ID A0A101WVR4_9CREN Unreviewed; 893 AA.
AC A0A101WVR4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
GN ORFNames=AT718_10570 {ECO:0000313|EMBL:KUO80130.1};
OS Vulcanisaeta sp. JCHS_4.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1714253 {ECO:0000313|EMBL:KUO80130.1, ECO:0000313|Proteomes:UP000054689};
RN [1] {ECO:0000313|EMBL:KUO80130.1, ECO:0000313|Proteomes:UP000054689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (OCT-2015) 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:KUO80130.1}.
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DR EMBL; LOCE01000074; KUO80130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WVR4; -.
DR STRING; 1714253.AT718_10570; -.
DR Proteomes; UP000054689; 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; 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; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KUO80130.1};
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:KUO80130.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..298
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 305..360
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 423..504
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 528..879
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
SQ SEQUENCE 893 AA; 99672 MW; 0D3459ED7ACB0260 CRC64;
MGSLGRYVLT FEEADPDDVK LIGGKASSLV LMTRLGLPVP PGIIITTKAC REYFDGGERL
PDGLMDEVAK GIKYLEERTG LKLGDPENPL LVSVRSGAAV SMPGMMDTVL NVGLNDRTVH
GLAKRINNEH GAYDAYRRFL AMFGRIVLGI PEEEFNKPLD EVKRKYGVKE DPEIPLEGFK
ELIEIYKQVY IRRFGKVFDD PWEQLRLSIE AVFKSWNSPR ARFYREANKI TPDIADCTAT
AIVTMVFGNA DWRSATGVVF SRDPATGEDK LYGEYLPYAQ GEDVVAGIRT PKLVEKLKEE
MPEVYEQLYR GVKLIEKTKK EVQDVEFTIE KGKLWFLQTR NAKMNPMAVV KTSVDMYKEG
MLTKEEAIMR VKPEYILQML YPRIDESKAG KPLTKGIAAS PGAVSGQAVF DPDRAVEWAK
AGRQVILVRE ETKPDDVHGF YASVGVLTSR GGATSHAAVV ARAIGRPAVV GAEALQIDYS
TRTARVGDVV IKEGDWVTID GFTGNVYAGK VPTIEPKLPP EFFEFLDMAD SVSVFEVRAN
ADTPDDASIS RRFGAKGIGL LRTERMFRAP GRLDLFRKVI LSDNPSERRE LLDQLAEMMK
RDFVEIFEIM EGYPITVRLF DPPLHEFLPN LEELVTEVTK ARTLGKPDPE KERLLARVKA
LMEANPMMGH RGVRVGITYP EIYAAQVKAI LSAALELKRR GKHVELQIMI PQVAEVRELE
IIINNVVKPT AEEVFKAYGD RINYKIGTMM ETVRSCLTAD KIAKVVDFMS FGTNDLTQAV
FSFSRDDVEN KFMSKYLELG VLPYDPFVTI DEDGVAKLMK IAIDLARGVK PDIEIGICGE
HGGDSDSIKI LARTVGRGLN YFSASPYRVP VARLVAAQES LKLLGRAPKI HIY
//
