ID A0A1E7RDU8_9GAMM Unreviewed; 792 AA.
AC A0A1E7RDU8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:KAA8735314.1};
GN ORFNames=BJI46_10035 {ECO:0000313|EMBL:OEY97432.1}, F4V57_00480
GN {ECO:0000313|EMBL:KAA8735314.1};
OS Acinetobacter qingfengensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY97432.1, ECO:0000313|Proteomes:UP000185895};
RN [1] {ECO:0000313|EMBL:OEY97432.1, ECO:0000313|Proteomes:UP000185895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY97432.1,
RC ECO:0000313|Proteomes:UP000185895};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8735314.1, ECO:0000313|Proteomes:UP000323633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8735314.1,
RC ECO:0000313|Proteomes:UP000323633};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) 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:OEY97432.1}.
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DR EMBL; VXKN01000001; KAA8735314.1; -; Genomic_DNA.
DR EMBL; MKKK01000009; OEY97432.1; -; Genomic_DNA.
DR RefSeq; WP_070069144.1; NZ_VXKN01000001.1.
DR AlphaFoldDB; A0A1E7RDU8; -.
DR STRING; 1262585.BJI46_10035; -.
DR OrthoDB; 9765468at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000185895; Unassembled WGS sequence.
DR Proteomes; UP000323633; 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:OEY97432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000854}.
FT DOMAIN 17..344
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 480..780
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
SQ SEQUENCE 792 AA; 86817 MW; 127314E0E714F220 CRC64;
MEARVIGLEK LGKHDVEKVG GKNASLGEMI SHLSNAGVSV PGGFATTADA YREFLDKSGL
KAKIQEELTH LNVDDIAALT ETGAKIRQWI IDSPLTPELE KETRNAFAAL SNGNPDIAVA
VRSSATAEDL PDASFAGQQE TFLNIRGIDN VLVAIKEVFA SLYNDRAIAY RVHQGFDHDI
VALSAGVQRM VRSETGSAGV MFTLDTESGF RDVVFITASY GLGEMVVQGA VNPDEFYLSK
PLLNTNRHAV LRRNLGSKHK KMIYSNEGAA GRSVEIVDVE KQDRQQFALN DHELQELAKQ
ALIIEKHYGA PMDIEWAKDG DDQQLYIVQA RPETVKSRQS AGTMERYLLK QKGTVLCEGR
SIGQRIGSGK VRIVTNIKDM DRVQPGDVLV SDMTDPDWEP VMKRAAAIIT NRGGRTCHAA
IIARELGVPA IVGCGNATEV LTEDQEVTVS CAEGDTGFIY ENALDFEVQS NSIESMPPLS
FKVMMNVGNP DRAFDFAQIP NAGIGLARLE FIINRMIGVH PKALLNIDSL PRETRAAVLA
RTAGYTSPVE FYVEKLVEGI ATLAAAFADK PVIVRMSDFK SNEYANLIGG KLYEPEEENP
MLGFRGASRY VSDNFRDCFE LECRALKKVR DEMGLTNIQI MIPFVRTVAE AKRVIELLAA
NGLKRGENGL KVIMMCELPT NALLAEQFLE HFDGFSIGSN DLTQLTLGLD RDSGIVSHLF
DERDPAVKAL LSMAIHACRK AGKYVGICGQ GPSDHPDLAK WLMEQGIESV SLNPDSVLDT
WFFLAEEKAS NQ
//
