ID A0A0P7JQ73_9RHOB Unreviewed; 849 AA.
AC A0A0P7JQ73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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 ORFNames=AKJ29_12720 {ECO:0000313|EMBL:KPN63502.1};
OS Aliiroseovarius crassostreae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=154981 {ECO:0000313|EMBL:KPN63502.1, ECO:0000313|Proteomes:UP000050471};
RN [1] {ECO:0000313|EMBL:KPN63502.1, ECO:0000313|Proteomes:UP000050471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV919-312 {ECO:0000313|EMBL:KPN63502.1,
RC ECO:0000313|Proteomes:UP000050471};
RA Kessner L., Spinard E., Nelson D.;
RT "Draft genome sequence of Aliiroseovarius crassostreae CV919-312TSm, the
RT causative agent of Roseovarius Oyster Disease (formerly Juvenile Oyster
RT Disease).";
RL Submitted (SEP-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:KPN63502.1}.
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DR EMBL; LKBA01000006; KPN63502.1; -; Genomic_DNA.
DR RefSeq; WP_055189909.1; NZ_LKBA01000006.1.
DR AlphaFoldDB; A0A0P7JQ73; -.
DR STRING; 154981.AKJ29_12720; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000050471; 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 NCBIfam; TIGR01828; pyru_phos_dikin; 1.
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:KPN63502.1};
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:KPN63502.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 392..474
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 490..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 849 AA; 93027 MW; 7CCCC5B67AD61B2C CRC64;
MSDLGFTEIT PTADIHVSQH GGRAKCLQRL IRLDMPVPRT MALSFDAVRA VSAGEMPDLD
AMLARFGSDP LVSVRPSSED SDWGGPGAIL NIGMNDVVHA KLMETHGEMA AHALYLRFIQ
AYAVHVWRLD PDEFDEFSQP TADTVQAALD LYEEETDSYF PQDPKVQLTE VLRSMSRAWQ
GTTARLLREA KGAPADAGLG LVVQQMALGV GRDICGSGVI QFVNGQTGHR ELRGRYLCKS
QGRDALTDAD DRDVMYLTRD PRGRSIEEVL PDMFQALLDC GDLCRTRLRE EMEVEFTIDN
EELFILDAVR VARSERANVR IAVQMAKEGI ITREEAVMRI PPRALTELLH SQVDPEGARD
VFVSGIAASP GAATGKIVFS ARDAQAMAAQ GEDCILVRRE TSPEDIRGMH AARGILTIRG
GITSHAAVIA RGLGLPCVVG ANGMTLEKKN KKIISAQGRE LREGDVITID GAKGEVLFGA
VGMLPPELGE SFQTLMSWAD EFRDIGVRTN ADTPPDARNA RMFAAEGIGL CRTEHMFFDD
DRLLAMREMI FADQSEDRRA ALARLLPMQR ADFTELFEIM QGLPVCIRLF DPPLHEFLPH
GREGIRELAE ALGLGMSAVE RRVAGLREFN PMLGMRGVRL GVTVPEIYDM QARAIFEATL
DASKSGKPVV PEIMIPLVSA KREVEIVKAR IDAVAAAVRI ERGEEFTYRL GVMVETPRAA
LQAGEIAKHV HFLSFGTNDL TQMTYGLSRD DAGRFMGEYV RQGVFEEDPF HVLDTDGVGE
LLEIGAQRGR EEDPDLTLSI CGEHGGNPES IRFCRDKGFS YVSCSPFRVP VARLAAAHLA
VAAKLGGGG
//
