ID A0A1M4S966_9BACE Unreviewed; 906 AA.
AC A0A1M4S966;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN05444405_10129 {ECO:0000313|EMBL:SHE28749.1};
OS Bacteroides luti.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHE28749.1, ECO:0000313|Proteomes:UP000184509};
RN [1] {ECO:0000313|EMBL:SHE28749.1, ECO:0000313|Proteomes:UP000184509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26991 {ECO:0000313|EMBL:SHE28749.1,
RC ECO:0000313|Proteomes:UP000184509};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQTV01000001; SHE28749.1; -; Genomic_DNA.
DR RefSeq; WP_073398476.1; NZ_FQTV01000001.1.
DR AlphaFoldDB; A0A1M4S966; -.
DR STRING; 1297750.SAMN05444405_10129; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000184509; 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; 1.
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:SHE28749.1};
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:SHE28749.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184509};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..390
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 457..537
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 552..902
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 489
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 864
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 595
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 651
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 778
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 778
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 799
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 800
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 802
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 906 AA; 99717 MW; 1F7F641E119C8A9B CRC64;
MDKKRVYTFG NGQAEGKAEM KNLLGGKGAN LAEMNLIGVP VPPGFTITTE VCSEYYELGR
DKVVDLLKED VEKSVAKVEA LMKSKFGDVE NPLLVSVRSG ARASMPGMMD TILNLGLNDE
VVEGLTRKTG NARFAWDSYR RFVQMYGDVV LGMKPTNKED IDPFEAIIEE VKESKGVKLD
NELEVEDLKV LVKKFKEAVK KQTGHDFPTC AYEQLWGAIC AVFDSWMNER AILYRKMEGI
PAEWGTAVSV QAMVFGNMGE TSATGVCFSR DAGTGEDLFN GEYLINAQGE DVVAGIRTPQ
QITKIGSQRW AELAGIPEDV RAAKYPSMEE AMPEIYKELD EIQTRLENHY RDMQDMEFTV
QEGKLWFLQT RNGKRTGAAM VKIAMDLLRQ GMIDEKTALK RVEPNKLDEL LHPVFDKAAL
KNAKVIAKGL PASPGAATGQ IVFFADDAAK WHADGHKVVM VRIETSPEDL AGMAVAQGIL
TARGGMTSHA AVVARGMGKC CVSGAGALSI DYKSRTLEVG GVTLKEGDYI SINGSTGEVY
EGKVATRAAE LSGDFADLMA LADKYTRMKV RTNADTPHDA EVARKFGAIG IGLCRTEHMF
FEGEKIKAMR EMILAENEEG RKIALAKILP YQKADFKGIF KAMEGCPVTV RLLDPPLHEF
VPHDEKGQQE MADAMGVSFK HIQQRVEALH EQNPMLGHRG CRLGNTYPEI TRMQTRAILG
AALELKKEGV ETFPEIMVPL TGLLPEFKEQ ENVIREEAAA LFAEMGDSID YKVGTMIEIP
RAALTAERIA QGAEFFSFGT NDLTQMTFGY SRDDVASFLP IYLEKKILQV DPFQVLDQNG
VGQLVRMATE KGRSVRPDLK CGICGEHGGE PSSVKFCHRV GLNYVSCSPF RVPIARLAAA
QAAIEE
//
