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Database: UniProt
Entry: A0A271J410_9BACT
LinkDB: A0A271J410_9BACT
Original site: A0A271J410_9BACT 
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
//
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