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Database: UniProt
Entry: A0A0L6D045_9RHOB
LinkDB: A0A0L6D045_9RHOB
Original site: A0A0L6D045_9RHOB 
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
//
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