Exopolyphosphatase (P0AFL6)

Identification
Name:Exopolyphosphatase
Synonyms:
  • ExopolyPase
  • Metaphosphatase
Gene Name:ppx
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Degradation of inorganic polyphosphates. Orthophosphate is released progressively from the ends of polyphosphate of circa 500 residues long, while chains of circa 15 residues compete poorly with polyphosphate as substrate
Cellular Location:Cell membrane; Peripheral membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Water ↔ 1.0Hydrogen ion + 1.0Phosphate + 1.0Guanosine 3',5'-bis(diphosphate)
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Water ↔ 1.0Guanosine 3',5'-bis(diphosphate) + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb
1.0Polyphosphate + 1.0Water ↔ 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb
1.0Water + 1.0Pyrophosphate → 1.0Hydrogen ion + 2.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine 3'-diphosphate 5'-triphosphate + 1.0Water ↔ 1.0Hydrogen ion + 1.0Phosphate + 1.0Guanosine 3',5'-bis(diphosphate)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Triphosphate → 1.0Hydrogen ion + 1.0Phosphate + 1.0Pyrophosphate
ReactionCard
1.0(Polyphosphate)(n)+1.0Thumb → 1.0(polyphosphate)(n-1)+1.0Thumb
1.0(Polyphosphate)(n) + 1.0Water → 1.0(polyphosphate)(n-1) + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20158Guanosine 3',5'-bis(diphosphate)MetaboCard
ECMDB20156Guanosine 3'-diphosphate 5'-triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB03379TriphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
exopolyphosphatase activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
ion binding
magnesium ion binding
metal ion binding
pyrophosphatase activity
Process
cellular metabolic process
metabolic process
phosphate metabolic process
phosphorus metabolic process
polyphosphate catabolic process
polyphosphate metabolic process
Gene Properties
Blattner:b2502
Gene OrientationClockwise
Centisome Percentage:56.54
Left Sequence End2623137
Right Sequence End2624678
Gene Sequence:
>1542 bp
ATGCGTCTGGAAGTCTTTTGTGAAGACCGACTCGGTCTGACCCGCGAATTACTCGATCTA
CTCGTGCTAAGAGGCATTGATTTACGCGGTATTGAGATTGATCCCATTGGGCGAATCTAC
CTCAATTTTGCTGAACTGGAGTTTGAGAGTTTCAGCAGTCTGATGGCCGAAATACGCCGT
ATTGCGGGTGTTACCGATGTGCGTACTGTCCCGTGGATGCCTTCCGAACGTGAGCATCTG
GCGTTGAGCGCGTTACTGGAGGCGTTGCCTGAACCTGTGCTCTCTGTCGATATGAAAAGC
AAAGTGGATATGGCGAACCCGGCGAGCTGTCAGCTTTTTGGGCAAAAATTGGATCGCCTG
CGCAACCATACCGCCGCACAATTGATTAACGGCTTTAATTTTTTACGTTGGCTGGAAAGC
GAACCGCAAGATTCGCATAACGAGCATGTCGTTATTAATGGGCAGAATTTCCTGATGGAG
ATTACGCCTGTTTATCTTCAGGATGAAAATGATCAACACGTCCTGACCGGTGCGGTGGTG
ATGTTGCGATCAACGATTCGTATGGGCCGCCAGTTGCAAAATGTCGCCGCCCAGGACGTC
AGCGCCTTCAGTCAAATTGTCGCCGTCAGCCCGAAAATGAAGCATGTTGTCGAACAGGCG
CAGAAACTGGCGATGCTAAGCGCGCCGCTGCTGATTACGGGTGACACAGGTACAGGTAAA
GATCTCTTTGCCTACGCCTGCCATCAGGCAAGCCCCAGAGCGGGCAAACCTTACCTGGCG
CTGAACTGTGCGTCTATACCGGAAGATGCGGTCGAGAGTGAACTGTTTGGTCATGCTCCG
GAAGGGAAGAAAGGATTCTTTGAGCAGGCGAACGGTGGTTCGGTGCTGTTGGATGAAATA
GGGGAAATGTCACCACGGATGCAGGCGAAATTACTGCGTTTCCTTAATGATGGCACTTTC
CGTCGGGTTGGCGAAGACCATGAGGTGCATGTCGATGTGCGGGTGATTTGCGCTACGCAG
AAGAATCTGGTCGAACTGGTGCAAAAAGGCATGTTCCGTGAAGATCTCTATTATCGTCTG
AACGTGTTGACGCTCAATCTGCCGCCGCTACGTGACTGTCCGCAGGACATCATGCCGTTA
ACTGAGCTGTTCGTCGCCCGCTTTGCCGACGAGCAGGGCGTGCCGCGTCCGAAACTGGCC
GCTGACCTGAATACTGTACTTACGCGTTATGCGTGGCCGGGAAATGTGCGGCAGTTAAAG
AACGCTATCTATCGCGCACTGACACAACTGGACGGTTATGAGCTGCGTCCACAGGATATT
TTGTTGCCGGATTATGACGCCGCAACGGTAGCCGTGGGCGAAGATGCGATGGAAGGTTCG
CTGGACGAAATCACCAGCCGTTTTGAACGCTCGGTATTAACCCAGCTTTATCGCAATTAT
CCCAGCACGCGCAAACTGGCAAAACGTCTCGGCGTTTCACATACCGCGATTGCCAATAAG
TTGCGGGAATATGGTCTGAGTCAGAAGAAGAACGAAGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:513
Protein Molecular Weight:58136
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Exopolyphosphatase
MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEE
AMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNE
EARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGG
VINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPE
RLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREG
VLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLE
ALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDD
LPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNA
LVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA
References
External Links:
ResourceLink
Uniprot ID:P0AFL6
Uniprot Name:PPX_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742168
Ecogene ID:EG11403
Ecocyc:EG11403
ColiBase:b2502
Kegg Gene:b2502
EchoBASE ID:EB1375
CCDB:PPX_ECOLI
BacMap:16130427
General Reference:
  • Akiyama, M., Crooke, E., Kornberg, A. (1993). "An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon." J Biol Chem 268:633-639. Pubmed: 8380170
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Reizer, J., Reizer, A., Saier, M. H. Jr, Bork, P., Sander, C. (1993). "Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily." Trends Biochem Sci 18:247-248. Pubmed: 8212131
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837