Identification
Name:Polyribonucleotide nucleotidyltransferase
Synonyms:
  • Polynucleotide phosphorylase
  • PNPase
Gene Name:pnp
Enzyme Class:
Biological Properties
General Function:Involved in RNA binding
Specific Function:Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction
Cellular Location:Cytoplasm.
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
RNA+ThumbRNA+Thumb
RNA + Phosphate ↔ RNA + ADP
ReactionCard
RNA+ThumbRNA+Thumb
RNA+ThumbRNA+Thumb
RNA+ThumbRNA+Thumb
RNA + Phosphate ↔ RNA + CDP
ReactionCard
RNA+ThumbNDP
RNA + Phosphate ↔ NDP
ReactionCard
Complex Reactions:
RNA(n+1)+ThumbRNA(n)+a nucleoside diphosphate
RNA(n+1) + Inorganic phosphate → RNA(n) + a nucleoside diphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
GO Classification:
Component
intracellular membrane-bounded organelle
membrane-bounded organelle
mitochondrion
organelle
Function
3'-5' exonuclease activity
3'-5'-exoribonuclease activity
binding
catalytic activity
exonuclease activity
hydrolase activity
hydrolase activity, acting on ester bonds
nuclease activity
nucleic acid binding
nucleotidyltransferase activity
polyribonucleotide nucleotidyltransferase activity
RNA binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular macromolecule metabolic process
macromolecule metabolic process
metabolic process
mRNA catabolic process
RNA catabolic process
RNA metabolic process
RNA processing
Gene Properties
Blattner:b3164
Gene OrientationCounterclockwise
Centisome Percentage:71.28
Left Sequence End3307055
Right Sequence End3309190
Gene Sequence:
>2136 bp
TTGCTTAATCCGATCGTTCGTAAATTCCAGTACGGCCAACACACCGTGACTCTGGAAACC
GGCATGATGGCTCGTCAGGCTACTGCCGCTGTTATGGTTAGCATGGATGACACCGCGGTA
TTCGTTACCGTTGTTGGCCAGAAAAAAGCCAAACCAGGTCAGGACTTCTTCCCACTGACC
GTTAACTATCAGGAGCGTACCTACGCTGCTGGTCGTATCCCGGGTAGCTTCTTCCGTCGT
GAAGGCCGCCCAAGCGAAGGCGAAACCCTGATCGCGCGTCTGATTGACCGCCCGATTCGC
CCGCTGTTCCCGGAAGGCTTCGTCAACGAAGTTCAGGTTATCGCCACCGTGGTTTCTGTT
AACCCGCAAGTTAACCCGGATATCGTCGCGATGATTGGTGCTTCCGCAGCGCTGTCTCTG
TCTGGTATTCCGTTCAATGGCCCGATTGGTGCTGCCCGCGTAGGTTACATCAATGACCAG
TACGTACTGAACCCGACTCAGGACGAGCTGAAAGAGAGCAAACTGGATCTGGTTGTTGCC
GGTACTGAAGCCGCTGTACTGATGGTTGAATCTGAAGCTCAACTGCTGAGCGAAGACCAG
ATGCTGGGCGCAGTAGTGTTCGGTCATGAACAACAGCAGGTTGTTATTCAGAACATCAAT
GAACTGGTGAAAGAAGCCGGTAAACCGCGTTGGGACTGGCAGCCGGAGCCGGTAAACGAA
GCGCTAAACGCGCGCGTTGCTGCACTGGCTGAAGCTCGCCTGAGCGATGCTTACCGCATC
ACCGACAAACAAGAGCGTTATGCGCAGGTTGATGTCATCAAATCTGAAACCATCGCGACG
CTGCTTGCTGAAGACGAAACCCTGGACGAAAACGAACTGGGTGAAATTCTGCACGCGATC
GAGAAAAACGTTGTTCGTAGCCGCGTACTGGCAGGCGAACCGCGTATCGACGGTCGTGAA
AAAGATATGATCCGTGGTCTGGATGTGCGTACTGGCGTGCTGCCGCGTACTCACGGTTCT
GCGCTGTTCACCCGTGGTGAAACGCAGGCGCTGGTTACCGCAACGCTGCGTACTGCTCGT
GACGCGCAGGTTCTTGATGAACTGATGGGCGAACGTACCGATACCTTCCTGTTCCACTAC
AACTTCCCTCCGTACTCCGTAGGCGAAACCGGCATGGTCGGTTCTCCGAAGCGTCGTGAA
ATTGGTCACGGTCGTCTGGCGAAGCGCGGCGTGCTGGCAGTCATGCCGGATATGGACAAA
TTCCCGTACACCGTACGTGTTGTGTCTGAAATCACTGAATCCAACGGTTCCTCTTCTATG
GCTTCCGTGTGCGGCGCGTCTCTGGCGTCGATGGACGCAGGTGTGCCGATCAAAGCTGCC
GTTGCGGGTATCGCAATGGGTCTGGTGAAAGAAGGCGACAACTACGTTGTACTGTCTGAC
ATTTTGGGCGACGAAGATCACCTGGGCGATATGGACTTCAAAGTTGCAGGTTCCCGCGAC
GGTATCTCTGCACTGCAGATGGATATCAAAATTGAAGGTATCACCAAAGAGATCATGCAG
GTTGCGCTGAACCAGGCTAAAGGTGCGCGTCTGCATATCCTGGGCGTAATGGAACAGGCG
ATCAACGCGCCGCGTGGCGATATCTCTGAGTTCGCACCGCGTATCCATACCATCAAGATC
AACCCGGACAAGATCAAAGATGTTATCGGTAAAGGCGGTTCTGTAATCCGTGCTCTGACC
GAAGAAACTGGCACCACCATCGAAATCGAAGATGACGGTACTGTGAAGATTGCAGCGACC
GACGGCGAGAAAGCGAAACATGCTATTCGTCGTATCGAAGAGATCACTGCAGAAATCGAA
GTGGGCCGCGTCTACACTGGTAAAGTGACCCGTATCGTTGACTTTGGCGCATTTGTTGCC
ATCGGCGGCGGTAAAGAAGGTCTGGTCCACATCTCTCAAATCGCTGACAAACGCGTTGAG
AAAGTGACCGATTACCTGCAGATGGGTCAGGAAGTACCGGTGAAAGTTCTGGAAGTTGAT
CGCCAGGGCCGTATCCGTCTGAGCATTAAAGAAGCGACTGAGCAGTCTCAACCTGCTGCA
GCACCGGAAGCTCCGGCTGCTGAACAGGGCGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:711
Protein Molecular Weight:77100
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Polyribonucleotide nucleotidyltransferase
MLNPIVRKFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLT
VNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPIRPLFPEGFVNEVQVIATVVSV
NPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVA
GTEAAVLMVESEAQLLSEDQMLGAVVFGHEQQQVVIQNINELVKEAGKPRWDWQPEPVNE
ALNARVAALAEARLSDAYRITDKQERYAQVDVIKSETIATLLAEDETLDENELGEILHAI
EKNVVRSRVLAGEPRIDGREKDMIRGLDVRTGVLPRTHGSALFTRGETQALVTATLGTAR
DAQVLDELMGERTDTFLFHYNFPPYSVGETGMVGSPKRREIGHGRLAKRGVLAVMPDMDK
FPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNYVVLSD
ILGDEDHLGDMDFKVAGSRDGISALQMDIKIEGITKEIMQVALNQAKGARLHILGVMEQA
INAPRGDISEFAPRIHTIKINPDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAAT
DGEKAKHAIRRIEEITAEIEVGRVYTGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVE
KVTDYLQMGQEVPVKVLEVDRQGRIRLSIKEATEQSQPAAAPEAPAAEQGE
References
External Links:
ResourceLink
Uniprot ID:P05055
Uniprot Name:PNP_ECOLI
GenBank Gene ID:J02638
Genebank Protein ID:551833
Ecogene ID:EG10743
Ecocyc:EG10743
ColiBase:b3164
Kegg Gene:b3164
EchoBASE ID:EB0736
CCDB:PNP_ECOLI
BacMap:145698316
General Reference:
  • 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
  • Bycroft, M., Hubbard, T. J., Proctor, M., Freund, S. M., Murzin, A. G. (1997). "The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold." Cell 88:235-242. Pubmed: 9008164
  • Evans, S., Dennis, P. P. (1985). "Promoter activity and transcript mapping in the regulatory region for genes encoding ribosomal protein S15 and polynucleotide phosphorylase of Escherichia coli." Gene 40:15-22. Pubmed: 3005122
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Portier, C., Regnier, P. (1984). "Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions." Nucleic Acids Res 12:6091-6102. Pubmed: 6382163
  • Prud'homme-Genereux, A., Beran, R. K., Iost, I., Ramey, C. S., Mackie, G. A., Simons, R. W. (2004). "Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'." Mol Microbiol 54:1409-1421. Pubmed: 15554978
  • Regnier, P., Grunberg-Manago, M., Portier, C. (1987). "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1." J Biol Chem 262:63-68. Pubmed: 2432069
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137