(data stored in ACNUC7421 zone)

SWISSPROT: A1AZF9_PARDP

ID   A1AZF9_PARDP            Unreviewed;       853 AA.
AC   A1AZF9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   SubName: Full=Pyruvate phosphate dikinase {ECO:0000313|EMBL:ABL68653.1};
DE            EC=2.7.9.1 {ECO:0000313|EMBL:ABL68653.1};
GN   OrderedLocusNames=Pden_0541 {ECO:0000313|EMBL:ABL68653.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68653.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000853-3};
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DR   EMBL; CP000489; ABL68653.1; -; Genomic_DNA.
DR   RefSeq; WP_011746886.1; NC_008686.1.
DR   STRING; 318586.Pden_0541; -.
DR   PRIDE; A1AZF9; -.
DR   EnsemblBacteria; ABL68653; ABL68653; Pden_0541.
DR   KEGG; pde:Pden_0541; -.
DR   eggNOG; ENOG4107QJD; Bacteria.
DR   eggNOG; COG0574; LUCA.
DR   HOGENOM; HOG000039664; -.
DR   KO; K01006; -.
DR   OMA; YRRFVQM; -.
DR   BioCyc; PDEN318586:G1GW1-544-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1490.20; -; 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; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR22931; PTHR22931; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PIRSF; PIRSF000853; PPDK; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   4: Predicted;
DR   PRODOM; A1AZF9.
DR   SWISS-2DPAGE; A1AZF9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Kinase {ECO:0000313|EMBL:ABL68653.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000853-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000853-3};
KW   Pyruvate {ECO:0000313|EMBL:ABL68653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000313|EMBL:ABL68653.1}.
FT   DOMAIN      390    471       PEP-utilizers. {ECO:0000259|Pfam:
FT                                PF00391}.
FT   DOMAIN      490    836       PEP-utilizers_C. {ECO:0000259|Pfam:
FT                                PF02896}.
FT   ACT_SITE    423    423       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000853-1}.
FT   ACT_SITE    798    798       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000853-1}.
FT   METAL       712    712       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000853-3}.
FT   METAL       736    736       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000853-3}.
FT   BINDING     529    529       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     585    585       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     712    712       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     733    733       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
FT   BINDING     734    734       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
FT   BINDING     735    735       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000853-2}.
FT   BINDING     736    736       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000853-2}.
SQ   SEQUENCE   853 AA;  92325 MW;  A39F97D7E1964DD8 CRC64;
     MTALTDPGAI VEITPSAGIQ TARHGWRAKC LQRLVRMELP VPTSFALSAE AVRAIAAGQM
     PDRARLAAMV ERADGLVSVR PSAMNPAWGG PGTVLNVGIN HACHARLVQT RGKAAADAIY
     LGFVQSYAIH VARLDPDMFS DSEGGLEAAL RAYEDETDEE FPQDPARQLA EVLRSMARAW
     DGPTARLLRQ AKGAPPLAPL GLVVQDMALA IGPGVTGSGT IQFIDSVTGA PRITGRFRGQ
     TQGRSKGEGA ETLYLTRDPR GPSLEEAAPE VFADLVRFGV AARERLREEM QIEFVVSDSR
     LSIIDAVRVS RNSRASVRIA VALARDGIIP PEEAVMRVEP RALSDLLHHQ VDPRAPRDVI
     ARGINASPGA ATGRIVFTAA AAQAAEARGE RCVLVRRETV PEDIRGMHAA VAVLTERGGM
     TSHAAVIARG IGLPCIVGAS GISIDPRART MLVGGRLFHE GEEITIDGTS GEVLAGAAEM
     LEPALDDGFT QLLEWADAHC RIKIRANADT PEDARTARMF NAQGIGLCRT EHMFFDDERL
     PAMREMIFAG KPEDRSLSLE RLLPMQRSDF AALFEIMAGL PVTIRLFDPP LHEFLPHDRE
     GMRELAESLD LPLSDVTRRV EALSEFNPML GMRGVRLGIT VPEIYDMQAR AIFEATIEAS
     RNGDPVVPEI MIPLVSARRE VELVKTRIDA VAAAVRNETR KDFTYRLGVM VETPRAALRA
     GDIAEHSAFL SFGTNDLTQM TYGLSRDDAG RFMGTYVSQG VYSEDPFHIL DFDGVGELVA
     IGTERARDHK PDITIAVCGE HGGNPESIAF CLRTGVNYVS CSPFRVPVAR LAAAQESILM
     GREEAESSVE VES
//

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