PEPQ_PSEHA
ID PEPQ_PSEHA Reviewed; 440 AA.
AC P77814;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Xaa-Pro dipeptidase;
DE Short=X-Pro dipeptidase;
DE EC=3.4.13.9;
DE AltName: Full=DFPase;
DE AltName: Full=Imidodipeptidase;
DE AltName: Full=Organophosphorus acid anhydrolase;
DE Short=OPAA;
DE EC=3.1.8.2;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=pepQ; Synonyms=opa;
OS Pseudoalteromonas haloplanktis (Alteromonas haloplanktis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=228;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 211-234 AND 350-356,
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 23821 / IAM 12917 / JCM 20769 / LMG 2867 / NCIMB 1545;
RX PubMed=9079288; DOI=10.1038/sj.jim.2900358;
RA Cheng T.-C., Liu L., Wang B., Wu J., DeFrank J.J., Anderson D.M.,
RA Rastogi V.K., Hamilton A.B.;
RT "Nucleotide sequence of a gene encoding an organophosphorus nerve agent
RT degrading enzyme from Alteromonas haloplanktis.";
RL J. Ind. Microbiol. Biotechnol. 18:49-55(1997).
CC -!- FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in
CC the C-terminal position and a nonpolar amino acid at the N-terminal
CC position. Also catalyzes the hydrolysis of toxic organophosphorus
CC cholinesterase-inhibiting compounds including nerve gases such as
CC diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate
CC (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-
CC cyclohexyl methylphosphonofluoridate. {ECO:0000269|PubMed:9079288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-
CC hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diisopropyl fluorophosphate + H2O = diisopropyl phosphate +
CC fluoride + 2 H(+); Xref=Rhea:RHEA:24100, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17051, ChEBI:CHEBI:17941,
CC ChEBI:CHEBI:57896; EC=3.1.8.2;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:9079288};
CC Note=Binds 2 manganese ions per monomer. {ECO:0000305|PubMed:9079288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9079288};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:9079288};
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; U56398; AAA99824.1; -; Genomic_DNA.
DR AlphaFoldDB; P77814; -.
DR SMR; P77814; -.
DR MEROPS; M24.003; -.
DR eggNOG; COG0006; Bacteria.
DR GO; GO:0047862; F:diisopropyl-fluorophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01279; X_Pro_dipeptid; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR022846; X_Pro_dipept.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Detoxification; Dipeptidase; Direct protein sequencing; Hydrolase;
KW Manganese; Metal-binding; Metalloprotease; Protease.
FT CHAIN 1..440
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000298945"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 50481 MW; 23A50F84AF49DAA5 CRC64;
MEKLAVLYAE HIATLQQRTR TICEQEGLEG LVIHSGQAKR QFLDDMYYPF KVNPHFKAWL
PVIDNPHCWI VVNGSDKPKL IFYRPIDFWH KVPDEPRDFW AEYFDIELLL QPDQVEKLLP
YDKAKFAYIG EYLEVAQALG FSIMNPEPVL NYIHYHRAYK TQYELECLRN ANRIAVDGHK
AARDAFFNGG SEFDIQQAYL MATRQSENEM PYGNIVALNE NCAILHYTHF EPKAPQTHNS
FLIDAGANFN GYAADITRTY DFKKQGEFAD LVNAMTAHQI ELGKSLKPGL LYGDLHIDCH
NRIAQLLSDF DIVKLPAAEI VERQITSTFF PHGLGHHLGA QVHDVGGFMR DETGAHQAPP
EGHPFLRCTR LIEKNQVFTI EPGLYFIDSL LGDLAQTDNK QFINWEKVEA FKPFGGIRIE
DNIIVHEDSL ENMTRNLLLD
