PPDK_TREPA
ID PPDK_TREPA Reviewed; 901 AA.
AC O83728;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pyruvate, phosphate dikinase;
DE EC=2.7.9.1 {ECO:0000250|UniProtKB:P22983};
DE AltName: Full=Pyruvate, orthophosphate dikinase;
GN Name=ppdK; OrderedLocusNames=TP_0746;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC phosphate. {ECO:0000250|UniProtKB:P22983}.
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:0000250|UniProtKB:P22983};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P11155};
CC -!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
CC Inhibited by dark-induced phosphorylation. Both reactions are catalyzed
CC by PDRP1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi active site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate active site. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-440 in the dark inactivates the enzyme.
CC Dephosphorylation upon light stimulation reactivates the enzyme (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, each mediated
CC by a carrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
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DR EMBL; AE000520; AAC65714.1; -; Genomic_DNA.
DR PIR; G71286; G71286.
DR RefSeq; WP_010882191.1; NC_021490.2.
DR AlphaFoldDB; O83728; -.
DR SMR; O83728; -.
DR STRING; 243276.TPANIC_0746; -.
DR EnsemblBacteria; AAC65714; AAC65714; TP_0746.
DR KEGG; tpa:TP_0746; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_12; -.
DR OMA; HFFHEVG; -.
DR OrthoDB; 997616at2; -.
DR Proteomes; UP000000811; Chromosome.
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; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; PTHR22931; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..901
FT /note="Pyruvate, phosphate dikinase"
FT /id="PRO_0000147050"
FT REGION 1..321
FT /note="N-terminal"
FT REGION 322..380
FT /note="Linker 1"
FT REGION 381..482
FT /note="Central"
FT REGION 483..522
FT /note="Linker 2"
FT REGION 523..901
FT /note="C-terminal"
FT REGION 879..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 835
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 750
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 771
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 772
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 774
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 774
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 440
FT /note="Phosphoserine; by PDRP1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 901 AA; 100298 MW; E9463FE160781ACE CRC64;
MNIAKSIHFL SNKEALDKRL DRGLLGIRGR QADELSSLGL PVLPSVVIDA TVSRSLYGEK
LRSALSPYLR KFTLLNRKEY ADAKNPMLLK VVLSPNLAIS NYPVLHNFGL TRDTFAGFAE
RVGEHFATHE VFFLLKGVFG VLLGIAESEE NTKGASEFVE TLKEIEVFLQ GGKSSPSGRE
AMNRYRALLP DGFFDDAYVQ LEEAVRLVSK LLSFEEDGED GVAILIQPMV YGNYGGGSYS
GRFFSRNIIT GEKKLQGQYF EERFDECDAE GSDVNAIKPA YLKQLQDIAW KLEDHSREIR
EVRFTIEAGS LWLIEQKPVE AKSTISLVRL LLDLYEREVV DAEYVVKSVK PGQLNEILHP
VIDMTSVTGL KSSQGGIIGV PGAAVGRVYF TADSLIEAWR VAKMGGQDTR CILCMPATYA
GDVKAIEVAT GVLSNEGGYS AHASVVARQY GKISLVRPDM KIYSDKAVVD GMTINEGDFV
TLNVPYYGES TLYMGAAQLI EPDPETSGLV SFIELAKGFV RSFHVRANAD SPHDAELALA
FGAQGIGLCR TEHMFFKEDR INVFRRMIFS ENAEERTGSL KQLQKMQGED FYGIFKVMQG
HEVTIRLLDA PLHEFLPHGE SEVSKFLEYL EKVCGKGLSR EELQERISML SEVNPMLGHR
GCRIAISYPE IYAMQVRAVF EAVYRLQKEK ISVYPEIMIP IVMNCRELKQ IVYGKKIEGH
AYQGIGSIEE EVRLALKAKE VDYKVGAMIE LPAAALSADE IARYAQFFSF GTNDLTQTTL
GLSRDDFNTF MPDYTMYDLV DGNPFAILDA RVRELIEVAM QRGRLARPDI QLGLCGEHGS
RSENIRFCME VGLDYVSCSS YSVPIALLAI AQAEIENAEK EGRKPAWRGR SSAKSGGRRA
R
