ID A0A1D7XI68_9CLOT Unreviewed; 875 AA.
AC A0A1D7XI68;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=BGI42_04355 {ECO:0000313|EMBL:AOR22996.1};
OS Clostridium taeniosporum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR22996.1, ECO:0000313|Proteomes:UP000094652};
RN [1] {ECO:0000313|Proteomes:UP000094652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RA Walker J.R.;
RT "Genomics of Clostridium taeniosporum, an organism which forms endospores
RT with ribbon-like appendages.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; CP017253; AOR22996.1; -; Genomic_DNA.
DR RefSeq; WP_069679151.1; NZ_CP017253.2.
DR AlphaFoldDB; A0A1D7XI68; -.
DR STRING; 394958.BGI42_04355; -.
DR KEGG; ctae:BGI42_04355; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000094652; 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; 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:AOR22996.1};
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:AOR22996.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094652};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..292
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 303..354
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 422..503
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 519..870
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 455
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 831
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 745
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 768
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 769
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 875 AA; 97343 MW; 6FCB532E21CFAB21 CRC64;
MTKKYVYLFN EGNASMRNLL GGKGANLAEM TNLGIPVPYG FTVTTEACNK YYEDGKTIAD
EIINEIYNSL QKLESVSGKE FGSNKNPLLV SVRSGARTSM PGMMDTILNL GLNDEVVESM
ATLTNNPRFA YDSYRRFIQM FSDVVMGIEN RLFENKIEEL KDKKGVEFDT ELDQNDLKVL
VSEFKAIYKK EKGEEFPQEP KTQLIEAVTA VFRSWNNPRA IVYRRLNDIP GEWGTAVNVQ
EMVFGNKGET SGTGVVFSRN PATGENFIYG EYLMNAQGED VVAGIRTPLP ISKLKEQDVK
IYNQLVGIIE KLENHYKDMQ DMEITIEEGK LYFLQTRNGK RTAQAALKIA VDLYNSGMLT
KEEAVLKVEP KQLDTLLHPT FYTEALKKAV SIAKGLPASP GAACGKIAFT AEEAKDRAAL
GEDVILVRLE TSPEDIEGMV AAKGILTVRG GMTSHAAVVA RGMGTCCVAG CGTIKVDEAK
KTLTVGDKVY TSDDFISIDG TSGNVYGEKI KTVVPEISGH FATFMSWADE IRKLKIRANA
DTPKDAKQAV EFGAEGIGLC RTEHMFFAED RIMAVRQMIT AKDEEQRRVA LAKILPMQRG
DFIGIYEALE ERPVTIRLLD PPLHEFLPNN EQDIKMLAKE IGLTFEELKL TVDNLHEFNP
MMGHRGCRLA VSYPEIAEMQ TRAIIEAAIE VKTNKGYNII PEIMIPLIGD LKELKYVKDT
IKNTAEKVIK EKNIDLQYKI GTMIEIPRAA LTADEVAKEA EFFSFGTNDL TQMTFGFSRD
DASKFLTDYY DKKIYEQDPF AKLDRDGVGA LIKIATEKGR ETRPNIKLGI CGEHGGDPSS
IEFCHDIGLN YVSCSPFRVP LARLAAAQAQ VKNSR
//
