ID A0A1F8MGW7_9CHLR Unreviewed; 807 AA.
AC A0A1F8MGW7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:ARBA00033470, ECO:0000256|PIRNR:PIRNR000854};
GN ORFNames=A2Z77_02180 {ECO:0000313|EMBL:OGN97843.1};
OS Chloroflexi bacterium RBG_13_51_36.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797625 {ECO:0000313|EMBL:OGN97843.1, ECO:0000313|Proteomes:UP000179678};
RN [1] {ECO:0000313|EMBL:OGN97843.1, ECO:0000313|Proteomes:UP000179678}
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 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:OGN97843.1}.
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DR EMBL; MGMS01000009; OGN97843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MGW7; -.
DR STRING; 1797625.A2Z77_02180; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000179678; 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; 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; 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 NCBIfam; TIGR01418; PEP_synth; 1.
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; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PIRSF; PIRSF000854; PEP_synthase; 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, 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:OGN97843.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 16..335
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 379..451
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 474..795
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 807 AA; 90365 MW; 3C5F08E0C62A0F81 CRC64;
MKFVKWFDEI GAEDVALVGG KNASLGEMIR SLGKKGVNIP PGFAITAEAY KYLVKRAGIR
QRIKGILADL DTHDMEDLAD RGEKLRNLIA HSRCPRDLEE EIVISYRKLE ERFGKSVDVA
VRSSATAEDL PTASFAGQQT SYLNVRGEGD LLERVMDCFA SLFTNRAISY RVDKGFDHLS
VYVSVGVQKM VRSDLACAGV MFSIDTDSGF RDVVYITAAY GLGENVVQGI VDPDQFYVFK
PTLKKGFRPI VEKKLGLKDN RLVYMRHGSG AEQKQVKVEE QRQFALNDDE ILTLARWACI
IEEHYGVPMD IEWAKDGTNG ELFVVQARPE TVHSQVDLTS LRTYVLEERG RLLARGEPVG
TKIGQGEVHV IEDSSEIQKF KSGQVLVADM TDPDWEPIMK IASGIVTNKG GRTCHAAIVS
RELGVPCVIS TGNGTEVLEE GQEVTINCSG GEGRVYEGRL KYRIDEVEVT KVPRPRTRIM
MNFGIPGGAF IQSQIPNDGV GLAREEFIIN SYIGIHPMAL IQYDELKKAA SGDEKLTKVI
KEIDQKSVPY RDKKGFFIDN LAMGIAKIAA GFHPNDVIVR FSDFRTNEYA NLVGGYRYEP
KERNPMLGWR GASRYYDKRF KPAFGLECLA IRKVRDEMGL TNVKVMIPFC RTPEEGMKVM
EAMEEFGLRR GENGLEVYVM CEIPSNVILA EEFADVFDGF SIGSNDLTQL TLGLDRDSEL
VAHIFDERNE AVKRLVKQLI YAAHRHKPRR KVGICGQAPS DFPEFAEFLV ECGIDSMSLN
PDVVLATRLN IAEVEKRIKS KTRRKQK
//
