ID A0A0G0R1I7_9BACT Unreviewed; 868 AA.
AC A0A0G0R1I7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KKR07642.1};
GN ORFNames=UT36_C0014G0022 {ECO:0000313|EMBL:KKR07642.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR07642.1, ECO:0000313|Proteomes:UP000034818};
RN [1] {ECO:0000313|EMBL:KKR07642.1, ECO:0000313|Proteomes:UP000034818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR07642.1}.
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DR EMBL; LBWM01000014; KKR07642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0R1I7; -.
DR STRING; 1619067.UT36_C0014G0022; -.
DR PATRIC; fig|1619067.4.peg.1139; -.
DR Proteomes; UP000034818; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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 Pfam; PF01326; PPDK_N; 3.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KKR07642.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:KKR07642.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKR07642.1}.
FT DOMAIN 16..52
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 59..285
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 300..353
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 417..498
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 514..864
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 450
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 826
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 556
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 613
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 740
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 740
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 761
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 762
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 763
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 764
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 764
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 868 AA; 96142 MW; 597490F3C2D4D2C6 CRC64;
MKYIFPFSEG SKDMKELLGG KGANLAEMTK LGLPVPPGFT ITTETCNYFL INKGYPSGFQ
EELKENLAEL ELNMSKNLGD GQNPLLVSVR SGAKISMPGM MDTVLNLGLN DTTVLGLISN
TQNERFCYDA YRRFVQMFGN VVLGVDHDHF EEAICELKEK KGIKLDTELT AENLKSLVQI
YKEIIQKHTN SPFPEQPSEQ LRLSIEAVFN SWNNKRACTY RNLHGIPHNI GTAVNIQAMV
FGNKGEDSGT GVAFTRNPST GEKIFYGEYL INAQGEDVVA GIRTPVPLDK LKIQMPTVYE
ELVSIKDRLE NHYHDMQDIE FTVEQGRLFI LQTRNGKRTA HAAVRIATEM VKEGLIDKHT
ALLRVEPNQL KQLLHPSIDP KAKITVIAKG LPASPGAATG KVIFTADEAY EKAQTGDQVI
LVRKETSPED IHGMHAAQGI LTSTGGNTSH AAVVCRGMGK CCVAGCGDII VNGKERKFTA
GEIVVYEGDI ITLNGTTGEV ILGEAPMCEP ELDGAFRELM QWTDDVRTLK VRANADTPED
AKVALEFGAE GIGLCRTEHM FFAEERIPLM REMILSKDNP EARKKALDKL LPIQKQDFAQ
IFEVMKGLPV TIRLFDPPLH EFLPDIDQHK RIQNLATELN LTIEHLKDII TNLHEVNPML
GHRGCRLGIT YPELYAMQVR AILTAAIECH DRGLAVHPEI EVPLIGNVSE LKAVKKIIQG
VIEELKEGIK FEYKIGTMIE LPRACLTADE IAPEADFFSF GTNDLTQMTY GFSRDDVGTF
LPYYLEKGIL VEDPTSSIDQ SGVGFLMKTC VKLGRQTKEN LEIGICGEHG GDPKSIEFCH
EIGLNYVSCS PYRVPIARLA AAQATLKH
//
