ID A0A0L6D045_9RHOB Unreviewed; 846 AA.
AC A0A0L6D045;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 Name=ppdK {ECO:0000313|EMBL:KNX43345.1};
GN ORFNames=ROTO_01340 {ECO:0000313|EMBL:KNX43345.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX43345.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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 -!- 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:KNX43345.1}.
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DR EMBL; LGVV01000001; KNX43345.1; -; Genomic_DNA.
DR RefSeq; WP_050661097.1; NZ_LGVV01000001.1.
DR AlphaFoldDB; A0A0L6D045; -.
DR STRING; 74031.SAMN04488077_11563; -.
DR PATRIC; fig|74031.6.peg.136; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000037046; Unassembled WGS sequence.
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; 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; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
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; PS00742; PEP_ENZYMES_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KNX43345.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3}; Pyruvate {ECO:0000313|EMBL:KNX43345.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW Transferase {ECO:0000313|EMBL:KNX43345.1}.
FT DOMAIN 393..474
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 488..839
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 425
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 801
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 588
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 715
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 736
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 737
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 739
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 846 AA; 91454 MW; C1BE89A9D02FEC67 CRC64;
MQQDDPDITL ITPTSPVHAN THGGRAKCLQ RLARLDLPVP RTIALSFKAV HGIAAGELPD
MAALLAPFGE APLLCVRPSS EDPDWGGPGA VLNIGINDAR FIELSDKIGK RAAAEIYLRF
VQSYAVHVAR LDPDIFDDVS EDPSIGLGQA LRAYEDETEE EFPQDPAVQL TEVLRSMARA
WEGTTARLLR QAKGAPADAG LGLVVQELAL GLGEGECGSG VMQLVNSQTG ARQITGRYLS
QSQGRDALQR GADALYLERD PRGPSLEELA PDAFAHVKAY AALMREKLRE DMQAEFTIEN
GKVWLLDGLR VARNARAAVS IAVALAEDGI ISHEEALMRV EPRALNELLH RQVDPDAERD
VLARGIAASP GAASGRVVFS AADAQAAQAR GEACILVRRE TSPEDIRGMH AAAGVLTERG
GMTSHAAVIG RGIGLPCVVG ASDIHFQPRR KQLTMPDGRV VKAGEMITID GTNGLVLAGE
APLLEAARDG SFQTLMSWAD NVRDIAVRAN ADTPADAEVA RNFKARGIGL CRTEHMFFEA
DRLTVMREMI FADASEDRAA VLERLLPMQR ADFTDLFRIM QGQPVCIRLF DPPLHEFLPT
DRAGHLQLAE ALDLPLSDVT RRVEALGEYN PMLGMRGVRL GITVPEIYDM QARAIFEATL
ESSKDGAPVV PEIMIPLVSA RREVELVKTR IDAVAAAVRN ETGRDFAYRL GVMVETPRAA
LRAGEIAPLV SFLSFGTNDL TQMTYGLSRD DAGRFMSNYV QQGVYPEDPF HSLDIDGVGE
LLRIGAERGR AANPDVVLSI CGEHGGNPES IAFCRDAGFT YVSCSPFRVP VARLAAAQLT
VRDKIG
//