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Protein

Phosphoribosyl 1,2-cyclic phosphodiesterase

Gene

phnP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate.2 Publications

Catalytic activityi

5-phospho-alpha-D-ribose 1,2-cyclic phosphate + H2O = alpha-D-ribose 1,5-bisphosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi21Zinc2 Publications1
Metal bindingi23Zinc2 Publications1
Metal bindingi26Zinc2 Publications1
Metal bindingi76Manganese 1; via tele nitrogen2 Publications1
Metal bindingi78Manganese 1; via pros nitrogen2 Publications1
Metal bindingi80Manganese 22 Publications1
Metal bindingi81Manganese 2; via tele nitrogen2 Publications1
Metal bindingi143Manganese 1; via tele nitrogen2 Publications1
Metal bindingi164Manganese 12 Publications1
Metal bindingi164Manganese 22 Publications1
Metal bindingi222Manganese 2; via tele nitrogen2 Publications1
Metal bindingi225Zinc; via pros nitrogen2 Publications1

GO - Molecular functioni

  • manganese ion binding Source: EcoCyc
  • phosphoric diester hydrolase activity Source: EcoCyc

GO - Biological processi

  • organic phosphonate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10725-MONOMER.
ECOL316407:JW4053-MONOMER.
MetaCyc:EG10725-MONOMER.
BRENDAi3.1.4.55. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosyl 1,2-cyclic phosphodiesterase (EC:3.1.4.55)
Alternative name(s):
Phosphoribosyl cyclic phosphodiesterase
Gene namesi
Name:phnP
Ordered Locus Names:b4092, JW4053
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10725. phnP.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi54D → A: Has a 1000-fold lower activity. 1 Publication1
Mutagenesisi75T → A: Has 40-fold lower activity. 1 Publication1
Mutagenesisi78H → A: Has 250-fold lower activity. 1 Publication1
Mutagenesisi80D → A: Has 1000-fold lower activity, and has 100-fold lower affinity for manganese. 1 Publication1
Mutagenesisi164D → A: Has a 1000-fold lower activity. 1 Publication1
Mutagenesisi187D → A: No effect. 1 Publication1
Mutagenesisi200H → A: Has 10-fold lower activity. 1 Publication1
Mutagenesisi222H → A: Has 9-fold lower activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000584021 – 252Phosphoribosyl 1,2-cyclic phosphodiesteraseAdd BLAST252

Proteomic databases

PaxDbiP16692.
PRIDEiP16692.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4261542. 7 interactors.
IntActiP16692. 1 interactor.
STRINGi511145.b4092.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi24 – 31Combined sources8
Helixi33 – 35Combined sources3
Beta strandi39 – 46Combined sources8
Beta strandi49 – 53Combined sources5
Helixi60 – 63Combined sources4
Beta strandi71 – 73Combined sources3
Helixi79 – 82Combined sources4
Helixi83 – 85Combined sources3
Turni86 – 90Combined sources5
Beta strandi92 – 94Combined sources3
Beta strandi96 – 100Combined sources5
Turni108 – 112Combined sources5
Beta strandi117 – 122Combined sources6
Beta strandi129 – 131Combined sources3
Beta strandi134 – 140Combined sources7
Beta strandi143 – 145Combined sources3
Beta strandi148 – 153Combined sources6
Beta strandi158 – 162Combined sources5
Helixi170 – 178Combined sources9
Beta strandi182 – 187Combined sources6
Beta strandi190 – 192Combined sources3
Beta strandi198 – 200Combined sources3
Helixi203 – 213Combined sources11
Beta strandi218 – 222Combined sources5
Helixi225 – 231Combined sources7
Beta strandi240 – 242Combined sources3
Beta strandi247 – 249Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G1PX-ray1.40A/B1-252[»]
3P2UX-ray1.48A/B1-252[»]
ProteinModelPortaliP16692.
SMRiP16692.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16692.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4107SA6. Bacteria.
COG1235. LUCA.
HOGENOMiHOG000223791.
InParanoidiP16692.
KOiK06167.
OMAiPRNHNDL.
PhylomeDBiP16692.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR017693. Phosphonate_metab_PhnP.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03307. PhnP. 1 hit.

Sequencei

Sequence statusi: Complete.

P16692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTLTLTGT GGAQGVPAWG CECAACARAR RSPQYRRQPC SGVVKFNDAI
60 70 80 90 100
TLIDAGLHDL ADRWSPGSFQ QFLLTHYHMD HVQGLFPLRW GVGDPIPVYG
110 120 130 140 150
PPDEQGCDDL FKHPGLLDFS HTVEPFVVFD LQGLQVTPLP LNHSKLTFGY
160 170 180 190 200
LLETAHSRVA WLSDTAGLPE KTLKFLRNNQ PQVMVMDCSH PPRADAPRNH
210 220 230 240 250
CDLNTVLALN QVIRSPRVIL THISHQFDAW LMENALPSGF EVGFDGMEIG

VA
Length:252
Mass (Da):27,848
Last modified:August 1, 1990 - v1
Checksum:iE23922C46A8386F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24356.1.
D90227 Genomic DNA. Translation: BAA14276.1.
U14003 Genomic DNA. Translation: AAA96991.1.
U00096 Genomic DNA. Translation: AAC77053.1.
AP009048 Genomic DNA. Translation: BAE78095.1.
PIRiH35719.
RefSeqiNP_418516.1. NC_000913.3.
WP_000059908.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77053; AAC77053; b4092.
BAE78095; BAE78095; BAE78095.
GeneIDi948600.
KEGGiecj:JW4053.
eco:b4092.
PATRICi32123743. VBIEscCol129921_4220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05260 Genomic DNA. Translation: AAA24356.1.
D90227 Genomic DNA. Translation: BAA14276.1.
U14003 Genomic DNA. Translation: AAA96991.1.
U00096 Genomic DNA. Translation: AAC77053.1.
AP009048 Genomic DNA. Translation: BAE78095.1.
PIRiH35719.
RefSeqiNP_418516.1. NC_000913.3.
WP_000059908.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G1PX-ray1.40A/B1-252[»]
3P2UX-ray1.48A/B1-252[»]
ProteinModelPortaliP16692.
SMRiP16692.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261542. 7 interactors.
IntActiP16692. 1 interactor.
STRINGi511145.b4092.

Proteomic databases

PaxDbiP16692.
PRIDEiP16692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77053; AAC77053; b4092.
BAE78095; BAE78095; BAE78095.
GeneIDi948600.
KEGGiecj:JW4053.
eco:b4092.
PATRICi32123743. VBIEscCol129921_4220.

Organism-specific databases

EchoBASEiEB0719.
EcoGeneiEG10725. phnP.

Phylogenomic databases

eggNOGiENOG4107SA6. Bacteria.
COG1235. LUCA.
HOGENOMiHOG000223791.
InParanoidiP16692.
KOiK06167.
OMAiPRNHNDL.
PhylomeDBiP16692.

Enzyme and pathway databases

BioCyciEcoCyc:EG10725-MONOMER.
ECOL316407:JW4053-MONOMER.
MetaCyc:EG10725-MONOMER.
BRENDAi3.1.4.55. 2026.

Miscellaneous databases

EvolutionaryTraceiP16692.
PROiP16692.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR017693. Phosphonate_metab_PhnP.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
TIGRFAMsiTIGR03307. PhnP. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHNP_ECOLI
AccessioniPrimary (citable) accession number: P16692
Secondary accession number(s): Q2M6L1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of strains K12 and B.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.