ID A0A0R2QS80_9ACTN Unreviewed; 787 AA.
AC A0A0R2QS80;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ABR78_07410 {ECO:0000313|EMBL:KRO51952.1};
OS Acidimicrobiia bacterium BACL6 MAG-120910-bin40.
OC Bacteria; Actinomycetota; Acidimicrobiia.
OX NCBI_TaxID=1655586 {ECO:0000313|EMBL:KRO51952.1, ECO:0000313|Proteomes:UP000050903};
RN [1] {ECO:0000313|EMBL:KRO51952.1, ECO:0000313|Proteomes:UP000050903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL6 MAG-120910-bin40 {ECO:0000313|EMBL:KRO51952.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO51952.1}.
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DR EMBL; LIBI01000169; KRO51952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QS80; -.
DR STRING; 1655586.ABR78_07410; -.
DR Proteomes; UP000050903; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KRO51952.1};
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:KRO51952.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRO51952.1}.
FT DOMAIN 81..176
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 190..236
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 311..390
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 411..777
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 344
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 739
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 652
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 652
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 673
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 674
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 675
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 676
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 676
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRO51952.1"
SQ SEQUENCE 787 AA; 85227 MW; 6F8D54D44F3CDA8B CRC64;
KSVVGLARTT NDERFSYDSY RRFISMYGRI VLGIDGAKFE HPFDDAKKTA GVKSDADLPA
SALKALCETY KQVVKAETGR EFPQDPMKQL RGAIEAVFRS WNGARAIAYR VREKISHDLG
TAVNVQAMVF GNRDNNSGTG VGFTRNAATG ENKPYGDFLV NAQGEDVVAG IRNTETLDDL
KRQFPAIHAE LMTIFDRLER HYKDMCDTEF TIDQGKLWML QTRVGKRTGA AALRMAVDMT
KPSGKGKAAW KISKKDALMR VAAEHLDQVL HPQFANKSKA LTKGLAASPG AAVGAVYFTA
DDAAAAAGRG EAVILVRSET SPEDVHGMMV AKGILTARGG LVSHAAVVAR GWGTPAIVGA
ESVHIDGKKF TVGDTVVREG DVISLDGTTG EVIIGAMMLA EAKPTKEFFT ILKWADEVRK
GKLAVRANAD TDEDAIKARE YGAEGIGLCR TEHMFLAPDR LPVVRRMILA STPAEETAAL
DELRKVQTED FAALLRAMSG LPVTVRLLDP PLHEFLPRVD ELEIKKATVG LSAEETKLIE
AARSWAEVNP MLGTRGVRLG VIKPGLYAMQ VRALLAAADI VASEGFSPIV EVMIPLTVTK
EELALARSWV EQEILDHSKQ IKSAPKSGAR KSIKNSIKNS KRPKVTIGTM IETPRAALVA
GELAEISDFF SFGTNDLTQM TFGFSRDDVE SRMMPAYLEA GLLKRNPFET IDQVGVGELV
QLAAKRGRKA KRGIKLGVCG EHGGDPESIG LFYRAGLDYV SCSPYRIPIA RLAAAQAIIG
GSKAETK
//
