ID A0A0Q9BCR2_9ACTN Unreviewed; 915 AA.
AC A0A0Q9BCR2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASE41_02370 {ECO:0000313|EMBL:KRD24632.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD24632.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD24632.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD24632.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD24632.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD24632.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRD24632.1}.
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DR EMBL; LMIZ01000001; KRD24632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9BCR2; -.
DR STRING; 1736503.ASE41_02370; -.
DR Proteomes; UP000051177; 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:KRD24632.1};
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:KRD24632.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRD24632.1}.
FT DOMAIN 77..302
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 310..361
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 435..517
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 551..903
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 468
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 867
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 593
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 648
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 780
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 780
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 801
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 802
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 803
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 804
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 804
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 915 AA; 99803 MW; 0DE61A794D27EC8D CRC64;
MSENKDLHGA EQAASVEGVK FVYDFTEGNK ELKDLLGGKG ANLAEMTNLG LPVPPGFTIT
TEACKVYLDS GEEPAALRDE VSAHLVALED RMGKKLGQAD DPLLVSVRSG AKFSMPGMMD
TVLNIGLSDK SVQGLAEQAG DARFAWDSYR RLIQMFGKTV LGVDGELFED ALEAAKKAKK
VAVDTELEAA DLKKLVTRFK KIVKTEAGRD FPQDPREQMD LAIKAVFESW NGDRAKLYRR
QERIPGDLGT AVNVCSMVFG NLGPDSGTGV AFTRDPASGH QGVYGDYLQN AQGEDVVAGI
RNTVPLAELE QIDKKSYDQL LGIMETLENH YKDLCDIEFT IERGHLWMLQ TRVGKRTAGA
AFRIATQLVD QGLIDETEAL QRVNGAQLAQ LMFPRFDEDA KVEKVGRGIA ASPGAAVGKA
VFDSYTAVKW SRSGEKVILV RRETNPDDLD GMIAAEGILT SRGGKTSHAA VVARGMGKTC
VCGAEELEVD TKRRRMTVPG GHVVEEGDVI SIDGSSGKVY LGEVPVVPSP VVEYFEGRMH
AGADDADELV EAVHRIMAFA DRKRRLRVRA NADNAEDALR ARRFGAQGIG LCRTEHMFLG
DRREQVERLI LADTQEEREE SLKQLLPLQK KDFVELFEAM DGLPVTVRLL DPPLHEFLPD
ITELSVRVAL AESRQESHEN DLRLLQAVHR LHEQNPMLGL RGVRLGLVIP GLFTMQVRAI
AEAAAERRNA KGDPRAEIMI PLVGTVQELE IVREEADQVI AEVEAATGVE LKLAIGTMIE
LPRAALTAGQ IAEAAEFFSF GTNDLTQTVW GFSRDDVEAS FFTAYLEKGI FGVSPFETID
RDGVGSLVKS AAEAGRATRP DLKLGVCGEH GGDPESVHFF HEVGLDYVSC SPFRIPVARL
EAGRAATQSA GSDHR
//
