ID A0A1J4UTQ2_9ARCH Unreviewed; 878 AA.
AC A0A1J4UTQ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
GN ORFNames=AUJ15_01275 {ECO:0000313|EMBL:OIO26473.1};
OS Candidatus Micrarchaeota archaeon CG1_02_55_41.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1805251 {ECO:0000313|EMBL:OIO26473.1, ECO:0000313|Proteomes:UP000183464};
RN [1] {ECO:0000313|EMBL:OIO26473.1, ECO:0000313|Proteomes:UP000183464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_55_41 {ECO:0000313|EMBL:OIO26473.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO26473.1}.
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DR EMBL; MNVI01000016; OIO26473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4UTQ2; -.
DR STRING; 1805251.AUJ15_01275; -.
DR Proteomes; UP000183464; 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; 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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OIO26473.1};
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:OIO26473.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..54
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 60..284
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 299..351
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 415..496
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 513..869
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT COILED 162..189
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 769
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
SQ SEQUENCE 878 AA; 96517 MW; D7F3D80AB3F109D6 CRC64;
MANQWVYLFG EHEFDKELLG GKGANLGEMT RVGFPVPEGF TITTEACRYY INEGSEPGDL
DAQVKEKLVE VERKTGKKFG DSANPLLLSV RSGAKISMPG MMDTVLNLGL NDETIRGLIK
KSGNERFAFD SYRRLIQMFG DVVLGVEHAK FEEILESHKD GRKDTELSVE ELKQIVKDYK
ELVEEETGKP FPNSPMEQLS LAVRAVFNSW DTERAKVYRK LHGIPDDLGT AVNVQAMVFG
NMGEKSGTGV AFTRNPATGA KEHYGEYLLN AQGEDVVAGI RTPHPVDDLK KDLPGPYAEL
IKVYDALEKH YKDVQDFEFT IEEGKFYLLQ TRTGKRTAQA AVKIAVDMAD EGLIDKETAV
MRVDPNSINQ LLHEQLDPSA ELNVIAQGLA ASPGAAVGKI AFTAEDAQAM AEKGEPVVLV
RNETSPEDIS GMAVAKGILT ARGGMTSHAA VVARGMGKCC ISGCSDIKVN EKARKMTVGD
EEFGAESWIS LDGGTGRVIK GQVKTVPPSF SSDFVKLMKW ADSFRKMGVR TNADTPKDAK
RARDFGAEGI GLTRTEHMFF GEDRLPWMQK MILAKNAEGR KEALSHLLEM QREDFKGIFK
AMDGLPVTIR LLDPPLHEFL PNHEELLVEI TALKIKGDNS ALLKEKEGLM KRVAELKESN
PMLGHRGCRL SITMPDVARM QVRAILEAAI ECAAKGIDVK PEIEVPLVGH ANELKLVKGF
IDETAKKVFA EKGETISYKV GTMIELPRAC LTANEIAEYA EFMSFGTNDL TQTTFGFSRD
DAGKFITEYR DKKILDGDPF AVIDRNGVGQ LMELTVKRGR ATKPGLEVGI CGEQGGEPDS
VEFCYLIGLS YVSCSPFRVP IARLAAAQSS IKHKGLRK
//
