ID Q73PF5_TREDE Unreviewed; 935 AA.
AC Q73PF5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 OrderedLocusNames=TDE_0844 {ECO:0000313|EMBL:AAS11335.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS11335.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS11335.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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}.
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DR EMBL; AE017226; AAS11335.1; -; Genomic_DNA.
DR RefSeq; NP_971454.1; NC_002967.9.
DR RefSeq; WP_002682103.1; NC_002967.9.
DR AlphaFoldDB; Q73PF5; -.
DR STRING; 243275.TDE_0844; -.
DR PaxDb; 243275-TDE_0844; -.
DR GeneID; 2739621; -.
DR KEGG; tde:TDE_0844; -.
DR PATRIC; fig|243275.7.peg.813; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_12; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000008212; 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; 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.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAS11335.1};
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:AAS11335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008212};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 408..482
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 522..873
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 883..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..168
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 921..935
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 834
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 749
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 770
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 935 AA; 103781 MW; ECADA8CF50E98575 CRC64;
MKISNNIHFF NSKEIVGKKV DKNLLGIRGR QANEFAELKL PILPGIIIDA SVAQDLGDIK
IYSEISPYLS KFGSEVKKTY GDAGSPLLLK LVISPNMLIT SYPTLHNFGL TKDTVIGFQE
NVGEDFAANE VLFLLNGILT VVLKIEELEK NEQKVKDLEK ALHDIKESMK MGKIGLKPGA
IMDKYSKFLP KHFFDDCKVQ LEESIRLIAR LLTLEEDSDH DVALLIQPMV YGNYSKDSYS
GSFFSRNIVN GEKKLQGQFF AEKFNEVNAE GKDINSIKPE YLKHLQQIAW QLEDYTKDIR
NIRFTIEAGR LWLIEQKSVE AKSTISMVQI LLDLYNRKIV DAEYVVRAVK PGQLNEILHP
VIDIMSTKGM KSSKGGIAGA PGAAVGRVYF TADSLIEAQR AAKLQGLDTR CILCMPATYA
GDVKGIEVST GVISNEGGYS AHASVVARQY GKISLVRPDM KISGNKAVIE GVTINEGDYI
TLNVPYYGDS TVYFGEAKLI EPDPETSGLL DFIGLAKSFL SNFHVRANAD SPRDAQLALD
FGAEGIGLCR TEHMFFNEKR INTFREMILA PSEAERKKVL DKLQKVQTED FYGIFKAMNG
KEVTIRLLDA PLHEFLPHND LELDGFVKYL TAQKKKVSKK DLTAEIEKLS EINPMLGHRG
CRIAISYPEI YAMQIRAIFE AAYKLKKEKV DVKPEIMIPL IMNFRELKQI IYGKKIEGHT
YLGIDAIAEE VKAAVKGGDL DYKVGTMIEL PASALSADEI AKYAQFFSFG TNDLTQTTLG
LSRDDFNSFM PDYTMYDLID GNPFAVLDSR VRDLIEIAIQ RGKLTRPDLH LGLCGEHGAR
PENVRFCMDA GLDYVSCSSY SVPIALLSIA QAELENAEKA GIKLEPKAHV SRKPSSAAPK
SAAKKQAPEK KAVKAKPASA KKASSAKKKT AKKSK
//
