ID A0A1E7KFG9_9ACTN Unreviewed; 902 AA.
AC A0A1E7KFG9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AN216_14420 {ECO:0000313|EMBL:OEV02679.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEV02679.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEV02679.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEV02679.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV02679.1}.
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DR EMBL; LJGU01000127; OEV02679.1; -; Genomic_DNA.
DR RefSeq; WP_070197056.1; NZ_LJGU01000127.1.
DR AlphaFoldDB; A0A1E7KFG9; -.
DR STRING; 1075402.AN216_14420; -.
DR PATRIC; fig|1075402.3.peg.1784; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000176101; 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:OEV02679.1};
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:OEV02679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000176101};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OEV02679.1}.
FT DOMAIN 69..294
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 303..356
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 427..509
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 543..895
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 460
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 860
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 585
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 640
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 795
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 796
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 797
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 902 AA; 98425 MW; 070DB691F7E00A2B CRC64;
MSEHAEKPAS EKFVYDFAEG NKDLKELLGG KGANLAEMTN LGLPVPPGFT ITTEACRRYL
DSGAQPTALR DEVGSHLAAL EQRMGKKLGQ ADDPLLVSVR SGAKFSMPGM MDTVLNIGLS
DDSVHGLAGQ AGDERFAWDS YRRLIQMFGE TVLGIDGELF SGALEAARNR HDAASDVELS
AEQLRELVEE FKGIVTRETG RDFPQEAREQ MDLAVRAVFD SWNGARARLY RRQERIPHDL
GTAVNICSMV FGNLGPDSGT GVAFTRDPAS GQQGVYGDYL QNAQGEDVVA GIRNTVPLAE
LERLDKPSYD RLLDIMETLE THYKDLCDIE FTIERGTLWM LQTRVGKRTA AAAFRIATQL
VDQGVIDEAE ALQRVNGTQL AQLMFPRFAS EARTDTIGRG IAASPGAAVG KAVFDSYTAI
KWSRSGERVI LVRRETNPDD LDGMLAAEGI LTSRGGKTSH AAVVARGMGK TCVCGAEELE
VDTKRRQLTT AAGTVVEEGD TLSIDGSSGR VYLGEVPVVP SPVVEYFEGR THAGADDADE
LVRAVHRIMA YADRMRRLRV RANADNAEDA LRARRFGAQG IGLCRTEHMF LGERREMVER
LILADTGSER DSALTGLLPQ QRQDFVELFE AMDGLPVTVR LLDPPLHEFL PDITELSVRV
ALAESRQDHN ENDLRLLQAV HRLHEQNPML GLRGVRLGLV IPGLFTMQVR AIAEAAAERR
VASGGDPRVE IMIPLVGTVQ ELELVRDDAE RVIAEVEETY GTELHLALGT MIELPRAALT
ADQIAESADF FSFGTNDLTQ TVWGFSRDDV EASFFTAYLE KGIFGVSPFE TIDKDGVGSL
VRDAVRAGRA TRPDLKLGVC GEHGGDPESV HFFHEAGLDY VSCSPFRIPV ARLEAGRAAA
AG
//
