(data stored in ACNUC7421 zone)

SWISSPROT: PEPQ_EDWI9

ID   PEPQ_EDWI9              Reviewed;         443 AA.
AC   C5BCB6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=NT01EI_0152;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-
CC       terminal position. {ECO:0000255|HAMAP-Rule:MF_01279}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Xaa-|-Pro dipeptides; also acts
CC       on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
CC       {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; CP001600; ACR67407.1; -; Genomic_DNA.
DR   RefSeq; WP_015869623.1; NC_012779.2.
DR   ProteinModelPortal; C5BCB6; -.
DR   SMR; C5BCB6; -.
DR   STRING; 634503.NT01EI_0152; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; ACR67407; ACR67407; NT01EI_0152.
DR   GeneID; 7958752; -.
DR   KEGG; eic:NT01EI_0152; -.
DR   PATRIC; fig|634503.3.peg.143; -.
DR   eggNOG; ENOG4105D9Y; Bacteria.
DR   eggNOG; COG0006; LUCA.
DR   HOGENOM; HOG000290531; -.
DR   KO; K01271; -.
DR   OMA; MQDDTGT; -.
DR   OrthoDB; POG091H0HZN; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; 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; C5BCB6.
DR   SWISS-2DPAGE; C5BCB6.
KW   Complete proteome; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome.
FT   CHAIN         1    443       Xaa-Pro dipeptidase.
FT                                /FTId=PRO_1000214203.
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       339    339       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       384    384       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       423    423       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       423    423       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
SQ   SEQUENCE   443 AA;  49906 MW;  BDD16A6F49BB3125 CRC64;
     MDTLASLYTK HLATLQQRAR TILERHQLDG LLIHSGEPIA RFLDDQDYPF KINPYFKAWV
     PVTQVPNCWL WIDGVNKPKL WFYSPLDYWH SVSPLPQAFW TEQVEMTAQR HADDIAALLP
     AARGNVAYIG PNAERARSLG IDEAHQNPQA VLNFLHYHRA YKSEYEQACM REAQKIAVDG
     HQAALEAFRA GMSEFDINLA YLSATGQGEN DVPYDNIIAL NRHAAVLHYT HLERRAPSEM
     HSFLIDAGAE FHGYAADLTR TYAANGQSDF AALVAEVNQA QQALIATLQT GVRYTDYNLQ
     FHQRLAAILR HHHILTGISD EAAVAQGLTT PFLPHGLGHP LGLQVHDVAG FMQDELGTQM
     AAPDRYPYLR CTRIMEPGMV MTIEPGLYFI DTLLAPWLEG EFGQHFNRGR IDALRPYGGI
     RIEDNVIFHA HGVENMTRDL HLA
//

If you have problems or comments...

PBIL Back to PBIL home page