ID A0A1S6IPJ1_9LACT Unreviewed; 879 AA.
AC A0A1S6IPJ1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN Name=ppdK {ECO:0000313|EMBL:AQS53370.1};
GN ORFNames=BW727_101000 {ECO:0000313|EMBL:AQS53370.1};
OS Jeotgalibaca dankookensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=708126 {ECO:0000313|EMBL:AQS53370.1, ECO:0000313|Proteomes:UP000188993};
RN [1] {ECO:0000313|EMBL:AQS53370.1, ECO:0000313|Proteomes:UP000188993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EX-07 {ECO:0000313|EMBL:AQS53370.1,
RC ECO:0000313|Proteomes:UP000188993};
RX PubMed=24554638; DOI=10.1099/ijs.0.057059-0;
RA Lee D.G., Trujillo M.E., Kang H., Ahn T.Y.;
RT "Jeotgalibaca dankookensis gen. nov., sp. nov., a member of the family
RT Carnobacteriaceae, isolated from seujeot (Korean traditional food).";
RL Int. J. Syst. Evol. Microbiol. 64:1729-1735(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
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; CP019728; AQS53370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6IPJ1; -.
DR STRING; 708126.BW727_101000; -.
DR KEGG; jda:BW727_101000; -.
DR Proteomes; UP000188993; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
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; 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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:AQS53370.1};
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:AQS53370.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AQS53370.1}.
FT DOMAIN 23..72
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 203..295
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 303..357
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 426..507
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 522..876
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 459
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 838
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 622
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 751
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 772
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 774
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 775
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 879 AA; 97471 MW; 41E250CB9C8FCF3F CRC64;
MIVTEKDTKF VYAFEEGQKE MVDLLGGKGS NLAEMTRLGL PVPSGFTIST QACLNYLKNN
KLDSELILQI EKKAEELEIK TNKKFNDLVS PLLVSVRSGA KFSMPGMMDT VLNLGMNDVT
VETIAKITGN SAFAYDSYRR FIQMFSDVVK EVDRQLFEQE LTYYKEKQGY QYDTQMKERD
WKIITQLYKE IYANEVNEQF PQEPEKQLLE SIEAVFKSWN NPRAKTYRRM HAISDDLGTA
VTVQEMVFGN TGMKSGTGVA FTRNPSNGKQ GLFGEFLINA QGEDVVAGIR TPQDISQLAK
IMPEAYQKFT DLAALLEAHY HDMQDIEFTI EEGQLFILQT RNGKRTPRAA IEIAIDLVEE
GVISKEEALK RLTPQMLEQL LHPTFVAKEL AQHEVFAQGL PASPGSASGK VYFTAEAAKK
ANQAGEKTVL LRKETSPEDI EGMAISEAIV TAHGGMTSHA AVVARGMGTC CVVGCEKLQI
EEGSKKATVA GHTIEEGTVI SVDGSTGCIY MGEIAKEKPT DESTALGKIV SWSKEIGTIK
VMANAETEKE IAEAFQLGAE GMGLVRTEHM FFGEKRIVEM RKMILSPDPT AKKAALMNLK
TFQKEDFKVI YRLAKEKSAT IRLLDPPLHE FIPVGKEVAK MATILGISEA EVNQRIANLA
ENNPMLGHRG CRLAITNPEI YEMQVAAIME AAIEVTEELG NESVIQPEIM IPLVSIEKEI
VFIKEKLEKI ISNTFIEKGK EIPYLIGTML ETPRACLIAD KISKHVDFIS FGTNDLTQLT
FGFSRDDIGK FVNDYERQQI IESDPFQHLD KDGVGKLLKI AINSVKENES SDVSIGICGE
VGGDPQSIEF LLNEGIQYVS CSPYRIPAAL LTIAKLNIS
//
