ID A0A1I3N139_9RHOB Unreviewed; 847 AA.
AC A0A1I3N139;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN ORFNames=SAMN04488138_101238 {ECO:0000313|EMBL:SFJ02911.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ02911.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFJ02911.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ02911.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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; FORY01000001; SFJ02911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3N139; -.
DR STRING; 576117.SAMN04488138_101238; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000183299; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.80.30; -; 1.
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 Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PIRSF; PIRSF000853; PPDK; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:SFJ02911.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3}; Pyruvate {ECO:0000313|EMBL:SFJ02911.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183299};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 395..476
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 496..841
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 428
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 803
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 534
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 590
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 717
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 738
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 739
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 740
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 741
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 741
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 847 AA; 92186 MW; 911990DFBEBD9DD7 CRC64;
MQQESDILGF TRIRRVAPIA VNTHGGRAKC LQRLIRLDLP VPETVALSFD AVHHLAEGQK
FDKQALLRVF GDAPLLSVRP SSEDPDWGGP GAILNIGMND ARHAELTASH GAEAADALYL
RFVQSFAVHV ERLDPELFEF DASTPVSEAL KSALEAHEDE TGEPFPQDAA EQLGQVLRSM
ARAWEGTTAR LLRQAKGAPA DAGLGLIVQA MALGVGPGES GAGVIQLVDS DTGAPLIKGR
YKRQSQGREA VSGEVDALYL TRDTRGPSLE EAQPEIFATL VEISKKCRTR LREEMQVEFT
IENGKLSILD AVRVPRSSRA ALRIAVQLAE DGIIPRTEAI TRVPARSLTE LLHQQVDPSA
KRDVIAQGIA ASPGGAVGRI VFNSSVAQSY QSRGDPCILV RRETTPEDIR GMHSSVGILT
ERGGVTSHAA VIARGMGVPC VVGASMRINS RERTLELADG RKLQEGDLLT LDGSAGVALL
GAVDMLPPVK DHWYLKLMEW ADAIRDIGVR ANADTPMDAA LARDFKAEGI GLCRTEHMFF
EGDRLTVMRE MIFASRHEDR AEAIARLLPM QRSDFIELFR IMEGLPVCIR LFDPPLHEFL
PSDREGAKEL AEALDLPLSD VTRRIEWLSE FNPMLGMRGV RLGITFPEIY EMQARAIFEA
TIEANKHGAP VVPEIMIPLV SAKREVELVK TQIDGVAAAV RTENGAEFTY RLGVMVETPR
AALRAGDIAQ NAAFLSFGTN DLTQMAYGLS RDDAGRFMNA YVQQGVFPED PFHMLDFEGV
GELLKIGAER GRLARPDVTV AVCGEHGGNP ESIAFCREAG FDYVSCSPFR VPVARLAAAQ
LVVADVK
//
