ID A0A1G1KDX2_9BACT Unreviewed; 1723 AA.
AC A0A1G1KDX2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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};
DE Flags: Fragment;
GN ORFNames=A3D28_03495 {ECO:0000313|EMBL:OGW91147.1};
OS Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_63_14.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801824 {ECO:0000313|EMBL:OGW91147.1, ECO:0000313|Proteomes:UP000179358};
RN [1] {ECO:0000313|EMBL:OGW91147.1, ECO:0000313|Proteomes:UP000179358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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:OGW91147.1}.
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DR EMBL; MHFJ01000051; OGW91147.1; -; Genomic_DNA.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000179358; 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 Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
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; IPR006319; PEP_synth.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
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; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 2.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 2.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 132..478
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 724..804
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 861..1150
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT DOMAIN 1502..1677
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGW91147.1"
SQ SEQUENCE 1723 AA; 189177 MW; 43A56ED0DBC8F97F CRC64;
GAAEVPEAKR RRLLVLDVVA IVQRLKATVP PGGWAALVAA PLATRQEIQL PDVLAFLLGL
GGFAATVPGG AAFVGRLPEG TTTEPGAGVV YFDVGSVSLD QIQSAGAQWA GAPSLAEASI
LWFEQLGQRD TEVAGGKGAN LGEMIRQEVG GVPQGYVVTA KAFQDTLSVN NAHEELEAIL
QRIDVGNAET AEQEAKRIQK LIRGLTLPQK LQEEILRYHQ ELADRVGIPA EEIRVAVRSS
ATAEDREVTE EMKARLGEEV TSGSSAGQQS TYLNVPRTDI VGRVLDDYAS LFNPEAVSYR
DTQGMVDFLL GLEPGVRGEL EHRLLEREET REVGRLLQGK RHVSRVQLRR GIELAVPELL
ESFDTAYEPY VNLHRLSLAV VVQHMIRSER AFTVFSYDNR SGWTGLSFEK DNFDQPAAGR
VFRIDANYGL GESIVQGKTN PDSYLVHVFT DPTDRQHVNI LEKTLGTKKL QYIYVEDALE
DIGLTEVEAM QIVGLVKATE QQGKVARRGG MPEPPMGVLS KLHLARSDSD ALITALLRVA
ELDYDVLDDF TLPDPIRHIA LDRAQFIRLA HFVKTRKVDP DDRSMATVVP AMLRGEFAFT
DDRVREIALA AKGATDFYGN VRDMEGAQEG KALGFVQSRA ITVETEIARP STLQLKKAVV
NEAAAKAAER AGDLLVSGVP GRNAVVGEIF VLDKESDVPY GLQLKQAQDR AAEIAREGRK
LLLRTKMTTP QDVPAMKVSG GVIADEGGDT SHAAIVSREL KIATVVGISE ELERIRRRDP
TRHAELLAAL NTPGNIVTVD ANTGKVYRGE LPIEVQEVDI PAKSDPTAPA SAPHLPELRF
TKPGLIVANP AAMREISKIG LYDSYYGVSL ARAEFILVDI GVHPRAIEAY DNLKTLEADP
EAQLDERGRR DVEMLRKNAS LIADIEDKVR GYPSAKEFFI QKMYEGIASM AAANGLHQKV
LYRFNDFKQN ELNQITGGPE FGLVEEASMI GDRGTGWLLK DENRTALGME LEALRRAYDD
GYTNVGAFFA FVRTPDELAE GLRRFEEAQM PLDTVGMMVE LPSNVIHARE FADLLAEYGK
RNEKHVFFSF GTNDLTQLTR VAGREEPHIR ELFSEAHRAI VGSIRHVVQE VARARERHGV
DFTCGLCGQA IVKLVDSDPA AARSIAVMLD STGLDILAFM KAVKLIAEAE LDLGRILAKA
AAGARILALG TGTQRHGAAS RQLLVAQKVP DLAQVSLGDV LVLANAGSLR TDDVQAMLRG
EPTAFTTALE PEVGRLEAKA VEQFVDRIQR DTLSAEMRRF AGELKERLPA DEAERQEVLA
SREFHEAYVR LSVFDAIDRA GAVVIPGDHP AREAVVTLAR TFAKPVFFVT EGLDRLHTGE
VVTVDFAAGR VYEGELPLTR AAADEEDAVR VVERADEPER LPAIVTTARD VYQRLGIHPV
AFTRRQAGTL DKRLSRLLDE PNHRYQQLVR EADGIEDAEP LFKRTVRQVL REAAEQARRR
ATALVYRTSD LNSHDFQALA LGEELDIHEE NPPLGLGGFY RFVKLDEYRT LLRWELEVVA
QLQQELGPIA VELADVRDLE HLDTALQVLA GVGLEPGKAG FQLGVRMVNP DNYLFASDYM
TRGRLSFVSV DERRLSQTYL AADRDNAFVP VDDAVAAKNL VLPMNMIKQA AHDAGVRWVV
PADAPAQPKG ITEEAGPPEA NISAAIEETF EADEAEDALL RQP
//
