ID A0A0S8F6X0_9GAMM Unreviewed; 974 AA.
AC A0A0S8F6X0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
GN ORFNames=AMJ59_22525 {ECO:0000313|EMBL:KPK56238.1};
OS Gammaproteobacteria bacterium SG8_31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK56238.1, ECO:0000313|Proteomes:UP000051321};
RN [1] {ECO:0000313|EMBL:KPK56238.1, ECO:0000313|Proteomes:UP000051321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK56238.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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:KPK56238.1}.
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DR EMBL; LJTI01000122; KPK56238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8F6X0; -.
DR PATRIC; fig|1703405.3.peg.5226; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000051321; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..974
FT /note="Phosphoenolpyruvate synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006645894"
FT DOMAIN 622..945
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 974 AA; 106205 MW; 51C821784943E004 CRC64;
MSKLVSLCLL LACIATARAS GPLATLNPEE AAQLRSIVES MKENPRGPFE RIRWFCNDGA
VLPPKAYACA DHGGGRQHGE WSDQTLRLRK EGFPIANVMV ALSASDFGES LAEQMHFRTL
VLEQFLIDVN DGWILRKARF YRGAFQVENE EASAYEFLSR LARDPLWRED RYPMLVEAAR
LVPHGAKGTG HAGVRGMATT LNEADADFGD LRNKIHGRPE PSDAARVREY ARTRGQPELA
DQYEALAAAI DAVAALPDPA PAVRAYADKV RDLQLAGDLR AGVSDLDTAG GPTERLAALA
SIMARLRQGL ATSGHPLDGI DLLLVLEGNV FGIGQQLDVD RGSYTRAESL TLMESFARAA
YGVGLLTTYE LDNLEGAVAR LQQTEVPLSD YLRELHYLGR APGWGSRRLA LYFEPAIEHL
AQIEPAARDY IPDRMRGSPL LFYSRLLNTL SVDGQRLAGI RQQLFGEEVP TGLRSLNPGI
GRGVLRTLED LEDVPEGTAD SIALVPETVS ELPVVAGILT EHEGNSLSHV QLLARNLGVP
NVVISDEYLP TLRGYVGKRV FVASSPGGVV QIALDEEVPA EAVEDTAPQV TERISIDVGR
LDLETWRLIP TSRLSAADQG VRVGPKAAQV GQLSRAFPDH VAPGLAVPFG MFAQALMERE
MSPGGPTLFE WMSDQYDELD KIQDPIARNR RTQALLQTFR DWFETLPPNP EKLAAFHEAL
LENFGPDGTY GVFVRSDTNV EDLPGFTGAG INLTVPNVVG FENIVAAMRD VWASPFTERS
FGWRQNIMSD PENVYASVLL HKSVNSHKSG VMVTADAETG DRDYVTVVVN EGVGGGVEGQ
AAESLLIRRS DGAVRLLGSA TAPFKRVLKE TGGSELVMTS GAERLLQPDE IRQLLDFVDQ
LPGWFVNLPP EERAQAVADV EFGFVDGKMY LFQIRPFVQS KGAERSQYLQ SLDAGLAESA
GRQVNMNARP GDAS
//
