ID X8HEU1_9FUSO Unreviewed; 851 AA.
AC X8HEU1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00020138};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE AltName: Full=Pyruvate, orthophosphate dikinase {ECO:0000256|ARBA:ARBA00032883};
GN Name=ppdK {ECO:0000313|EMBL:EUB27164.1};
GN ORFNames=HMPREF1500_2159 {ECO:0000313|EMBL:EUB27164.1};
OS Fusobacterium sp. CM22.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=936563 {ECO:0000313|EMBL:EUB27164.1, ECO:0000313|Proteomes:UP000020631};
RN [1] {ECO:0000313|EMBL:EUB27164.1, ECO:0000313|Proteomes:UP000020631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM22 {ECO:0000313|EMBL:EUB27164.1,
RC ECO:0000313|Proteomes:UP000020631};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB27164.1}.
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DR EMBL; JAQC01000014; EUB27164.1; -; Genomic_DNA.
DR RefSeq; WP_032846306.1; NZ_JAQC01000014.1.
DR AlphaFoldDB; X8HEU1; -.
DR PATRIC; fig|936563.3.peg.534; -.
DR Proteomes; UP000020631; Unassembled WGS sequence.
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; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:EUB27164.1};
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:EUB27164.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EUB27164.1}.
FT DOMAIN 16..276
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 284..336
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 397..480
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 497..844
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 608..635
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 432
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 807
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 538
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 594
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 721
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 742
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 743
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 744
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"
SQ SEQUENCE 851 AA; 95921 MW; 5E3D08F15B033BE3 CRC64;
MKQVYEFKDG GKEMVALLGG KGANLAEMAK IDLPIPKGII ISTTACNDYF KNDKKLSFVL
EEEILRNIRV LEYETGKKFQ SAKPLLVSVR SGAPVSMPGM MDTILNLGFN DYVAEKMLEI
TKDEKFVYTS YLRFVQMFSE IAKGINRKKF MHLKATDYKA QIIESKNIYR EECGEMFPEN
YKAQILIAVK SIFDSWNNDR AILYRKLHNI DNNMGTAVVI QEMVFGNFND KSGTGVLFTR
NPSTGENKIF GEVLLNAQGE DIVAGIRTPD NIELLKISMP NIYNELVDTV KRLEKHNRDM
QDVEFTIEDS KLYILQTRNG KRTAEASLKI AMDLVNEGII TKEEAILKVE PASINKLLNG
DFEEKYLKEA TLLTKGLAAS SGVAVGRIMF DAKRVKIREK TILVREETSP EDLQGMALAQ
GIVTLKGGAT SHGAVVARGM GKCCVTGCSE IKIDEVNKTM TVGKYTLKEG DFISVSGHTG
EIYLGKIPLK ENSFSDELKE FVSWAIEIKR MGVRMNADTP EDVEQGKAFG AKGIGLCRTE
HMFFKKDKIW TIREFILSDR GGEKEKALEK LHNLQKEDFL NIFKVLDGDE ANIRLLDPPV
HEFLPKTLED KKKMAEILSI SLEDIEKRIY RLKDENPMLG HRGCRLGVSY PELYRIQARA
IVEAAYECEK KGIKVHPEIM IPFIMESKEL AYLRKEIEEE IESFFKEVGA TVEYKLGTMI
EIPRACLLAD EIAEYADFFS FGTNDLTQMS MGLSRDDSVK FLDDYREKGI WEGEPFYSID
TKAVTKLVEI GVKNGKSAKP NLQIGVCGEH GGDPKSIEFF EGQKFDYVSC SPFRVPTAIL
AAAQSYLKLK K
//
