(data stored in ACNUC7421 zone)

SWISSPROT: PEPQ_PSEHT

ID   PEPQ_PSEHT              Reviewed;         440 AA.
AC   Q3IJ21;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, 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=PSHAa0013;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85127.1; -; Genomic_DNA.
DR   RefSeq; WP_011326745.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ21; -.
DR   SMR; Q3IJ21; -.
DR   STRING; 326442.PSHAa0013; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; CAI85127; CAI85127; PSHAa0013.
DR   KEGG; pha:PSHAa0013; -.
DR   PATRIC; fig|326442.8.peg.15; -.
DR   eggNOG; ENOG4105D9Y; Bacteria.
DR   eggNOG; COG0006; LUCA.
DR   HOGENOM; HOG000290531; -.
DR   KO; K01271; -.
DR   OMA; MQDDTGT; -.
DR   OrthoDB; POG091H0HZN; -.
DR   Proteomes; UP000006843; Chromosome I.
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   HAMAP; MF_01279; X_Pro_dipeptid; 1.
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; Q3IJ21.
DR   SWISS-2DPAGE; Q3IJ21.
KW   Complete proteome; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome.
FT   CHAIN         1    440       Xaa-Pro dipeptidase.
FT                                /FTId=PRO_0000303852.
FT   METAL       244    244       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       255    255       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       255    255       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       336    336       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       381    381       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       420    420       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
FT   METAL       420    420       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01279}.
SQ   SEQUENCE   440 AA;  50460 MW;  53AC70BCC55B6E23 CRC64;
     MDKLAVLYAE HIATLQQRTR TICEREGLEG LVIHSGQAKR QFLDDMYYPF KVNPHFKAWL
     PVLDNPHCWI VVNGSDKPKL IFYRPVDFWH KVPDEPRDFW AEYFDIELLL QPDQVEKLLP
     YDKANYAYVG EYLEVAQALG FSVMNPEPVL NYFHYHRAYK TQYELECLRN ANRIAVDGHK
     AARDTFFNGG SEFDIQQAYL MATRQSENEM PYGNIVALNE NCAILHYTHF EAKAPQQHNS
     FLIDAGANFN GYAADITRTY DFKKQGEFAE LVQAMTAAQI ELGTGLKPGM LYGDLHVECH
     NRVAQILSDF DIVKLPAEEI VERKITSTFF PHGLGHHLGL QVHDMGGFMA DEMGAQQAAP
     EGHPFLRCTR IIEKNQVFTI EPGLYFIDSL LGDLAQTDNK QFINWQKVES FKPYGGIRIE
     DNIIVHEDSL ENMTRNLALD
//

If you have problems or comments...

PBIL Back to PBIL home page