ID A0A0N0MT22_9ACTN Unreviewed; 901 AA.
AC A0A0N0MT22;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=OK074_4478 {ECO:0000313|EMBL:KPI05559.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI05559.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI05559.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI05559.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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}.
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:KPI05559.1}.
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DR EMBL; LJCV01000262; KPI05559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0MT22; -.
DR PATRIC; fig|1592327.3.peg.6864; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
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; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KPI05559.1};
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:KPI05559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPI05559.1}.
FT DOMAIN 59..284
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 290..343
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 417..499
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 533..885
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 450
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 849
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 575
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 630
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 762
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 783
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 784
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 785
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 786
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 786
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 901 AA; 98293 MW; 40264909998D6928 CRC64;
MKFVYDFTEG NRDLKDLLGG KGANLAEMTN LGLPVPPGFT ITTEACKVYL DSGEEPAALR
DEVSAHLDAL EQRMGKRLGQ ADNPLLVSVR SGAKFSMPGM MDTVLNIGLS DKSVQGLAKQ
AGDERFAWDS YRRLIQMFGK TVLDVDGDLF EDALEAAKDA KKVSDDTQLE AADLKKLVTR
FKKIVKTEAG RDFPQDPREQ MDLAIKAVFD SWNGDRAKLY RRQERIPHDL GTAVNVCSMV
FGNLGPDSGT GVAFTRNPAS GHQGVYGDYL QNAQGEDVVA GIRNTVPLAQ LESIDKQSYD
QLTQIMETLE NHYLDLCDIE FTIERGQLWM LQTRVGKRTA GAAFRIATQL VDQGLIDEAE
ALQRVNGAQL AQLMFPRFDE QAKVDQIGRG IAASPGAAVG KAVFDSYTAI KWSRSGEKVI
LVRRETNPDD LDGMIAAEGI LTSRGGKTSH AAVVARGMGK TCVCGAEELE VDTKRRRLSA
PGGVVVEEGD VISIDGSSGK VYVGEVPVVP SPVVEYFEGR MHAGADDADE LVEAVHRIMA
FADRKRRLRV RANADNAEDA LRARRFGAQG IGLCRTEHMF LGDRRELVER LILADTEAER
EESLKELLPL QKQDFVELFE AMDGLPVTIR LLDPPLHEFL PDITELSVRV ALAESRQEPH
ENELRLLQAV HRLHEQNPML GLRGVRLGLV IPGLFTMQVR AIAEAAAERR AAKGDPRGEI
MIPLVGTVQE LEIVRDEADQ VIAEVQAATG TELKLAIGTM IELPRAALTA GQIAEAAEFF
SFGTNDLTQT VWGFSRDDVE ASFFTAYLEK GIFGVSPFET IDKDGVGSLV RSAVEAGRAT
RPNLKLGVCG EHGGDPESVH FFHEVGLDYV SCSPFRIPVA RLEAGRAASA AASSAVGSDH
R
//
