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Database: UniProt
Entry: A0A0B5DNP5_9RHOB
LinkDB: A0A0B5DNP5_9RHOB
Original site: A0A0B5DNP5_9RHOB 
ID   A0A0B5DNP5_9RHOB        Unreviewed;       798 AA.
AC   A0A0B5DNP5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=P73_0468 {ECO:0000313|EMBL:AJE45183.1};
OS   Celeribacter indicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE45183.1, ECO:0000313|Proteomes:UP000031521};
RN   [1] {ECO:0000313|EMBL:AJE45183.1, ECO:0000313|Proteomes:UP000031521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P73 {ECO:0000313|EMBL:AJE45183.1};
RX   PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA   Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT   "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT   bacterium from deep-sea sediment and reclassification of Huaishuia
RT   halophila as Celeribacter halophilus comb. nov.";
RL   Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988,
CC       ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC       phosphate. {ECO:0000256|ARBA:ARBA00003144}.
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; CP004393; AJE45183.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5DNP5; -.
DR   STRING; 1208324.P73_0468; -.
DR   KEGG; cid:P73_0468; -.
DR   HOGENOM; CLU_007308_6_2_5; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000031521; 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; 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:AJE45183.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031521};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          17..341
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          384..454
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          477..786
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   798 AA;  86771 MW;  1ABFC43A50D83E90 CRC64;
     MSELLIWFEN LRRGDVARVG GKNASLGEMI STLGAKNIRV PQGFATTADA YRGFITANGL
     ERVIAERIDA LEAGRTTLRE AGLAIRTAIT SGEWPKETAD AIRAAYRELT TRSGRTKPAV
     AVRSSATAED LPEASFAGQQ ETFLNVTGEA ALLDACRRCY ASLFTDRAIT YRQIHGFGQT
     EIALSVGVQM MVRSDIGSSG VMFSIDTESG CDRFVLINGA WGLGENVVQG AVDPDEFQVF
     KPFLDDPGRL PVVARRLGAK EIKMIHGRAG EAATRNVPTS LAERERFTLS DAEVVELARY
     AKTIEAHYGV AMDMEWAKDG ETGELFIVQA RPETVQSRKT GAVFQSFEVT PAGRLMVDGL
     SVGSAAAAGR VCLIRSADEI DRFVDGSVLV TSTTDPDWVP VMKRAAAIVT DHGGRTSHAA
     IVSRELGLPA VVGTGNATHV LHDGQDVTVS CAEGGTGVVY DGLGHIDVRD ISLDDVPETR
     TGVMLNIANP SAAVRWWRLP ADGVGLARME FLVSNEIKVH PLALLNPERV TDATERSAIA
     ELTKGYKDGR SYFTECLAMG LARIAAVWHP KPVIVRLSDF KSNEYADLLG GRHFEPLEEN
     PMIGLRGAAR YYSEFYRDAF ALECVALKRL RDDMGFTNVI VMVPFCRSPE EADKVLEVMT
     ANGLTRGENG LEVYVMTEIP SNVIRAAEFA ERFDGFSIGS NDLTQLTLGV DRDSEALAEV
     FRERDPAVIW MIETAIRRAR EAGRKIGLCG QAPSNDPDFA RLLVKAGIDT ISVTPDSFLE
     VKRNVALAEE GDVRMRRA
//
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