PEPD_DICDI
ID PEPD_DICDI Reviewed; 501 AA.
AC Q55E60;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Xaa-Pro dipeptidase;
DE Short=X-Pro dipeptidase;
DE EC=3.4.13.9;
DE AltName: Full=Imidodipeptidase;
DE AltName: Full=Peptidase D;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=pepd; Synonyms=prd; ORFNames=DDB_G0269382;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 49-56 AND 491-501, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Splits dipeptides with a prolyl or hydroxyprolyl residue in
CC the C-terminal position. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type
CC prolidase subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72041.1; -; Genomic_DNA.
DR RefSeq; XP_645921.1; XM_640829.1.
DR AlphaFoldDB; Q55E60; -.
DR SMR; Q55E60; -.
DR STRING; 44689.DDB0266378; -.
DR MEROPS; M24.007; -.
DR PaxDb; Q55E60; -.
DR EnsemblProtists; EAL72041; EAL72041; DDB_G0269382.
DR GeneID; 8616862; -.
DR KEGG; ddi:DDB_G0269382; -.
DR dictyBase; DDB_G0269382; pepD.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; Q55E60; -.
DR OMA; DQKFIYN; -.
DR PhylomeDB; Q55E60; -.
DR PRO; PR:Q55E60; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Dipeptidase; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..501
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000328066"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 56426 MW; 359939E7B9E35E3A CRC64;
MSVHPRNQGK DDCCEKTHLD SQYSPGYYWL GNNTLKVPLV LHKENRQRLV SQILSKHKDQ
VKENSFILLE SGKSTMQYDT DHEPLFKQER YFFWTFGSDI PDCFGIVGLD EQATSILCIP
KLPAEYATWM GEIRSKEYYK SIFLVDQVLY VDEMMDYLKS KNASTIYTIL GTNTDSGSTF
VEPQYPGLRE TFNVNNTLLF PEIAECRVIK SPKEVEVIRY CVDASVSAHK HVMRKVKVGL
KEYQCESEFL HHVYNEWGCR NVGYTCICAA NKNSAVLHYG HAGEPNSATI SENGFCLFDM
GAEYHSYTAD ITCSFPATGK FSPEQRVVYQ AVLDASVAVM EAMRPGVSWV DMHKLAERCI
LAALLKAGIL VGDLQDLIAN KIGSVFFPHG LGHFLGLDTH DVGGYLGDCQ PKVHSLRTTR
TLKAGMVITS EPGCYFINHL LTQALSNPET AKFFNLTELD KYRNIGGVRI EDDILVTETG
CDNLSKNLPR TIDEIEAFML K
