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Database: UniProt
Entry: A0A0E9MZ74_9BACT
LinkDB: A0A0E9MZ74_9BACT
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ID   A0A0E9MZ74_9BACT        Unreviewed;       814 AA.
AC   A0A0E9MZ74;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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:GAO43037.1};
GN   ORFNames=FPE01S_02_01420 {ECO:0000313|EMBL:GAO43037.1};
OS   Flavihumibacter petaseus NBRC 106054.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO43037.1, ECO:0000313|Proteomes:UP000033121};
RN   [1] {ECO:0000313|EMBL:GAO43037.1, ECO:0000313|Proteomes:UP000033121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO43037.1,
RC   ECO:0000313|Proteomes:UP000033121};
RA   Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA   Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL   Submitted (APR-2015) 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:GAO43037.1}.
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DR   EMBL; BBWV01000002; GAO43037.1; -; Genomic_DNA.
DR   RefSeq; WP_046368981.1; NZ_BBWV01000002.1.
DR   AlphaFoldDB; A0A0E9MZ74; -.
DR   STRING; 1220578.FPE01S_02_01420; -.
DR   OrthoDB; 9765468at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000033121; 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:GAO43037.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          23..356
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          400..471
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          494..805
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   814 AA;  89930 MW;  8B84033F5BEEEAC0 CRC64;
     MENLERGEYI RDLKDVGLTD IAIAGGKNAS LGEMLQHLNE LQINVPEGFV ITVNAYTHFV
     MANNLDGKIR ELIAAIDVNN IESLRRQGLA IRQLIRNSRF PKDLAIEIIE AYERLSDRYS
     QLVTDVAVRS SATAEDLPDA SFAGQQETYL NVRGQAALID AVRNCFASLF TDRAISYREN
     FGFDHFQVGL SVCVQKMVRS DLASSGVAFS IDTESGFPDA VVINGSYGLG ELIVQGSVSP
     DEFLVFKPTL QQGFAAIIEK KLGSKQEMMI YGDDPDQRLR IIPTEKSLQH KFCLNDKMIL
     QLSAWVTSIE TYYTQKKGHW CPMDVEWAVD GLSGELFIVQ ARPETIHSRK QGHSIREYAF
     KREAGNEILF KGIAIGDGIA SGQATVMHSL DRRVGDGHDF KAGDVLVTDM TDPDWEPIMK
     KVSAIITNKG GRTCHAAIVA RELGVPAIIG CGNATERLAQ QQLVTVSCVE GDEGFVYSGE
     LDFDVIETDL SALPEVKTDI MLNIGSPAMA FSYAAYPHKG VGLAREEFII NNFIRVHPLA
     LLQHRELNDA GLSAEISKAI AGFASEADYF VQKLAFGIAR IAAAFYPETV IVRFSDFKSN
     EYFNLLGGKY FEPAEENPMI GWRGASRYYS PEYMAAFELE CRAIKKVREE MGLTNVVVMI
     PFCRTVGELK KVLDVMQLFG LERGKDGLQV YLMAELPSNI IMAGEFAKHI DGFSIGSNDL
     TQLTLGLDRD SSLVAHLYDE RDPAVKAMIR MLVKTAKEHN VKVGICGQGP SDFPDFAQFL
     VEEGIDSISI TPDALIKTVK AIAAIEKEKV FSHV
//
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