ID E3ZRR8_LISSE Unreviewed; 716 AA.
AC E3ZRR8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
DE Flags: Fragment;
GN ORFNames=NT03LS_2196 {ECO:0000313|EMBL:EFR99676.1};
OS Listeria seeligeri FSL N1-067.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFR99676.1};
RN [1] {ECO:0000313|EMBL:EFR99676.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFR99676.1};
RX PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT characterized by limited gene acquisition and limited gene loss.";
RL BMC Genomics 11:688-688(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EFR99676.1}.
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DR EMBL; ADXJ01000765; EFR99676.1; -; Genomic_DNA.
DR RefSeq; WP_003748509.1; NZ_CM001051.1.
DR AlphaFoldDB; E3ZRR8; -.
DR PATRIC; fig|702453.3.peg.1825; -.
DR HOGENOM; CLU_385687_0_0_9; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000004302; Chromosome.
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; 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 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:EFR99676.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:EFR99676.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..136
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 140..187
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 260..340
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 357..705
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFR99676.1"
SQ SEQUENCE 716 AA; 79255 MW; BA331FB8A5E5AA4A CRC64;
NYLLDTELTA EDLSELVATY KTIFTQATGQ NFPQEPLEQL RLAIIAVFNS WMNPRAVIYR
RLNNIDASFG TAVNIQAMVF GNTGETSGTG ITFTRNPSTG EKAVFGEFLL NAQGEDVVAG
IRTPEPIKAL EKRMPIVYNE LIKTCELLEN HYLDMQDIEF TIEKEKLFIL QTRSGKRTAK
AAIQVAVDLV HEGKITKAEA LIRVETKQLD QLLHPTFVES ALKVGQVLAT GLPASPGAAT
GQIYFTAKEA VQAAERGISV ILVRNETSPE DIEGMAKSAA ILTAHGGMTS HAAVVARGMG
KCCIAGCSEL IINEKEKTII LKNGTQLHEG EQISLDGTSG KVYLGEIELT EAAIGGHFDE
LMTWADEEKQ LMIRVNADTP ADFKKALLFG AEGIGLCRTE HMFFDEKRIP YVRQMILAES
LAERESVLTT LKEMQKEDFT ALFRIADGRA VNIRLLDPPL HEFLPNTNRE IEQLASEMNR
TVPQLTKRIH SLAETNPMLG HRGSRLAITF PEIYRMQAEA IIESAVIVHD EGIAVHPEIM
IPLIATKSEL KYIKKEIKHA IHSIFDKERV VLPYDIGTMI EIPRACVTAD EIAEEAQFFS
FGTNDLTQLT YGFSRDDAAK FLSDYYEKNI LPNDPFVTID KEGVGALVEM AVTRGRMTHA
NLKMGVCGEH GGDPESIRFF HQLGLSYVSC SPYRVPIARL AAAQASLHEK EMLTTV
//
