000218032; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016301; F:kinase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.80.30; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1. DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR018274; PEP_util_AS. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR036637; Phosphohistidine_dom_sf. DR InterPro; IPR002192; PPDK_AMP/ATP-bd. DR InterPro; IPR010121; Pyruvate_phosphate_dikinase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR NCBIfam; TIGR01828; pyru_phos_dikin; 1. DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1. DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 2. DR PIRSF; PIRSF000853; PPDK; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000853-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Pyruvate {ECO:0000313|EMBL:PBQ28258.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 72..300 FT /note="Pyruvate phosphate dikinase AMP/ATP-binding" FT /evidence="ECO:0000259|Pfam:PF01326" FT DOMAIN 308..371 FT /note="Pyruvate phosphate dikinase AMP/ATP-binding" FT /evidence="ECO:0000259|Pfam:PF01326" FT DOMAIN 436..517 FT /note="PEP-utilising enzyme mobile" FT /evidence="ECO:0000259|Pfam:PF00391" FT DOMAIN 532..877 FT /note="PEP-utilising enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF02896" FT ACT_SITE 469 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1" FT ACT_SITE 839 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1" FT BINDING 575 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 631 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 753 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3" FT BINDING 753 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 774 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 775 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 776 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" FT BINDING 777 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3" FT BINDING 777 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2" SQ SEQUENCE 884 AA; 97732 MW; 0A60DEFA77E36155 CRC64; MFISENPKKM QEKLIYYFSQ SNCEGNAAMR NLLGGKGANL AEMCNIGIPV PPGFTISTAV CQAYCQDNEL SCDLRNEIKN YMAMLESDIG CKFGDSNNPL LVSIRSGSVN SMPGMLDTVL NVGLNDATVV GLAKKSGERF AYDSYCRFIM MYSSVVLQLD HHLFQDIVDS EQQKSGAKSL ADLNVDVLKK IVNDFKEIVC EKTGKHFPQN VEEQLLNSVN AVFASWKNDR AVSYRRIHNI PENLGTAVNV QAMVFGNLND NSATGVIFTR NPSTGEKKLF GEFLVNAQGE DVVSGVYTPM PIDGEQESTM EKLLPSVYRE LCAVCEKLES HNKDMQDIEF TVQDGKLWIL QTRSGKRTAE AAIRIIVDMV NEGVITKEEG ILRIDPKTFD NFLHPVLDVK IDQEVIGKGL PASPGVASGY VVFSASDAEK AAEQGKKVIL VRSETSPEDI NGMNAASGIV TARGGMTSHA AVVTRGMGKP CICSLNGLYI DKDEKFLSMG DIKVNKGESI TINGGTGEVM LGILPTILPE LSQEFKTIIN WVDEIKTVKV RANADTPKDA KIAKEFGSEG IGLCRTEHMF FASDRIESIQ KLIIADDENE RTNALNKLEE MQKSDFKEIF SIMEGREVTI RLLDPPLHEF LPHNQSIIEK IAKSLNKSVE SVKNKIAQLS EKNPMLGHRG CRLAISHPEI YGMQIRAILS AASELRKEKK IEVKPEIMIP FIMSEKEFIL ICELIKKEAE NFDVNYSIGT MIELPRAALI ADKLAKHAEF FSFGTNDLTQ TTMGLSRDDS VNFLDSYKES NIFKNDPFEV LDVEGVGELI RIAIERGKKT RKEIKLGICG EHGANPQSIE FFIKSGVDYV SCSPYRVLVA KLVAAQLSIS LLGK //