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Database: UniProt
Entry: B3DWD9_METI4
LinkDB: B3DWD9_METI4
Original site: B3DWD9_METI4 
ID   B3DWD9_METI4            Unreviewed;       815 AA.
AC   B3DWD9;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
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   Name=ppsA {ECO:0000313|EMBL:ACD83642.1};
GN   OrderedLocusNames=Minf_1588 {ECO:0000313|EMBL:ACD83642.1};
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=481448 {ECO:0000313|EMBL:ACD83642.1, ECO:0000313|Proteomes:UP000009149};
RN   [1] {ECO:0000313|EMBL:ACD83642.1, ECO:0000313|Proteomes:UP000009149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149};
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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}.
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DR   EMBL; CP000975; ACD83642.1; -; Genomic_DNA.
DR   RefSeq; WP_012463924.1; NC_010794.1.
DR   AlphaFoldDB; B3DWD9; -.
DR   STRING; 481448.Minf_1588; -.
DR   KEGG; min:Minf_1588; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   HOGENOM; CLU_007308_6_2_0; -.
DR   OrthoDB; 9765468at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000009149; Chromosome.
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; 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   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.
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:ACD83642.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          26..359
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          400..470
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          494..804
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   815 AA;  92561 MW;  EED3BD72AA376CFF CRC64;
     MKLTSSISIN NYIRWYHDIS LQDICHVGGK NASLGEMTRE LSFNGIVVPK GFAIIGWAYD
     QYIKYNGLRS IINEYINKLD YNNINDIKNA SKNIKKCIIN GKFPREIKSS IIEAYHILSQ
     EYNTNEVDVA VRSSATAEDL PNASFAGQQD TFLNIKGEER LLHSIKLCYA SIYSDRVLLY
     RKEMGYDTLK ISMSVGIQKM VRSDLAYSGI MFTIEPESGF KNIIVINASY GLGENIVRGN
     VNPDEYYIFK ELIHSRYNPV IKKVLGRKEK KLIYSNTNNN EINLIDIDVP IIDRNKYVLS
     KEEVITLSKW GIIIEKHYSK KYGKYTPMDI EWAKDGNDNN IYVLQARPIT TKINNENNII
     TIYKIEEKGK VIIEGTRIGE KIINGTIKNI KSINEAHRFN IGDILVTENT DPDWESIMSK
     ASAIITDKGA KTCHAAIICR ELDIPAVIGT YNATKILKDD QKVTVVCIEG EKGQVYDGII
     NYKKDIIKIN KKIITQTRVM MNIGNPQKAI QLSSLPNDGV GLARQEFILS NYVKIHPLAL
     IHYNKLSSND TKNIIDKITE NYTNKEEYYI DKLAEGIALI AAAFYPKDVI LRLSDFKSNE
     YINLIGGAEF EPQERNPMIG FRGASRYYNN RYNQAFKLEC CAIKKARDEI GLKNIKIMVP
     FVRTIMEGIC VIEELNKNGI NQGKNGTEIY MMCEIPSNII LAEEFLNIYD GYSIGTNDLT
     QLILGVDRDS EIISYIYDER NDAVKKSISN VINVAKKKNK KVGICGEAPS LYEEFLKFLI
     IEGIDSISVN PSSIQSIKIK VSELEKNIKY EKEEV
//
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