| Type | Description |
|---|---|
| Definition | 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase |
| Date | Results | Publications |
|---|---|---|
| 2011-12-17 10:38:00 | Alteration of H200 to alanine in PhnP resulted in a 6-33-fold decrease in activity. | 21830807 |
| 2011-07-02 10:03:00 | the role of PhnP was examined by (31)P NMR spectrometry on the culture supernatants of E. coli phn mutants grown in the presence of alkylphosphonic acid or phosphite. | 21341651 |
| 2010-01-21 00:00:00 | The overall fold of PhnP is very similar to that of the tRNase Z endonucleases but lacks the long exosite module used by these enzymes to bind their tRNA substrates. | 19366688 |
| Type | IDs |
|---|---|
| Synonymous | ECK4085 |
| Gene |
UniProtKB-ID:
PHNP_ECOLI
UniprotKB:
P16692
UniParc:
UPI00001319A5
EMBL:
U14003,
AP009048,
D90227,
U00096,
J05260
EnsemblGenome:
b4092,
BAE78095
KO:
ecj:JW4053,
eco:b4092
|
| Nucleutide sequences |
EMBL-CDS:
AAA96991.1,
BAA14276.1,
AAA24356.1,
AAC77053.1,
BAE78095.1
EnsemblGenome_TRS:
BAE78095,
AAC77053
|
| Protein sequencees |
EnsemblGenome_PRO:
AAC77053,
BAE78095
RefSeq:
NP_418516.1
|
| Others |
UniRef100:
UniRef100_P16692
UniRef90:
UniRef90_P16692
UniRef50:
UniRef50_P16692
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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