Xaa-Pro dipeptidase - Alteromonas sp.

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Q44238 (PEPQ_ALTSX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Alteromonas sp.

Taxonomic identifier

232 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_01279
Sequence similarities	Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=2.99 mM for diisopropylfluorophosphate Ref.1 Ref.2 K_M=1.57 mM for O-isopropyl methylphosphonofluoridate K_M=2.48 mM for O-pinacolyl methylphosphonofluoridate K_M=0.63 mM for O-cyclohexyl methylphosphonofluoridate K_M=1.27 mM for a chromogenic soman analog V_max=230 µmol/min/mg enzyme with diisopropylfluorophosphate as substrate V_max=442 µmol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate V_max=151 µmol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate V_max=652 µmol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate V_max=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.

Ontologies

Keywords
Biological process	Detoxification
Ligand	Manganese Metal-binding
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	aryldialkylphosphatase activity Inferred from electronic annotation. Source: EC diisopropyl-fluorophosphatase activity Inferred from electronic annotation. Source: EC dipeptidase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 517

517

Xaa-Pro dipeptidase HAMAP-Rule MF_01279

PRO_0000298944

Sites

Metal binding

244

Manganese 2 By similarity

Metal binding

255

Manganese 1 By similarity

Metal binding

255

Manganese 2 By similarity

Metal binding

336

Manganese 1 By similarity

Metal binding

381

Manganese 1 By similarity

Metal binding

420

Manganese 1 By similarity

Metal binding

420

Manganese 2 By similarity

Secondary structure

517

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q44238 [UniParc].

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

FASTA

517

58,998

        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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L24	X-ray	2.30	A/B/C	1-517	[»]
3L7G	X-ray	2.70	A/B/C	1-517	[»]

ProteinModelPortal

Q44238.

ModBase

Search...

Protein family/group databases

MEROPS

M24.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-7712.

Family and domain databases

Gene3D

3.90.230.10. 1 hit.

HAMAP

MF_01279. X-Pro_dipeptid.

InterPro

IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
IPR022846. X_Pro_dipept.
[Graphical view]

Pfam

PF00557. Peptidase_M24. 1 hit.
[Graphical view]

SUPFAM

SSF55920. Peptidase_M24_cat_core. 1 hit.

PROSITE

PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4252.

EvolutionaryTrace

Q44238.

Entry information

Entry name

PEPQ_ALTSX

Accession

Primary (citable) accession number: Q44238

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	January 15, 2008
Last modified:	April 3, 2013
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents