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Protein

Xaa-Pro dipeptidase

Gene

pepQ

Organism
Alteromonas sp.
Status
Reviewed-Annotation score: 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

Mn2+1 PublicationNote: 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
  1. Vmax=230 µmol/min/mg enzyme with diisopropylfluorophosphate as substrate2 Publications
  2. Vmax=442 µmol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate2 Publications
  3. Vmax=151 µmol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate2 Publications
  4. Vmax=652 µmol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate2 Publications
  5. 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)DescriptionActionsGraphical viewLength
Metal bindingi244Manganese 2By similarity1
Metal bindingi255Manganese 1By similarity1
Metal bindingi255Manganese 2By similarity1
Metal bindingi336Manganese 1By similarity1
Metal bindingi381Manganese 1By similarity1
Metal bindingi420Manganese 1By similarity1
Metal bindingi420Manganese 2By similarity1

GO - Molecular functioni

GO - Biological processi

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.
BRENDAi3.1.8.2. 275.

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.

Chemistry databases

ChEMBLiCHEMBL4252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002989441 – 517Xaa-Pro dipeptidaseAdd BLAST517

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1517
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 25Combined sources23
Beta strandi29 – 34Combined sources6
Helixi54 – 57Combined sources4
Beta strandi69 – 72Combined sources4
Beta strandi74 – 76Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi88 – 90Combined sources3
Helixi99 – 103Combined sources5
Beta strandi104 – 111Combined sources8
Helixi112 – 117Combined sources6
Helixi123 – 125Combined sources3
Beta strandi126 – 131Combined sources6
Helixi133 – 139Combined sources7
Beta strandi143 – 145Combined sources3
Helixi147 – 156Combined sources10
Helixi162 – 187Combined sources26
Helixi192 – 203Combined sources12
Helixi207 – 209Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi215 – 218Combined sources4
Helixi219 – 223Combined sources5
Beta strandi240 – 245Combined sources6
Beta strandi256 – 264Combined sources9
Helixi267 – 283Combined sources17
Helixi292 – 309Combined sources18
Beta strandi312 – 315Combined sources4
Helixi317 – 322Combined sources6
Turni323 – 325Combined sources3
Helixi326 – 329Combined sources4
Beta strandi334 – 337Combined sources4
Beta strandi339 – 343Combined sources5
Beta strandi347 – 351Combined sources5
Beta strandi376 – 380Combined sources5
Beta strandi383 – 385Combined sources3
Helixi388 – 395Combined sources8
Turni396 – 399Combined sources4
Helixi400 – 402Combined sources3
Helixi405 – 411Combined sources7
Helixi412 – 414Combined sources3
Beta strandi416 – 418Combined sources3
Beta strandi420 – 425Combined sources6
Beta strandi430 – 432Combined sources3
Helixi433 – 436Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L24X-ray2.30A/B/C1-517[»]
3L7GX-ray2.70A/B/C1-517[»]
4ZWOX-ray2.14A/B1-437[»]
4ZWPX-ray2.40A/B1-437[»]
4ZWUX-ray2.20A/B1-437[»]
ProteinModelPortaliQ44238.
SMRiQ44238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44238.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01279. X_Pro_dipeptid. 1 hit.
InterProiIPR000994. Pept_M24.
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:
EMBLi
GenBanki
DDBJi
Links Updated
U29240 Genomic DNA. Translation: AAB05590.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29240 Genomic DNA. Translation: AAB05590.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L24X-ray2.30A/B/C1-517[»]
3L7GX-ray2.70A/B/C1-517[»]
4ZWOX-ray2.14A/B1-437[»]
4ZWPX-ray2.40A/B1-437[»]
4ZWUX-ray2.20A/B1-437[»]
ProteinModelPortaliQ44238.
SMRiQ44238.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL4252.

Protein family/group databases

MEROPSiM24.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7712.
BRENDAi3.1.8.2. 275.

Miscellaneous databases

EvolutionaryTraceiQ44238.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01279. X_Pro_dipeptid. 1 hit.
InterProiIPR000994. Pept_M24.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 78 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

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.