ID K4LDF7_THEPS Unreviewed; 886 AA.
AC K4LDF7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AFV10818.1};
GN OrderedLocusNames=Tph_c05800 {ECO:0000313|EMBL:AFV10818.1};
OS Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermacetogenium.
OX NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV10818.1, ECO:0000313|Proteomes:UP000000467};
RN [1] {ECO:0000313|EMBL:AFV10818.1, ECO:0000313|Proteomes:UP000000467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC {ECO:0000313|Proteomes:UP000000467};
RX PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA Schink B.;
RT "Genome-guided analysis of physiological and morphological traits of the
RT fermentative acetate oxidizer Thermacetogenium phaeum.";
RL BMC Genomics 13:723-723(2012).
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; CP003732; AFV10818.1; -; Genomic_DNA.
DR AlphaFoldDB; K4LDF7; -.
DR STRING; 1089553.Tph_c05800; -.
DR KEGG; tpz:Tph_c05800; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_9; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000000467; 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:AFV10818.1};
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:AFV10818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFV10818.1}.
FT DOMAIN 18..53
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 55..291
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 302..355
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 419..500
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 518..875
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 452
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 558
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 614
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 886 AA; 97654 MW; B71EDAD482C9955F CRC64;
MGRKYVYLFE EGNASMRDLL GGKGAGLAEM TNLGLPVPPG FTITTEACNE YSATGRFPDG
LEEQIRDALK VLEEKTGKTF GGLENPLLVS VRSGAKVSMP GMMDTVLNLG LNDRTVRALS
GVTGDERFAL DCYRRFIQMF GDIVLHVDFN GFESILEKHK KQHRARYDHE LKPEHLKEII
KEYKNLIREK VREEFPQDPF EQLNRAVRAV FESWNNPRAQ VYRKVNRIPD DLGTAVNVQT
MVFGNMGDNS GTGVAFTRDP ATGESTLYGE YLVNAQGEDV VAGIRTPHPI ARLQEEMPGA
YEQFQKTCSL LEKHYRDMQD IEFTIEKGKL YILQTRSAKR TAAAAVKVAV DMVKEGLISK
EEAVMRVEPA QLNQVLHKRL DPRAEIRVIA TGLPASPGAA CGAVVFDADE AERRGNEGEK
VILVRLETTP DDIHGVVAAQ GVLTSRGGMT SHAAVVARGM GKPCVCGCEA LSIDYREKRM
TVGDLVIGEG DLITIDGSTG KVIMGAVPLI SPELGEELRL LLRWADEIRK LGVLANADTP
DDARRARDFG AEGIGLCRTE HMFMSQDRLP IVQRMILARS AEERGEALAK LLPVQQEDFY
GILKAMDGLP VIIRLLDPPL HEFLPKVEEL AVEVNTLKLS GGASEEIAAK EELLKKARSL
QEFNPMLGHR GCRLAVTTPE IYAMQVRAIV QAAVQLKKEG YNPVAEIMIP LVMSPKELEI
MRGLCMEVIR QVEEETGVRL EIPIGTMIEL PRACLLADEI GKHADFFSFG TNDLTQTTFG
FSRDDAEGKF IPQYIEKKIL PDNPFAVLDR DGVGKLVKMG VELGRGANPK LVVGICGEHG
GDPDSIEFCH LAGLDYVSCS PFRVPVARLA AAQAQVKNPR SAKRKK
//
