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Database: UniProt
Entry: D2MP70_9FIRM
LinkDB: D2MP70_9FIRM
Original site: D2MP70_9FIRM 
ID   D2MP70_9FIRM            Unreviewed;       880 AA.
AC   D2MP70;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
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:EFC05690.1};
GN   ORFNames=HMPREF9013_0296 {ECO:0000313|EMBL:EFC05690.1};
OS   Bulleidia extructa W1219.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Bulleidia.
OX   NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC05690.1, ECO:0000313|Proteomes:UP000005017};
RN   [1] {ECO:0000313|Proteomes:UP000005017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RT   "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:EFC05690.1}.
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DR   EMBL; ADFR01000008; EFC05690.1; -; Genomic_DNA.
DR   RefSeq; WP_006627191.1; NZ_ADFR01000008.1.
DR   AlphaFoldDB; D2MP70; -.
DR   STRING; 679192.HMPREF9013_0296; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG1080; Bacteria.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000005017; Unassembled WGS sequence.
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; 2.
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:EFC05690.1};
KW   Magnesium {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:EFC05690.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005017};
KW   Transferase {ECO:0000313|EMBL:EFC05690.1}.
FT   DOMAIN          19..292
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          304..357
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          425..506
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          522..874
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        458
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   ACT_SITE        836
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   BINDING         564
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         621
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         750
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         750
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         771
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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         774
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ   SEQUENCE   880 AA;  97915 MW;  9BEAF4B42A73E75F CRC64;
     MTNQKYVYQF QEGNGSMRAL LGGKGANLAE MRNLGMPVPE GFTVTTEACT AYYEDGKRIN
     ESILEEIKKN VLWLEETTGK KLGSRENPLL VSVRSGARAS MPGMMDTILN LGINDEVVQV
     IEEKSNNTRF AYDSYRRFIQ MFSDVVMGLD KSKFEKIIDE VKKQRGVELD IDLNGEDMKE
     LTARFKAFYE ENLHETFPQD PHVQLERSVE AVFRSWNNER AIFYRRMNDI PSSWGTAVNV
     MEMVFGNMGN DCGTGVAFTR NPATGEKKLF GEFLMNAQGE DVVAGIRTPQ PIAELAKTIP
     NAYQEFIEIC NRLEKHYHDM QDMEFTIEHG KLFMLQTRNA KRTATAALKV AVDMEMEGLV
     TKEQALLMVE PKQLDDLLHP QFDQKSLAAK SGDIIAKGLA ASPGAACGEV VFTAEDAKNK
     ASLGRKVILV RLETSPEDIE GMHVSQGILT VRGGMTSHAA VVARGMGTCC VSGAGMIQVD
     EEAETFTVGQ ETYKVGDIIS LDGSTGNVYR GRIETVPATI SGDFKTFMTW ADETRTMKVR
     TNADTPEDAR KALEFGAEGV GLVRTEHMFF NSQERINAIR ELCISTNDEQ REKALALLEP
     MQQADFEGIY EAMEGRSVTI RLLDPPLHEF LPKTAQEAEQ VAKDLGVTVD EIIMASANLH
     EFNPMMGHRG CRLDVTYPEI GRMQARAIMK ATLAVNKRHP EYHLVPEVMI PLVGEKKELD
     YVADVVRSTF DEVIQEAGVK QDYQVGTMIE IPRAALTADQ LAETAEFFSF GTNDLTQMTF
     GFSRDDASKF LTDYYDKHVY ESDPFAHVDQ VGVGQLIQMA CEKGRSTRPD IHLGVCGEHG
     GDPASIKFFQ KVGLTYVSCS PYRVPIARLA AAQAAILEKQ
//
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