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}.
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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
//