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Database: UniProt
Entry: A0A0S2HVM6_9BACT
LinkDB: A0A0S2HVM6_9BACT
Original site: A0A0S2HVM6_9BACT 
ID   A0A0S2HVM6_9BACT        Unreviewed;       905 AA.
AC   A0A0S2HVM6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   Name=ppdK {ECO:0000313|EMBL:ALO14058.1};
GN   ORFNames=L21SP5_00379 {ECO:0000313|EMBL:ALO14058.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC   Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO14058.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO14058.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO14058.1,
RC   ECO:0000313|Proteomes:UP000064893};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of a novel strain predominating
RT   in hypersaline microbial mats and representing a new family of the
RT   Bacteriodetes phylum.";
RL   Submitted (NOV-2015) 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}.
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DR   EMBL; CP013118; ALO14058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2HVM6; -.
DR   STRING; 1307839.L21SP5_00379; -.
DR   KEGG; blq:L21SP5_00379; -.
DR   PATRIC; fig|1307839.3.peg.415; -.
DR   Proteomes; UP000064893; Chromosome.
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; 1.
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:ALO14058.1};
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:ALO14058.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW   Transferase {ECO:0000313|EMBL:ALO14058.1}.
FT   DOMAIN          21..390
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          456..537
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          553..903
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        489
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   ACT_SITE        864
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT   BINDING         595
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         651
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         778
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         778
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         799
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         800
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         801
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT   BINDING         802
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT   BINDING         802
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ   SEQUENCE   905 AA;  99974 MW;  DDABAC8789B07A1A CRC64;
     MTKHVYTFGD GKAEGKTEMK NLLGGKGANL AEMNLIGVPV PAGFTITTEV CTKYNQEGEE
     ATFAAIKGEV EDAVRATEKA MNAKFGSQSD EFPLLLSVRS GARVSMPGMM DTVLNLGMND
     DTVKIVAEKS GNERFAWDSY RRFIQMYGDV VMGVEAEKGE SDPFEIEIEK IKEEKGYKLD
     TEFTPEDLKK LVEAFKKVIK DKTGKAFPND PWEQLWGSVA AVFGSWNNKR AIYYRRMHQI
     PDEWGTAVNV QAMVYGNMGK NSATGVAFTR DAATGEDIFN GEYLIDAQGE DVVAGIRTPQ
     EITKEGSLRW AKRAGISEEQ RKAEFPSLEE AMPVVYKELD EVQQKLEDHY KDMQDLEFTI
     QDGKLWMLQT RNGKRTGAAM VKMAVDMMEE GMIDEKTAML RVEPNRLDEL LHPVFDKEAI
     KDAHTIAKGL PASPGAATGR VVFDADEAEE WKGRGEKVVL VRTETSPEDL SGMNVSEGIL
     TSRGGMTSHA AVVARGMGKC CVSGAGDVVV NYAKKEFTVD GKAYKEGDWI SLNGSTGEIY
     DGKVATIDPE LAGNFGQIME LAEKYTRMDV RTNADTPHDA ETAFNFGAKG IGLCRTEHMF
     FEGDRIKAVR EMILANDESG RRKALEKLLP WQREDFEGIL KAMDGYGVTI RLLDPPLHEF
     TPNDEKSQEQ MAKELGIPAD EVKAKVESLH EFNPMLGHRG CRLGNTYPEI TEMQARAIIE
     AACNLKSQGL NPKPEIMVPL IGTVGELKMQ EEIIRNVAAD VFKEKGVEVD YLVGTMIEIP
     RAALTADEVA EVAEFFSFGT NDLTQMTFGY SRDDAGKFLP IYLEKGLLKN DPFQVLDQTG
     VGQLVEMGTE KGRSAKKDLK VGICGEHGGE PSSVEFCHRV GMNYVSCSPF RVPIARLAAA
     QANIR
//
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