ID A0A1Q4B7Y2_9GAMM Unreviewed; 792 AA. AC A0A1Q4B7Y2; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-APR-2021, entry version 15. DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623, ECO:0000256|PIRNR:PIRNR000854}; DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854}; DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996, ECO:0000256|PIRNR:PIRNR000854}; DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00020377, ECO:0000256|PIRNR:PIRNR000854}; GN ORFNames=BGO90_13915 {ECO:0000313|EMBL:OJX98942.1}; OS Legionella sp. 40-6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella; unclassified Legionella. OX NCBI_TaxID=1895903 {ECO:0000313|EMBL:OJX98942.1, ECO:0000313|Proteomes:UP000186293}; RN [1] {ECO:0000313|EMBL:OJX98942.1, ECO:0000313|Proteomes:UP000186293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=40-6 {ECO:0000313|EMBL:OJX98942.1}; RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K., RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.; RT "Genome-resolved meta-omics ties microbial dynamics to process performance RT in biotechnology for thiocyanate degradation."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988, CC ECO:0000256|PIRNR:PIRNR000854}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2; CC Evidence={ECO:0000256|ARBA:ARBA00001518, CC ECO:0000256|PIRNR:PIRNR000854}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRNR:PIRNR000854}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|PIRNR:PIRNR000854}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000854}. 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:OJX98942.1}. 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; MKVI01000546; OJX98942.1; -; Genomic_DNA. DR UniPathway; UPA00138; -. DR Proteomes; UP000186293; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR006319; PEP_synth. 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR PANTHER; PTHR43030; PTHR43030; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 1. DR PIRSF; PIRSF000854; PEP_synthase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01418; PEP_synth; 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, ECO:0000256|PIRNR:PIRNR000854}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000854}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000854}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000854}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000854}; Pyruvate {ECO:0000313|EMBL:OJX98942.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}. FT DOMAIN 19..347 FT /note="PPDK_N" FT /evidence="ECO:0000259|Pfam:PF01326" FT DOMAIN 387..458 FT /note="PEP-utilizers" FT /evidence="ECO:0000259|Pfam:PF00391" FT DOMAIN 484..786 FT /note="PEP-utilizers_C" FT /evidence="ECO:0000259|Pfam:PF02896" SQ SEQUENCE 792 AA; 87275 MW; 4CB0A20C2A8AC235 CRC64; MAVNKHVIDL AHLGMKDIEQ VGGKNASLGE MISHLSSAGV LVPGGFATTA DSFREFLAQN DLDKAIYTKL ATLDTDNVHQ LSVVGKEIRD LIIKTPFHPE FEAAVRDAYT AMARTIGSET FSVAVRSSAT AEDLPDASFA GQQETLLNVR GVDQVLLAIK EVFASLYNDR AIAYRTHHEF AHHDVALSAG IQQMVRSDLA VSGVMFTMDT ESGFDQVVFI TSSYGLGEMI VQGAVNPDEF YVHKPGLQAG RPALIRRNLG SKAIKMIYCN NPELNRRVQT VEVPAEERLV FSLTAEEVEN LARHALIIEK HYGRPMDIEW AKDGINGQLY ILQARPETVK SRVNKQILER YSLQKRSTIL SEGRSIGQRI GQGKARIIHD VSEMHRVEPG DVLISDMTDP DWEPVMKRAA AIVTNRGGRT CHAAIIAREL GIPAVVGCGD ATKTIKDGDE VTVSCAEGDT GLVYEGILPF THDCLDVETM PELPLKVMLN VGNPERAFAF QFIPNAGVGL ARLEFLISNT IGIHPRALLE FDQLEDAELK KFITEKTMAY ASPVEYYIER LKEGIATIAA AFYPKPVIVR LSDFKSNEYA NLVGGSLYEP HEENPMLGFR GASRYVSPEF APCFALECKA VRRVREDMGL DNVEIMIPFV RTVEEAKQVI TVLKDNGLER GKHGLRVIMM CELPSNALLA KEFLEHFDGF SIGSNDLTQL TLGLDRDSGL VAAQFDERNE AVKALLHLAI AACRQAGKYI GICGQGPSDH QDFARWLMDE GIESVSLNPD SVLETCLFLA KQ //