ID A0A078LTC1_9PSED Unreviewed; 790 AA.
AC A0A078LTC1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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:CDZ93612.1};
GN ORFNames=BN1079_00907 {ECO:0000313|EMBL:CDZ93612.1}, EGJ00_08730
GN {ECO:0000313|EMBL:RRV15879.1};
OS Pseudomonas saudiphocaensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ93612.1, ECO:0000313|Proteomes:UP000053902};
RN [1] {ECO:0000313|EMBL:CDZ93612.1, ECO:0000313|Proteomes:UP000053902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ93612.1,
RC ECO:0000313|Proteomes:UP000053902};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRV15879.1, ECO:0000313|Proteomes:UP000271179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS_399 {ECO:0000313|EMBL:RRV15879.1,
RC ECO:0000313|Proteomes:UP000271179};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCSF01000001; CDZ93612.1; -; Genomic_DNA.
DR EMBL; RHQU01000005; RRV15879.1; -; Genomic_DNA.
DR RefSeq; WP_037022608.1; NZ_RHQU01000005.1.
DR AlphaFoldDB; A0A078LTC1; -.
DR STRING; 1499686.BN1079_00907; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_6; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000053902; Unassembled WGS sequence.
DR Proteomes; UP000271179; 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 PRINTS; PR01736; PHPHTRNFRASE.
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:CDZ93612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 17..345
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 383..454
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 481..780
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 790 AA; 86302 MW; D52D292000AD8186 CRC64;
MVEYVVSLDK LGNHDVERVG GKNASLGEMI SNLAGAGVSV PGGFATTAQA YRDFMELSGL
NEQIHTMLDA LDVDDVNALA KAGAQIRSWI MSAEFPAQLD ADIRAAFAEM SAGNDNLAVA
VRSSATAEDL PDASFAGQQE TFLNIRGVDN VIRAAKEVFA SLFNDRAIAY RVHQGFDHKL
VALSAGVQRM VRSETGTAGV MFTLDTESGF RDVVFITGAY GLGETVVQGA VNPDEFYVHK
HTLEAGRPAI LRRNLGSKAI KMIYGAEASA GKSVKTVEVD QAERMRFCLT DEEVSNLARQ
AMIIEKHYGR PMDIEWAKDG DDGQLYIVQA RPETVKSRSS ANVMERYLLK EKGTVLVEGR
AIGQRIGSGP VKIIRDVSEM DRVQPGDVLV SDMTDPDWEP VMKRASAIVT NRGGRTCHAA
IIARELGIPA VVGCGNATDL LKDGQRVTVT CAEGDTGLIF EGELGFDIRQ NSIDAMPELP
FKIMMNVGNP DRAFDFAQLP NEGVGLARLE FIINRMIGVH PKALLNFDSL PAEIKSSVEK
RIAGYGDPVD FYVEKLVEGV STLAAAFWPK KVIVRLSDFK SNEYANLIGG KLYEPEEENP
MLGFRGASRY ISESFRDCFE LECRAMKKVR DVMGLTNVEL MVPFVRTLGE ASQVIDILAK
FGLKRGENGL RIIMMCELPS NALLADEFLE YFDGFSIGSN DMTQLALGLD RDSGIIAHLF
DERNPAVKKL LASAIEACKK ADKYVGICGQ GPSDHPDLAK WLMEQGIESV SLNPDSVLDT
WFFLADQEIS
//
