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Q44238 (PEPQ_ALTSX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xaa-Pro dipeptidase

Short name=X-Pro dipeptidase
EC=3.4.13.9
Alternative name(s):
DFPase
Imidodipeptidase
Organophosphorus acid anhydrolase 2
Short name=OPAA-2
EC=3.1.8.2
Paraoxon hydrolase
Phosphotriesterase
EC=3.1.8.1
Proline dipeptidase
Short name=Prolidase
Gene names
Name:pepQ
Synonyms:opaA
OrganismAlteromonas sp.
Taxonomic identifier232 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position and a nonpolar amino acid at the N-terminal position. Also catalyzes the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds including insecticide paraoxon and nerve gases such as diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-cyclohexyl methylphosphonofluoridate. Ref.1 Ref.2 Ref.3 Ref.4

Catalytic activity

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. HAMAP-Rule MF_01279

Diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride. HAMAP-Rule MF_01279

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. HAMAP-Rule MF_01279

Cofactor

Binds 2 manganese ions per monomer. Ref.1

Subunit structure

Monomer. Ref.2

Biotechnological use

Can be used for the catalytic detoxification of some nerve agents neurotoxins. HAMAP-Rule MF_01279

Miscellaneous

Has a stereoselective preference for isomers with R-configuration at the phosphorous center of sarin and soman, and with S-configuration in phosphotriesters.

Sequence similarities

Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=2.99 mM for diisopropylfluorophosphate Ref.1 Ref.2

KM=1.57 mM for O-isopropyl methylphosphonofluoridate

KM=2.48 mM for O-pinacolyl methylphosphonofluoridate

KM=0.63 mM for O-cyclohexyl methylphosphonofluoridate

KM=1.27 mM for a chromogenic soman analog

Vmax=230 µmol/min/mg enzyme with diisopropylfluorophosphate as substrate

Vmax=442 µmol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate

Vmax=151 µmol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate

Vmax=652 µmol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate

Vmax=52 µmol/min/mg enzyme with a chromogenic soman analog as substrate

pH dependence:

Optimum pH is 8.5 with DFP as substrate.

Temperature dependence:

Optimum temperature is 50 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Xaa-Pro dipeptidase HAMAP-Rule MF_01279
PRO_0000298944

Sites

Metal binding2441Manganese 2 By similarity
Metal binding2551Manganese 1 By similarity
Metal binding2551Manganese 2 By similarity
Metal binding3361Manganese 1 By similarity
Metal binding3811Manganese 1 By similarity
Metal binding4201Manganese 1 By similarity
Metal binding4201Manganese 2 By similarity

Secondary structure

.......................................................................... 517
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q44238 [UniParc].

Last modified January 15, 2008. Version 3.
Checksum: 9B92D811445C72A3

FASTA51758,998
        10         20         30         40         50         60 
MNKLAVLYAE HIATLQKRTR EIIERENLDG VVFHSGQAKR QFLDDMYYPF KVNPQFKAWL 

        70         80         90        100        110        120 
PVIDNPHCWI VANGTDKPKL IFYRPVDFWH KVPDEPNEYW ADYFDIELLV KPDQVEKLLP 

       130        140        150        160        170        180 
YDKARFAYIG EYLEVAQALG FELMNPEPVM NFYHYHRAYK TQYELACMRE ANKIAVQGHK 

       190        200        210        220        230        240 
AARDAFFQGK SEFEIQQAYL LATQHSENDN AYGNIVALNE NCAILHYTHF DRVAPATHRS 

       250        260        270        280        290        300 
FLIDAGANFN GYAADITRTY DFTGEGEFAE LVATMKQHQI ALCNQLAPGK LYGELHLDCH 

       310        320        330        340        350        360 
QRVAQTLSDF NIVDLSADEI VAKGITSTFF PHGLGHHIGL QVHDVGGFMA DEQGAHQEPP 

       370        380        390        400        410        420 
EGHPFLRCTR KIEANQVFTI EPGLYFIDSL LGDLAATDNN QHINWDKVAE LKPFGGIRIE 

       430        440        450        460        470        480 
DNIIVHEDSL ENMTRELRAR LTTHSLRGLS APQFSINDPA VMSEYSYPSE PLSYEEEIKK 

       490        500        510 
STFIVHVRTR RILVRRRTLS PILIAVTPMP AITAGLM 

« Hide

References

[1]"Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme."
Cheng T.-C., Harvey S.P., Chen G.L.
Appl. Environ. Microbiol. 62:1636-1641(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: JD6.5.
[2]"Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate."
DeFrank J.J., Cheng T.-C.
J. Bacteriol. 173:1938-1943(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: JD6.5.
[3]"Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis."
Cheng T.-C., Liu L., Wang B., Wu J., DeFrank J.J., Anderson D.M., Rastogi V.K., Hamilton A.B.
J. Ind. Microbiol. Biotechnol. 18:49-55(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: JD6.5.
[4]"Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters."
Hill C.M., Wu F., Cheng T.-C., DeFrank J.J., Raushel F.M.
Bioorg. Med. Chem. Lett. 10:1285-1288(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY, STEREOSELECTIVITY.
Strain: JD6.5.
[5]"Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin."
Hill C.M., Li W.-S., Cheng T.-C., DeFrank J.J., Raushel F.M.
Bioorg. Chem. 29:27-35(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STEREOSELECTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29240 Genomic DNA. Translation: AAB05590.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L24X-ray2.30A/B/C1-517[»]
3L7GX-ray2.70A/B/C1-517[»]
ProteinModelPortalQ44238.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL4252.

Protein family/group databases

MEROPSM24.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7712.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
HAMAPMF_01279. X_Pro_dipeptid.
InterProIPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
IPR022846. X_Pro_dipept.
[Graphical view]
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. SSF55920. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ44238.

Entry information

Entry namePEPQ_ALTSX
AccessionPrimary (citable) accession number: Q44238
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references