Pyruvate, phosphate dikinase
Details
- Name
- Pyruvate, phosphate dikinase
- Kind
- protein
- Synonyms
- 2.7.9.1
- Pyruvate, orthophosphate dikinase
- Gene Name
- ppdK
- UniProtKB Entry
- P22983Swiss-Prot
- Organism
- Clostridium symbiosum
- NCBI Taxonomy ID
- 1512
- Amino acid sequence
>lcl|BSEQ0011357|Pyruvate, phosphate dikinase MAKWVYKFEEGNASMRNLLGGKGCNLAEMTILGMPIPQGFTVTTEACTEYYNSGKQITQE IQDQIFEAITWLEELNGKKFGDTEDPLLVSVRSGARASMPGMMDTILNLGLNDVAVEGFA KKTGNPRFAYDSYRRFIQMYSDVVMEVPKSHFEKIIDAMKEEKGVHFDTDLTADDLKELA EKFKAVYKEAMNGEEFPQEPKDQLMGAVKAVFRSWDNPRAIVYRRMNDIPGDWGTAVNVQ TMVFGNKGETSGTGVAFTRNPSTGEKGIYGEYLINAQGEDVVAGVRTPQPITQLENDMPD CYKQFMDLAMKLEKHFRDMQDMEFTIEEGKLYFLQTRNGKRTAPAALQIACDLVDEGMIT EEEAVVRIEAKSLDQLLHPTFNPAALKAGEVIGSALPASPGAAAGKVYFTADEAKAAHEK GERVILVRLETSPEDIEGMHAAEGILTVRGGMTSHAAVVARGMGTCCVSGCGEIKINEEA KTFELGGHTFAEGDYISLDGSTGKIYKGDIETQEASVSGSFERIMVWADKFRTLKVRTNA DTPEDTLNAVKLGAEGIGLCRTEHMFFEADRIMKIRKMILSDSVEAREEALNELIPFQKG DFKAMYKALEGRPMTVRYLDPPLHEFVPHTEEEQAELAKNMGLTLAEVKAKVDELHEFNP MMGHRGCRLAVTYPEIAKMQTRAVMEAAIEVKEETGIDIVPEIMIPLVGEKKELKFVKDV VVEVAEQVKKEKGSDMQYHIGTMIEIPRAALTADAIAEEAEFFSFGTNDLTQMTFGFSRD DAGKFLDSYYKAKIYESDPFARLDQTGVGQLVEMAVKKGRQTRPGLKCGICGEHGGDPSS VEFCHKVGLNYVSCSPFRVPIARLAAAQAALNNK
- Number of residues
- 874
- Molecular Weight
- 96653.645
- Theoretical pI
- 4.82
- GO Classification
- FunctionsATP binding / kinase activity / metal ion binding / pyruvate, phosphate dikinase activityProcessespyruvate metabolic process
- General Function
- Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
- Specific Function
- ATP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003751|2523 bp ATGGCAAAATGGGTTTATAAGTTCGAAGAAGGCAATGCATCTATGAGAAACCTTCTTGGA GGCAAAGGCTGCAACCTTGCAGAGATGACCATCTTAGGAATGCCGATTCCACAGGGCTTT ACTGTAACAACAGAAGCTTGTACAGAGTACTACAACAGTGGAAAACAGATCACACAGGAA ATTCAGGATCAGATTTTCGAAGCTATCACATGGTTAGAGGAACTGAACGGCAAGAAGTTC GGCGACACTGAAGATCCGTTATTAGTATCTGTACGTTCCGCGGCCCGCGCATCCATGCCG GGTATGATGGATACCATCCTGAACCTTGGTTTAAACGACGTTGCAGTAGAGGGCTTTGCA AAGAAAACGGGAAATCCAAGATTTGCATATGATTCTTACAGAAGATTTATCCAGATGTAT TCCGACGTAGTTATGGAAGTTCCGAAGTCCCATTTCGAGAAAATCATCGATGCGATGAAA GAAGAAAAGGGCGTTCACTTCGATACAGACCTGACTGCCGATGATTTAAAAGAGCTGGCT GAGAAGTTCAAAGCTGTTTACAAAGAGGCTATGAACGGCGAAGAGTTCCCACAGGAGCCG AAGGATCAGTTAATGGGCGCTGTTAAAGCAGTTTTCCGTTCCTGGGACAACCCTCGTGCA ATCGTATACCGCCGTATGAACGATATCCCTGGAGACTGGGGTACTGCAGTTAACGTTCAG ACCATGGTATTTGGTAACAAGGGCGAGACCAGCGGTACAGGCGTTGCCTTCACACGTAAC CCATCCACAGGTGAAAAAGGCATCTACGGTGAGTACCTGATCAATGCACAGGGCGAGGAC GTAGTTGCAGGTGTCCGCACACCACAGCCTATCACCCAGTTAGAGAACGATATGCCTGAC TGCTACAAGCAGTTCATGGATCTGGCCATGAAGCTGGAGAAACATTTCCGTGACATGCAG GATATGGAGTTCACAATCGAGGAAGGTAAATTATACTTCTTACAGACACGTAACGGCAAG AGAACAGCTCCGGCTGCTCTTCAGATTGCCTGCGATTTAGTAGACGAAGGCATGATCACA GAGGAAGAGGCTGTTGTAAGAATCGAAGCAAAATCTCTTGATCAGTTACTTCACCCGACC TTCAACCCGGCTGCTTTAAAGGCCGGCGAAGTAATCGGTTCCGCTCTTCCGGCATCTCCT GGCGCAGCAGCAGGTAAAGTATACTTCACCGCTGATGAGGCTAAGGCTGCCCACGAGAAG GGTGAGAGAGTTATCCTTGTTCGTCTTGAGACATCTCCGGAAGATATCGAAGGTATGCAT GCAGCCGAAGGTATCCTGACAGTGCGCGGCGGTATGACAAGCCATGCAGCCGTAGTTGCA CGTGGTATGGGAACATGCTGCGTATCCGGATGCGGTGAGATCAAGATCAACGAAGAAGCT AAGACATTCGAACTTGGCGGACACACATTTGCAGAGGGAGATTACATCTCCTTAGATGGT TCCACAGGTAAGATTTACAAGGGCGACATCGAGACTCAGGAACGTTCCGTAAGCGGAAGC TTCGAGCGTATCATGGTATGGGCTGACAAGTTCAGAACATTAAAGGTTCGTACAAATGCC GACACACCGGAAGATACACTCAATGCCGTTAAACTGGGTGCAGAGGGCATCGGTCTTTGC CGTACAGAGCATATGTTCTTCGAGGCTGACAGAATCATGAAGATCAGAAAGATGATCCTT TCCGATTCAGTGGAAGCAAGAGAAGAGGCTCTGAACGAATTAATCCCGTTCCAGAAGGGC GATTTCAAGGCTATGTACAAAGCTCTGGAAGGCAGGCCAATGACGGTTCGCTACCTGGAT CCGCCGCTGCATGAGTTCGTTCCTCATACAGAAGAGGAGCAGGCTGAACTGGCTAAGAAC ATGGGCCTTACTTTAGCAGAAGTAAAAGCAAAAGTTGACGAATTACACGAGTTCAACCCA ATGATGGGCCATCGTGGCTGCCGTCTTGCAGTTACCTATCCGGAAATTGCAAAGATGCAG ACAAGAGCCGTTATGGAAGCTGCTATCGAAGTGAAGGAAGAGACAGGAATCGATATTGTT CCTGAGATCATGATTCCGTTAGTTGGCGAGAAGAAAGAGCTTAAGTTCGTTAAGGACGTA GTTGTGGAAGTAGCTGAGCAGGTTAAGAAAGAGAAAGGTTCCGATATGCAGTACCACATC GGTACCATGATCGAAATTCCTCGTGCAGCTCTCACAGCAGATGCCATCGCTGAGGAAGCA GAGTTCTTCTCCTTCGGTACAAACGACTTAACACAGATGACATTCGGCTTCTCCCGTGAC GACGCCGGCAAGTTCCTGGATTCCTACTATAAAGCAAAAATTTATGAGTCCGATCCATTC GCAAGACTTGACCAGACAGGCGTTGGCCAGTTAGTAGAGATGGCAGTTAAGAAAGGCCGT CAGACACGTCCGGGCCTTAAGTGCGGCATCTGCGGCGAGCACGGCGAGATCCTTCTTCCG TAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P22983 UniProtKB Entry Name PPDK_CLOSY GenBank Protein ID 143961 GenBank Gene ID M60920 PDB ID(s) 1DIK, 1GGO, 1JDE, 1KBL, 1KC7, 2DIK, 2FM4, 2R82 - General References
- Pocalyko DJ, Carroll LJ, Martin BM, Babbitt PC, Dunaway-Mariano D: Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs. Biochemistry. 1990 Dec 4;29(48):10757-65. [Article]
- Goss NH, Evans CT, Wood HG: Pyruvate phosphate dikinase: sequence of the histidyl peptide, the pyrophosphoryl and phosphoryl carrier. Biochemistry. 1980 Dec 9;19(25):5805-9. [Article]
- Xu Y, Yankie L, Shen L, Jung YS, Mariano PS, Dunaway-Mariano D, Martin BM: Location of the catalytic site for phosphoenolpyruvate formation within the primary structure of Clostridium symbiosum pyruvate phosphate dikinase. 1. Identification of an essential cysteine by chemical modification with [1-14C]bromopyruvate and site-directed mutagenesis. Biochemistry. 1995 Feb 21;34(7):2181-7. [Article]
- Wei M, Ye D, Dunaway-Mariano D: Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase. Biochemistry. 2001 Nov 13;40(45):13466-73. [Article]
- Ye D, Wei M, McGuire M, Huang K, Kapadia G, Herzberg O, Martin BM, Dunaway-Mariano D: Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase. J Biol Chem. 2001 Oct 5;276(40):37630-9. Epub 2001 Jul 23. [Article]
- Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D: Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2652-7. [Article]
- McGuire M, Huang K, Kapadia G, Herzberg O, Dunaway-Mariano D: Location of the phosphate binding site within Clostridium symbiosum pyruvate phosphate dikinase. Biochemistry. 1998 Sep 29;37(39):13463-74. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Phosphonopyruvate experimental unknown target Details