GenomeNet

Database: UniProt
Entry: A0A0K1E8F1_CHOCO
LinkDB: A0A0K1E8F1_CHOCO
Original site: A0A0K1E8F1_CHOCO 
ID   A0A0K1E8F1_CHOCO        Unreviewed;       916 AA.
AC   A0A0K1E8F1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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:AKT36863.1};
GN   ORFNames=CMC5_009840 {ECO:0000313|EMBL:AKT36863.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT36863.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT36863.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT36863.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP012159; AKT36863.1; -; Genomic_DNA.
DR   RefSeq; WP_050429312.1; NZ_CP012159.1.
DR   AlphaFoldDB; A0A0K1E8F1; -.
DR   STRING; 52.CMC5_009840; -.
DR   KEGG; ccro:CMC5_009840; -.
DR   PATRIC; fig|52.7.peg.1053; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000067626; 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; 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   Kinase {ECO:0000313|EMBL:AKT36863.1};
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:AKT36863.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW   Transferase {ECO:0000313|EMBL:AKT36863.1}.
FT   DOMAIN          21..58
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          66..318
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          330..385
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          448..537
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          552..902
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
FT   ACT_SITE        481
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   916 AA;  98659 MW;  BA9C8A18F89B8057 CRC64;
     MVSSIYFFGA GRADGDATMK ALLGGKGAGL AEMSRLGVPV PPGFTLTTEV CTAFYAGGGA
     LPDGVEEELR EAIGRVEKIV GGGFGSTTAP LLVSVRSGAR ASMPGMMDTI LNLGLNDAIV
     AGLAERTGNE RFALDAYRRF ILTYAGVVLG VEREQFEEAL VTARRKAATA LKIDHSRLNN
     AELERKVPDS ALDPEALRGL IARQKEIVLA ATGKSFPDDP WAQLEGAIHA VFGSWNNQRA
     KVYRKMHGIP ESWGTACTVQ AMVFGNMGDD SGTGVAFTRD PSTGERRFFG EWLPNAQGED
     VVAGVRTPHP LSKGGSDDER SLEVRMPQAF AQLMEVQARL EHHFRDMQDM EFTIQEGSLY
     LLQTRNGKRT GRAAVRIAVE MVKEKLITQN EAVLRVDPGS IDQLLHPSLD PSAPKEILAR
     GLPASPGAAT GEIVFTADEA ERRAAQGKAV ILVRAETSPE DIHGMKAARG ILTARGGMTS
     HAAVVARGMG KSCVAGCSSV SVGRDIVTVS LYDDDGRPTG SKSLKAGDVI TLDGGSGRVY
     LGAIPTVPAA LSGEFGELMA WADGVRRMRV RANADTPHDA RTARNFGAEG VGLCRTEHMF
     FDEKRIEAMR EMILAGDKHA RHRAVDKLLP YQRDDFTGVF REMAGLPVTI RLLDPPLHEF
     LPQEKAQLEQ MAQVLGVSVA EIVRKNEELH EFNPMLGHRG CRLAVTYPEI YEMQVRAILE
     AACDVAAEGV DVHPEIMIPL TMTQRELTLM RELVDRIAEQ VFSEKGRKVS FHFGTMIELP
     RAAIRAGEIA EHAEFFSFGT NDLTQTTLGI SRDDAGKFLG AYVDLGIFPS DPFQSIDVDG
     VGALVELASE RGRAKRPGIH LGVCGEHGGD PASVTFFEKV GLDYVSCSPF RVPIARLAAA
     QAALNAGTHG GPKATD
//
DBGET integrated database retrieval system