ID A0A124FR68_9BACT Unreviewed; 887 AA.
AC A0A124FR68;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=XD80_0971 {ECO:0000313|EMBL:KUK58207.1};
OS Synergistales bacterium 53_16.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK58207.1, ECO:0000313|Proteomes:UP000053116};
RN [1] {ECO:0000313|Proteomes:UP000053116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK58207.1}.
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DR EMBL; LGGB01000064; KUK58207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FR68; -.
DR PATRIC; fig|1635273.3.peg.696; -.
DR Proteomes; UP000053116; 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; 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; 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:KUK58207.1};
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:KUK58207.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..61
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 67..296
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 308..361
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 425..506
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 522..882
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 458
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 843
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 564
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 620
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 756
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 756
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 777
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 778
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 779
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"
SQ SEQUENCE 887 AA; 97793 MW; 5825934D26ED8EB5 CRC64;
MSEKAGNKKY IYNFREGRAD MKDLLGGKGA NLAEMLRIGL PVPPGFTITT EACLEFLEKR
ETFLEKLWPH VKEAVAEMER ETGKTFGGDK NPLLVSVRSG AAVSMPGMMD TILNLGLNDE
TVKVLAEASG DERFAYDSYR RFIQMYADVV LGIDGSLLDN VITQTKRSLG VKYDYEVTAE
AWKEVIDKFK RVVSKEKESA FPTDPWEQLK KAVVAVFDSW NTPRAKTYRK INRIPDNLGT
AVNVVTMVFG NLGDDCGTGV CFTRNPATGE KVLYGEFLTN AQGEDVVAGI RNPEPIADLE
KQMPEVYREL EEVASLLEKH YKDMQDIEFT IEKGKLYILQ TRSAKRTAKA AVNVAVDMYE
EGLIDAAVAV SRVTPDQVEQ LLHKQVDPEA TYEVLAKGLP ASPGAAVGEV VFDADEAEKL
GQSGKAVILV RPETTPDDIH GLFAAQGVLT SRGGMTSHAA VVARGIGKPC VSGCEAVQID
LDGQLMRVGE KVIRKGEILT IDGTRGEVIE GEVPLVQPSF SQEFRELLDL ADTISDLEVW
TNADTPEDAR KARGFGAKGI GLCRTEHMFM EAGRLPVMQE MIMADSKNAR IEALDKLKVM
QKEDFRGIFK AMEGLPVTIR LLDPPLHEFL PNEEELREKI ARLEREGKKD TPEYEKSKAT
LKRALSLREN NPMLGFRGCR LGMIYPEIYE MQIAAILEAA CELAAEGKKV IPDIMMPLVG
TQEEMRRLKT MVDRVAEKVF KECGTSVEYL VGTMIELPRA ALVAGPIAEY AEFFSFGTND
LTQTTFGYSR DDAEGKFLAQ YVTDGILADN PFHVLDREGV GRLMKIAVSD GRATRKDIQI
GICGEHGGNP PSIAFCHKLG LKYVSCSPYR VPVARLAAAQ AKLGLIG
//
