ID A0A1I0R9N9_9FIRM Unreviewed; 878 AA.
AC A0A1I0R9N9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05216413_2588 {ECO:0000313|EMBL:SEW37499.1};
OS Ruminococcaceae bacterium KH2T8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1855400 {ECO:0000313|EMBL:SEW37499.1, ECO:0000313|Proteomes:UP000198503};
RN [1] {ECO:0000313|EMBL:SEW37499.1, ECO:0000313|Proteomes:UP000198503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2T8 {ECO:0000313|EMBL:SEW37499.1,
RC ECO:0000313|Proteomes:UP000198503};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOIY01000006; SEW37499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0R9N9; -.
DR STRING; 1855400.SAMN05216413_2588; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000198503; 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; 3.
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:SEW37499.1};
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:SEW37499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198503};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..72
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 77..291
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 306..358
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 424..505
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 522..872
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 457
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 834
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 563
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 619
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 748
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 771
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 772
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 878 AA; 96357 MW; CD046E6C502A5449 CRC64;
MTKYVYMFTE GNGSMRELLG GKGANLAEMT KIGLPVPQGF TITTEACTKY YEDGRKINDE
IMAQAMAGVD EMEKINGKKF GDLKNPLLVS VRSGARASMP GMMDTILNLG LNDEVVAAMI
AGNPDPAFER FVYDSYRRFI QMFSDVVMEV GKKYFEQLID KMKEEKGVEF DVELTAADLK
TLAEQFKAEY KNQIGEDFPS DPVVQLKLAI EAVFKSWDNP RANVYRRDND IPYSWGTAVN
VMPMVFGNLN NESGTGVAFT RDPGTGENKL MGEFLINAQG EDVVAGVRTP MPIAQMEEEF
PEAYAEFIKV CDILENHYHD MQDMEFTVEN KKLYMLQCRN GKRTAQAALQ IAVDLVKEGH
KTEAEAVAMI DPRNLDTLLH PQFDLAAIKA ANAAGKGLGA SPGAACGKVV FTADDAVEWA
GRGEKVILVR LETSPEDITG MKAAQGILTV RGGMTSHAAV VARGMGTCCV SGCGDINMDE
ENKKFTLAGK TYNEGDFISI DGSTGNIYDG IIPTVDAKID GNFGTVMAWA DKYRRLKVRT
NADTPADAKR ARELGAEGIG LCRTEHMFFE EDRIAAFREM ICSDTVEERE AALDKILPYQ
QGDFKALYEA LEGYPVTIRF LDPPLHEFVP TDEADIKKLA DSQGKPVEDI KALIASLHEF
NPMMGHRGCR LAVTYPEIAK MQTKAVIRAA LEVKAAHPDW DIKPEIMIPL VCEIKELAFV
KKVVVETADA EIAASGVALE YSVGTMIEIP RAALTADEIA KEAEFFCFGT NDLTQMTYGF
SRDDAGKFLP AYYDTKIFES DPFVKLDQTG VGKLMEMAIK LGKPVNPDLH VGICGEHGGD
PSSVEFCDAI GLDYVSCSPF RVPIARLAAA QASIKHQG
//
