Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q44238

- PEPQ_ALTSX

UniProt

Q44238 - PEPQ_ALTSX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Xaa-Pro dipeptidase

Gene

pepQ

Organism
Alteromonas sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride.
An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.

Cofactori

Binds 2 manganese ions per monomer.1 Publication

Kineticsi

  1. KM=2.99 mM for diisopropylfluorophosphate2 Publications
  2. KM=1.57 mM for O-isopropyl methylphosphonofluoridate2 Publications
  3. KM=2.48 mM for O-pinacolyl methylphosphonofluoridate2 Publications
  4. KM=0.63 mM for O-cyclohexyl methylphosphonofluoridate2 Publications
  5. KM=1.27 mM for a chromogenic soman analog2 Publications

Vmax=230 µmol/min/mg enzyme with diisopropylfluorophosphate as substrate2 Publications

Vmax=442 µmol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate2 Publications

Vmax=151 µmol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate2 Publications

Vmax=652 µmol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate2 Publications

Vmax=52 µmol/min/mg enzyme with a chromogenic soman analog as substrate2 Publications

pH dependencei

Optimum pH is 8.5 with DFP as substrate.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi244 – 2441Manganese 2By similarity
Metal bindingi255 – 2551Manganese 1By similarity
Metal bindingi255 – 2551Manganese 2By similarity
Metal bindingi336 – 3361Manganese 1By similarity
Metal bindingi381 – 3811Manganese 1By similarity
Metal bindingi420 – 4201Manganese 1By similarity
Metal bindingi420 – 4201Manganese 2By similarity

GO - Molecular functioni

  1. aryldialkylphosphatase activity Source: UniProtKB-EC
  2. diisopropyl-fluorophosphatase activity Source: UniProtKB-EC
  3. dipeptidase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW
  5. metalloexopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Detoxification

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7712.

Protein family/group databases

MEROPSiM24.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidase (EC:3.4.13.9)
Short name:
X-Pro dipeptidase
Alternative name(s):
DFPase
Imidodipeptidase
Organophosphorus acid anhydrolase 2 (EC:3.1.8.2)
Short name:
OPAA-2
Paraoxon hydrolase
Phosphotriesterase (EC:3.1.8.1)
Proline dipeptidase
Short name:
Prolidase
Gene namesi
Name:pepQ
Synonyms:opaA
OrganismiAlteromonas sp.
Taxonomic identifieri232 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Pathology & Biotechi

Biotechnological usei

Can be used for the catalytic detoxification of some nerve agents neurotoxins.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Xaa-Pro dipeptidasePRO_0000298944Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2523
Beta strandi29 – 346
Helixi54 – 574
Beta strandi69 – 724
Beta strandi74 – 763
Beta strandi79 – 835
Beta strandi88 – 903
Helixi99 – 1035
Beta strandi104 – 1118
Helixi112 – 1143
Helixi116 – 1183
Helixi123 – 1253
Beta strandi126 – 1316
Helixi133 – 1397
Beta strandi143 – 1453
Helixi147 – 15711
Helixi162 – 18726
Helixi192 – 20312
Helixi207 – 2093
Beta strandi210 – 2123
Beta strandi215 – 2184
Helixi219 – 2235
Beta strandi240 – 24910
Beta strandi252 – 26413
Helixi267 – 28317
Helixi292 – 30918
Beta strandi312 – 3154
Helixi317 – 3226
Helixi326 – 3283
Beta strandi339 – 3435
Beta strandi376 – 3805
Beta strandi383 – 3853
Helixi388 – 3958
Helixi398 – 4025
Helixi405 – 4117
Helixi412 – 4143
Beta strandi416 – 4183
Beta strandi420 – 4256
Beta strandi430 – 4323
Helixi433 – 4364

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L24X-ray2.30A/B/C1-517[»]
3L7GX-ray2.70A/B/C1-517[»]
ProteinModelPortaliQ44238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44238.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01279. X_Pro_dipeptid.
InterProiIPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
IPR022846. X_Pro_dipept.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q44238-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKLAVLYAE HIATLQKRTR EIIERENLDG VVFHSGQAKR QFLDDMYYPF
60 70 80 90 100
KVNPQFKAWL PVIDNPHCWI VANGTDKPKL IFYRPVDFWH KVPDEPNEYW
110 120 130 140 150
ADYFDIELLV KPDQVEKLLP YDKARFAYIG EYLEVAQALG FELMNPEPVM
160 170 180 190 200
NFYHYHRAYK TQYELACMRE ANKIAVQGHK AARDAFFQGK SEFEIQQAYL
210 220 230 240 250
LATQHSENDN AYGNIVALNE NCAILHYTHF DRVAPATHRS FLIDAGANFN
260 270 280 290 300
GYAADITRTY DFTGEGEFAE LVATMKQHQI ALCNQLAPGK LYGELHLDCH
310 320 330 340 350
QRVAQTLSDF NIVDLSADEI VAKGITSTFF PHGLGHHIGL QVHDVGGFMA
360 370 380 390 400
DEQGAHQEPP EGHPFLRCTR KIEANQVFTI EPGLYFIDSL LGDLAATDNN
410 420 430 440 450
QHINWDKVAE LKPFGGIRIE DNIIVHEDSL ENMTRELRAR LTTHSLRGLS
460 470 480 490 500
APQFSINDPA VMSEYSYPSE PLSYEEEIKK STFIVHVRTR RILVRRRTLS
510
PILIAVTPMP AITAGLM
Length:517
Mass (Da):58,998
Last modified:January 15, 2008 - v3
Checksum:i9B92D811445C72A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29240 Genomic DNA. Translation: AAB05590.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29240 Genomic DNA. Translation: AAB05590.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q44238.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL4252.

Protein family/group databases

MEROPSi M24.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-7712.

Miscellaneous databases

EvolutionaryTracei Q44238.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01279. X_Pro_dipeptid.
InterProi IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
IPR022846. X_Pro_dipept.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 1 hit.
PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPEPQ_ALTSX
AccessioniPrimary (citable) accession number: Q44238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: January 15, 2008
Last modified: October 1, 2014
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3