(data stored in ACNUC7421 zone)

SWISSPROT: PEPQ_AERHH

ID   PEPQ_AERHH              Reviewed;         440 AA.
AC   A0KEL3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Xaa-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=X-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            EC=3.4.13.9 {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Imidodipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Proline dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=Prolidase {ECO:0000255|HAMAP-Rule:MF_01279};
GN   Name=pepQ {ECO:0000255|HAMAP-Rule:MF_01279};
GN   OrderedLocusNames=AHA_0141;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-
CC       terminal position. {ECO:0000255|HAMAP-Rule:MF_01279}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on
CC         aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.;
CC         EC=3.4.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01279};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01279};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01279};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type
CC       prolidase subfamily. {ECO:0000255|HAMAP-Rule:MF_01279}.
DR   EMBL; CP000462; ABK36051.1; -; Genomic_DNA.
DR   RefSeq; WP_011704167.1; NC_008570.1.
DR   RefSeq; YP_854678.1; NC_008570.1.
DR   SMR; A0KEL3; -.
DR   STRING; 380703.AHA_0141; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; ABK36051; ABK36051; AHA_0141.
DR   GeneID; 4490322; -.
DR   KEGG; aha:AHA_0141; -.
DR   PATRIC; fig|380703.7.peg.135; -.
DR   eggNOG; ENOG4105D9Y; Bacteria.
DR   eggNOG; COG0006; LUCA.
DR   HOGENOM; HOG000290531; -.
DR   KO; K01271; -.
DR   OMA; MQDDTGT; -.
DR   BioCyc; AHYD380703:G1G7B-141-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro.
DR   GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.350.10; -; 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; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   InterPro; IPR022846; X_Pro_dipept.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KEL3.
DR   SWISS-2DPAGE; A0KEL3.
KW   Complete proteome; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome.
FT   CHAIN         1    440       Xaa-Pro dipeptidase.
FT                                /FTId=PRO_0000303837.
FT   METAL       246    246       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       257    257       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       257    257       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       337    337       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       382    382       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       421    421       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       421    421       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
SQ   SEQUENCE   440 AA;  50049 MW;  89AFC06646CB643D CRC64;
     MSSYSQLFAQ HLDTLQQRTR DILQQQGLSG LAIHSGQTHR IFLDDQDYPF KVNPQFKAWL
     PVLDNPHCWL LVDGVNKPVL LFYRPVDFWH KVAELPNAFW VDFFDIRFLT RPEQVADHLP
     ANKQEWAYLG GHLEVAELLG LGQPNPEAVL NYLHYHRAYK TAYELECLRD ANRIGVRGHI
     AAKDSFMAGA SEFEINLAYM KAVGQGANEA PYGNIVAINR NAAILHYTHL SAQRVPDAER
     YSFLIDAGVD VHGYASDITR TWAWRRGEFA DLIAALDAQQ QEIIEEIKPG RRYSELHLQM
     HHRLARLLQA TELVDMSVDE MIHTGVTNVF FPHGLGHFLG LQVHDAGGFM QDERGTHLSA
     PEQFPYLRCT RVMEVGQVFT IEPGLYFIDS LLEPLRLGEQ GKRVNWNKVE ALRPYGGIRI
     EDNVVLHANG VENLTRQAGL
//

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