ID A0A1M6ETJ8_9CLOT Unreviewed; 874 AA.
AC A0A1M6ETJ8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMN02745176_01688 {ECO:0000313|EMBL:SHI88728.1};
OS Lutispora thermophila DSM 19022.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHI88728.1, ECO:0000313|Proteomes:UP000184442};
RN [1] {ECO:0000313|EMBL:SHI88728.1, ECO:0000313|Proteomes:UP000184442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19022 {ECO:0000313|EMBL:SHI88728.1,
RC ECO:0000313|Proteomes:UP000184442};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZS01000010; SHI88728.1; -; Genomic_DNA.
DR RefSeq; WP_073025775.1; NZ_FQZS01000010.1.
DR AlphaFoldDB; A0A1M6ETJ8; -.
DR STRING; 1122184.SAMN02745176_01688; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000184442; 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; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:SHI88728.1};
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:SHI88728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 62..294
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 302..355
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 421..502
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 517..868
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 454
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 830
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 744
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 744
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 765
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 767
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 768
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 768
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 874 AA; 97812 MW; 51BDF3E6784E5110 CRC64;
MKKLVYSFSE GKAEMKDLLG GKGANLAEMT NIGLPVPPGF TITTEACNMY YEKNEEIWPE
LIDEIFKKLS ELENKVGKRF GDKEKPLLVS VRSGAKFSMP GMMDTILNLG LNDVTVQAIH
RNTGNERFAY DSYRRFIQMF GDVVMTIEKY KFDSIFENIK EKYNAKYDTD LNAEALKEVV
EQYKELFKKE IGSEFPEDPR TQLVLAVKAV FRSWNNDRAK IYRKLNNIPD DLGTAVNVQS
MVFGNMGDDS GTGVAFTRNP ATGEKKLFGE FLVNAQGEDV VAGIRTPQSI EKLKEIMPDV
YEQFVKVAEL LENHYKDMQD IEFTIEKGKL YMLQTRNGKR TAFAAVKIAV DLVEEGKITK
EEAIMRVEPN QLDQLLHPTF DAEALKTIKP LAKGLPASPG AASGKIYFTA EAAVEAARQG
EKVILVRQET SPEDIEGMIE AQGILTARGG MTSHAAVVAR GMGKCCVAGC ESIKVNEQSK
KFVVDGRTFN EGDYISLDGS TGNVYEGIIE THEPELSGHF GKLMAWADEI RRLKVRTNAD
TPRDAAQAVK FGAEGIGLCR TEHMFFDESR IPAVREMIIA DSLEQRKAAL EKILPMQRED
FIGIFEAMGD RPVTIRLLDP PLHEFLPQSQ EDIKKLASDM KIDYDKLRAR VEELKEFNPM
LGHRGCRLVI TYPEIAEMQT RAIIEAAIHV KKSKGIDVKP EIMIPLIGDV KELAYIKNIV
VKVADDIIEE SGVELKYLYG TMIEIPRATL VADEIAKEAE FFSFGTNDLT QMTYGFSRDD
AGKFLKEYYD KKIFDKDPFQ AIDRKGVGKL MKMAVELGRG ERTNIKLGIC GEHGGEPSSV
EFCHMLGLDY VSCSPYRVPI ARLAAAQAAI SNRD
//
