ID A0A151EDG1_9EURY Unreviewed; 930 AA.
AC A0A151EDG1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
GN ORFNames=AYK23_02805 {ECO:0000313|EMBL:KYK26621.1};
OS Candidatus Proteinoplasmatales archaeon SG8-5.
OC Archaea; Euryarchaeota; Candidatus Proteinoplasmatales.
OX NCBI_TaxID=1803822 {ECO:0000313|EMBL:KYK26621.1, ECO:0000313|Proteomes:UP000075319};
RN [1] {ECO:0000313|Proteomes:UP000075319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL Submitted (FEB-2016) 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:KYK26621.1}.
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DR EMBL; LSSH01000091; KYK26621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151EDG1; -.
DR Proteomes; UP000075319; 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: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; 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:KYK26621.1};
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:KYK26621.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..53
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 62..292
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 300..357
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 420..501
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 517..915
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT BINDING 790
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 814
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
SQ SEQUENCE 930 AA; 103763 MW; D7516E3DA4F55231 CRC64;
MPDKYLYLFS EGRADMKELL GGKGANLAEM TRGGLSVPPG FTITTQACNF YREMKGRLPD
DMWNQVKEGL KTLEEQTGKR FGDPGKPLLL SVRSGALHSM PGMMDTILNL GLNKETVEGL
AKVSGNRRFA LDCYRRLIQM FSDVVLGIEL ENFEKQLLAL KRKLGITLDV ELDEHALDEL
VGTYKDIVRE HTGEDFPADP ETQLLMSVKA VFASWDNPRA KTYRMLNDIS DDLGTAVTVQ
AMVFGNIGES SATGVAFTRN PGTGNKEYYG EFLINAQGED VVAGIRTPKP VIEMESDMPA
QFEELKKVYH DLEAHYKDMQ DFEFTIEEGK LYILQTRTGK RTAQAAIKIA VDMVDEKLID
KKEAILMIDP NQIARLLHRR LDPKESVNPV GTGLPASPGA AVGRVVFHAD DAVAWNDRGE
EVILVREETK PDDIHGFFAA QGILTARGGK TSHAAVVARG MGKPCVSGCE DMDIDAKART
FRIGDVEVCE GDFITIDGTD GAVICGQIHT IAPDLSAEAE RVLKWADEIR ELGVWANAST
PEAARAALKF GAEGLGLCRT ERMFNAVDRL PIVVEMILAD SEEERKKSLD RLMPFQRDDF
VDIFRIMEPM PVVVRLLDIP LHEFLPSVEE LNTDVQNLTR FVDWIKSMRT LSGAVNMVGL
PDETQSVIHR LSKETEMLHE QEVAQKVLER KLTMLSKVRK MVEVNPMLGH RGVRLGITYP
EIYRMQMRAV CEAAALLIKE GKNIEPQIMI PQVCTTDELK WIYGQILEEK ILVEEETGVK
IPVLLGTMIE VVRACMRAGR IAEWADFFSF GTNDLTQACF SFSREDAENT FLPLYNERKV
LKHNPFEILD QKGVGRLMAI TVQWGRKTKP DLKIGICGEH GGEPNSIGFV HTINLDYVSC
SPYRVPVARF AAAQAALKEP EELSAIWGTY
//
