PEPQ_PYRHO
ID PEPQ_PYRHO Reviewed; 351 AA.
AC O58885;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Xaa-Pro dipeptidase;
DE Short=X-Pro dipeptidase;
DE EC=3.4.13.9;
DE AltName: Full=Imidodipeptidase;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=pepQ; OrderedLocusNames=PH1149;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RA Mizutani M., Kunishima N.;
RT "Crystal structure of the prolidase from Pyrococcus horikoshii OT3.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Splits dipeptides with a prolyl in the C-terminal position
CC and a nonpolar amino acid at the N-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=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|Ref.2};
CC Note=Binds 2 cobalt ions per subunit. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Archaeal-type
CC prolidase subfamily. {ECO:0000305}.
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DR EMBL; BA000001; BAA30249.1; -; Genomic_DNA.
DR PIR; G71056; G71056.
DR PDB; 1WY2; X-ray; 1.70 A; A/B=1-351.
DR PDBsum; 1WY2; -.
DR AlphaFoldDB; O58885; -.
DR SMR; O58885; -.
DR STRING; 70601.3257566; -.
DR MEROPS; M24.008; -.
DR PRIDE; O58885; -.
DR EnsemblBacteria; BAA30249; BAA30249; BAA30249.
DR KEGG; pho:PH1149; -.
DR eggNOG; arCOG01000; Archaea.
DR OMA; YCSDRTR; -.
DR BRENDA; 3.4.13.9; 5244.
DR EvolutionaryTrace; O58885; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Cytoplasm; Dipeptidase; Hydrolase; Metal-binding;
KW Metalloprotease; Protease.
FT CHAIN 1..351
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000185094"
FT BINDING 212
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 223
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 223
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 287
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 316
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 330
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 330
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 235..254
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:1WY2"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1WY2"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1WY2"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1WY2"
SQ SEQUENCE 351 AA; 39401 MW; 38CB76FFFB766A7E CRC64;
MDIMNEKVKK IIEFMDKNSI DAVLIAKNPN VYYISGASPL AGGYILITGE SATLYVPELE
YEMAKEESNI PVEKFKKMDE FYKALEGIKS LGIESSLPYG FIEELKKKAN IKEFKKVDDV
IRDMRIIKSE KEIKIIEKAC EIADKAVMAA IEEITEGKKE REVAAKVEYL MKMNGAEKPA
FDTIIASGYR SALPHGVASD KRIERGDLVV IDLGALYQHY NSDITRTIVV GSPNEKQKEI
YEIVLEAQKK AVESAKPGIT AKELDSIARN IIAEYGYGEY FNHSLGHGVG LEVHEWPRVS
QYDETVLREG MVITIEPGIY IPKIGGVRIE DTILITKNGS KRLTKTEREL I
