ID A0A271J410_9BACT Unreviewed; 896 AA.
AC A0A271J410;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BSZ37_18485 {ECO:0000313|EMBL:PAP78271.1};
OS Rubrivirga marina.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubrivirga.
OX NCBI_TaxID=1196024 {ECO:0000313|EMBL:PAP78271.1, ECO:0000313|Proteomes:UP000216339};
RN [1] {ECO:0000313|EMBL:PAP78271.1, ECO:0000313|Proteomes:UP000216339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-28 {ECO:0000313|EMBL:PAP78271.1,
RC ECO:0000313|Proteomes:UP000216339};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
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 -!- 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:PAP78271.1}.
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DR EMBL; MQWD01000001; PAP78271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A271J410; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000216339; 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; 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; 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:PAP78271.1};
KW Magnesium {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:PAP78271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216339};
KW Transferase {ECO:0000313|EMBL:PAP78271.1}.
FT DOMAIN 70..295
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 308..358
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..889
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 851
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 765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 765
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 786
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 787
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 789
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 896 AA; 95776 MW; 4A59ABB4B1C9B4BE CRC64;
MPTVDTDRRW VYAFEDAPAD ARALLGGKGA GLAAMTAAGL PVPPGFTITT EACVAYQDAG
HHVPDGLWDQ TETALAEVEA AAGRRFGDAD DPLLLSVRSG AAVSMPGMMD TVLNLGLNDG
TAAALARQTG DERFAYDAYR RFVAMFGEIV MGVEADRFER IVQRAKGQTE GGQDTDLSVD
QLKEIVAQSK RVIAGQTRQH FPDDPREQLR QAVAAVFDSW DNDRAVHYRR VHNIPDDIGT
GVTVQAMVFG NKGWDSGTGV AFTRDPSTGA KGLYGEYLLN AQGEDVVAGI RTPKPIAEMA
GDLPETFDQF QALADQLEQT YGDVQDIEFT IEQGTLWLLQ TRTAKRSGAA AVRIAVEMVG
EGVIDERTAV GRVDPAALEA LLHPAVNDDA EVELLAEGLP ASPGAAQGRV AFTSDDAEAR
AAEGEPVVLV RQQTSPEDFH GMVAAVAVVT AEGGMTSHAA VVARGMGTPC VAGASSLRLD
AAQGRLEAGG HTVLDGDWVT VDGATGRVLL GRVPTKDPEL GDDFRTLMSW ADDVRRLGVR
ANADTGEDAA KAREFGAEGI GLCRTEHMFF GDERLQPMRE MILAEDAGAR EAALRKLLPL
QRRDFDALLR AMDGLPVTVR LLDPPLHEFL PDLLELTGRI AETKLALKQA TTLEEMDRLL
DESAASRALL RQVEKLHEEN PMLGLRGCRL GMLYPEITQM QVRALFEAAA DCVEDGIGVQ
PEVMIPLVSA AAEIETQAAL VRETADAVLA ERGVALDYLV GTMIELPRAA LRAGDIARTA
EFFSFGTNDL TQTTFGLSRD DAGRFLSAYV ERGVLPADPF QTLDVEGVGE LVRLGTDRGR
AERPDLKVGV CGEHGGDPAS VAFFHGVGLD YVSCSPFRVP VARLAAARAT LGGDAS
//