ID U7SSU0_FUSNU Unreviewed; 851 AA.
AC U7SSU0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=HMPREF1766_01376 {ECO:0000313|EMBL:ERT35318.1};
OS Fusobacterium nucleatum CTI-5.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=1316586 {ECO:0000313|EMBL:ERT35318.1, ECO:0000313|Proteomes:UP000017135};
RN [1] {ECO:0000313|EMBL:ERT35318.1, ECO:0000313|Proteomes:UP000017135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTI-5 {ECO:0000313|EMBL:ERT35318.1,
RC ECO:0000313|Proteomes:UP000017135};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kostic A., Garrett W.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium nucleatum CTI-5.";
RL Submitted (OCT-2013) 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:ERT35318.1}.
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DR EMBL; AXNW01000019; ERT35318.1; -; Genomic_DNA.
DR RefSeq; WP_023039042.1; NZ_KI518374.1.
DR AlphaFoldDB; U7SSU0; -.
DR PATRIC; fig|1316586.3.peg.1342; -.
DR HOGENOM; CLU_015345_0_2_0; -.
DR Proteomes; UP000017135; 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 Kinase {ECO:0000313|EMBL:ERT35318.1};
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:ERT35318.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 57..279
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 284..337
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 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; 95972 MW; B3DFE49B5A9F1393 CRC64;
MKQVYEFKDG GKEMVALLGG KGANLAEMAK INLPIPKGII ISTTACNEYF KNDKKLSTVL
EEEILTNIRV LEYETGKKFQ STKPLLVSVR SGAPVSMPGM MDTILNLGFN DYVAEKMLEI
TKDEKFVYTS YLRFVQMFSE IAKGINRKKF MHLKATDYKA QIIESKNIYR EECGEIFPEN
YKDQILIAVK SIFDSWNNDR AILYRKLHNI DNNMGTAVVI QEMVFGNFND KSGTGVLFTR
NPSTGENKIF GEVLLNAQGE DIVAGIRTPE NIELLKNSMP NIYNELVDTV KKLEKHNRDM
QDVEFTIENS KLYILQTRNG KRTAEASLKI AMDLVKEGII TKEEAILKVE PASINKLLNG
DFEEKYLKEA TLLTKGLAAS SGVAVGRIMF DAKRVKIREK TILVREETSP EDLQGMALAQ
GIVTLKGGAT SHGAVVARGM GKCCVTGCSE IKIDEINKTM TVGKYTLKEG DFISVSGHTG
EIYLGKIPLK ENSFSDELKE FVSWASEIKR MGVRMNADTP EDVEQGKAFG AKGIGLCRTE
HMFFKHNKIW TIREFILSDR GEEKEKALKK LHNLQKEDFL NIFKILNGDE ANIRLLDPPV
HEFLPKTLED KEKMAEILSI SLEAVEKRIY RLKDENPMLG HRGCRLGVSY PELYRIQARA
IIEAAYECAK KGIKVHPEIM IPFIMEAKEL AYLRKEIEEE IESFFKEVGE KVEYKLGTMI
EIPRACLLAN EIAEYADFFS FGTNDLTQMS MGLSRDDSVK FLDDYREKGI WEGEPFYSID
TKAVTKLVEI GVKNGKSTKH NLQIGVCGEH GGDPKSIEFF EGQKLDYVSC SPFRVPTAIL
AAAQSYLKLK K
//
