PEPQ1_IDILO
ID PEPQ1_IDILO Reviewed; 452 AA.
AC Q5QXH5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Xaa-Pro dipeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01279};
DE Short=X-Pro dipeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01279};
DE EC=3.4.13.9 {ECO:0000255|HAMAP-Rule:MF_01279};
DE AltName: Full=Imidodipeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01279};
DE AltName: Full=Proline dipeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01279};
DE Short=Prolidase 1 {ECO:0000255|HAMAP-Rule:MF_01279};
GN Name=pepQ1 {ECO:0000255|HAMAP-Rule:MF_01279}; Synonyms=pepQ;
GN OrderedLocusNames=IL0013;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal
CC position. {ECO:0000255|HAMAP-Rule:MF_01279}.
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 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}.
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DR EMBL; AE017340; AAV80857.1; -; Genomic_DNA.
DR RefSeq; WP_011233277.1; NC_006512.1.
DR AlphaFoldDB; Q5QXH5; -.
DR SMR; Q5QXH5; -.
DR STRING; 283942.IL0013; -.
DR EnsemblBacteria; AAV80857; AAV80857; IL0013.
DR KEGG; ilo:IL0013; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OMA; HRDKNEN; -.
DR OrthoDB; 415910at2; -.
DR Proteomes; UP000001171; 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 GO; GO:0006508; P:proteolysis; 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; 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;
KW Dipeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..452
FT /note="Xaa-Pro dipeptidase 1"
FT /id="PRO_0000303847"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 383
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ SEQUENCE 452 AA; 51104 MW; C5B203E44B89BA1C CRC64;
MTATADLWPL FPDHIKQLQT RAERLFKREN LDLVAIHSGQ QKRWFLDDMN YPFRANPHFK
AWCPETQLAN AWVILKPNTR PTLVLLSSPD FWHTTASLEG APWLEEFHVE HISSPEAIEK
LLPYDKKSAA YLGEHIEVAK ALGFENINPD PVLHFFHYHR LFKTDYEIAC LTQANHIAAE
GHVAAADAFF NGASEFDCLL KYMAATRQGQ NEVPYNHIIG QNENASVLHH WMPDKKASGS
LKSMLVDAGA EVCGYAADIS RTWSKQHNEY EELIAALDQI TLALIDKMKP GVEFPALHQL
AHEQIANVLF AFGFVSCSPE QMIEDGITTV FLPHGLGHPL GLQVHDVGAA QADERGTPIA
PPSGHLTLKT TRTVEPRQVY TIEPGIYFIE PLLQKLANSR NKHLINWRRV DEFKPFGGVR
IEDNIVVYRE RNDNLTRQTA LDAYVKKVTR LA
