ID A0A0H3J8R3_CLOPA Unreviewed; 876 AA.
AC A0A0H3J8R3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AJA52351.1};
GN ORFNames=CLPA_c22930 {ECO:0000313|EMBL:AJA52351.1}, CP6013_00886
GN {ECO:0000313|EMBL:KRU11639.1};
OS Clostridium pasteurianum DSM 525 = ATCC 6013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA52351.1, ECO:0000313|Proteomes:UP000030905};
RN [1] {ECO:0000313|EMBL:AJA52351.1, ECO:0000313|Proteomes:UP000030905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 525 {ECO:0000313|EMBL:AJA52351.1}, and DSM 525 / ATCC 6013
RC {ECO:0000313|Proteomes:UP000030905};
RX PubMed=25700415;
RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT Clostridium pasteurianum DSM 525.";
RL Genome Announc. 3:e01591-e01514(2015).
RN [2] {ECO:0000313|EMBL:KRU11639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11639.1};
RA Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KRU11639.1, ECO:0000313|Proteomes:UP000028042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11639.1,
RC ECO:0000313|Proteomes:UP000028042};
RX PubMed=25103768;
RA Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Genome Announc. 2:0-0(0).
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; CP009268; AJA52351.1; -; Genomic_DNA.
DR EMBL; JPGY02000001; KRU11639.1; -; Genomic_DNA.
DR RefSeq; WP_003441575.1; NZ_JPGY02000001.1.
DR AlphaFoldDB; A0A0H3J8R3; -.
DR GeneID; 76626692; -.
DR KEGG; cpae:CPAST_c22930; -.
DR KEGG; cpat:CLPA_c22930; -.
DR PATRIC; fig|1262449.3.peg.697; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR Proteomes; UP000028042; Unassembled WGS sequence.
DR Proteomes; UP000030905; 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:AJA52351.1};
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:AJA52351.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030905};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AJA52351.1}.
FT DOMAIN 19..298
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 423..504
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 520..871
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 456
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 832
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 618
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 746
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="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 876 AA; 97761 MW; 44AE21ADCB08D0ED CRC64;
MENKKYVYLF SEGNAKMRNL LGGKGANLAE MTRLGIPVPQ GFTVSTDACL KYYKNGEKIS
EDIIEQINNS IEDLEKITGK HFGISDNPLL LSVRSGARVS MPGMMDTILN LGLNDVTVEK
IAALTKNPRF AYDSYRRFIQ MFSDVVMGIE KRKFEDLIDK AKGEKEVKYD IELDENDLKK
LALGFKKLYE REIGKPFPDN PKEQLIESIT AVFRSWNNPR AIVYRRLNDI PGEWGTAVNV
QAMVFGNMGS NSGTGVAFTR NPATGENKIF GEYLINAQGE DVVAGIRTPE PIAKLKEDLP
ECYEEFINTA HRLENHYRDM QDMEFTIEQG KLYFLQTRNG KRTAQSALKI AVDMVNERAI
TKEQAILKVE PRQLETLLHP AFDAEDIKKA KVIAKGLPAS PGAACGKVYF TAEEAKKHHE
KGEKVILVRL ETSPEDIEGM VAAEGILTIR GGMTSHAAVV ARGMGTCCVA GCGSISIDEE
KKVFKVQGKE YIEGDYISLD GSTGNVYGGA VKTTLPAVSG NFEIFMKWAD GIKKLQVRTN
ADTPKDAKEA IKFGAKGIGL CRTEHMFFEV DRIPAVREMI VASTVEQRKR ALDKLLPMQR
EDFIGIYEAM EGNPVTVRFL DPPLHEFLPS EEMDIENLSK EMNIDLQDLK ATITSLHEFN
PMMGHRGCRL SVSYPEIAEM QTRAVIEAAL YVNKTKKLNI IPEIMIPLVG EIKELKFVKD
IVVKTAEEII NKSGEELKYQ VGTMIEIPRA ALTADEIAKE AEFFSFGTND LTQMTFGFSR
DDAGKFLSYY YDNKIYEFDP FEKLDQIGVG KLIKMAVELG KKTRPDIHLG ICGEHGGDPS
SVEFCHNVGL DYVSCSPFRV PLARLAAAQA QVKNPR
//
