ID A0A369SY43_9ARCH Unreviewed; 548 AA. AC A0A369SY43; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 22-FEB-2023, entry version 13. DE RecName: Full=Pyruvate, water dikinase {ECO:0000256|Google:ProtNLM}; GN ORFNames=BA065_03135 {ECO:0000313|EMBL:RDD52165.1}; OS Nanoarchaeota archaeon NZ13-N. OC Archaea; Nanoarchaeota. OX NCBI_TaxID=1852704 {ECO:0000313|EMBL:RDD52165.1, ECO:0000313|Proteomes:UP000253820}; RN [1] {ECO:0000313|EMBL:RDD52165.1, ECO:0000313|Proteomes:UP000253820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NZ13-N {ECO:0000313|EMBL:RDD52165.1}; RA Kelley J.F., Reysenbach A.-L.; RT "Nanoarchaeota genome from a New Zealand hot spring."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. 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:RDD52165.1}. 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; MAIT01000039; RDD52165.1; -; Genomic_DNA. DR AlphaFoldDB; A0A369SY43; -. DR EnsemblBacteria; RDD52165; RDD52165; BA065_03135. DR Proteomes; UP000253820; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:InterPro. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR036637; Phosphohistidine_dom_sf. DR InterPro; IPR002192; PPDK_AMP/ATP-bd. DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1. DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF01326; PPDK_N; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}. FT DOMAIN 53..110 FT /note="Pyruvate phosphate dikinase AMP/ATP-binding" FT /evidence="ECO:0000259|Pfam:PF01326" FT DOMAIN 260..326 FT /note="PEP-utilising enzyme mobile" FT /evidence="ECO:0000259|Pfam:PF00391" FT COILED 426..453 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 548 AA; 63891 MW; EE650A8E5F4013C0 CRC64; MITSLIEDPN LIGNKAANLS KFKGLLNMPK SLVITTEAFR EYIKDKSFLD KLVEYLDDSL SDFKRPLIFR SSSTVEDTPE KSYAGVFKSV LNVYTKEDMK EAIKEIYEDF LRKSREDIAI LVQEQFTKGK FGVMFGFDDK IVLEVTLNDP TGITSGRAKI KDLYIIDGEN AYVYNNRNWK ILFDLEIEKI KEADGKIKNV IYPYDVEFIV YKGDFYLLQV RPLHKKPEFR IGTSNLYGVG VSSGKVMGRV SFSEDNKGGD KILVIDEVPF DEIEKVKEFG GIIIEIGSLL SHIAIHMREY GIPAIVEVPI KYFREGELIE MDGSTGEIRF LDRRGFEIPR IEREIEIYDP KMLRLLIVDK YAFVLYPKDG YSILFYRDSR GLDYVLRISE DPLVDGGVDS WHTYVTILEL SLLDSEVRGD FERVIKAIEE ANMEKIEKLY GELKNKISRY YREAEMKEDL YLVEKTYAYI RLVRNVLLFE YGQKLMNNPK FMELVKKDEG ERLPELYKIY ELFDKLYDRI EKEHGLKKMD YTSYLAFQID ILKKESKV //