PIP_SERMA
ID PIP_SERMA Reviewed; 317 AA.
AC O32449;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Proline iminopeptidase;
DE Short=PIP;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
DE Short=PAP;
GN Name=pip;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9348090; DOI=10.1093/oxfordjournals.jbchem.a021795;
RA Kabashima T., Kitazono A., Kitano A., Ito K., Yoshimoto T.;
RT "Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene
RT and crystallization of the expressed enzyme.";
RL J. Biochem. 122:601-605(1997).
RN [2]
RP MUTAGENESIS.
RX PubMed=11011150; DOI=10.1093/oxfordjournals.jbchem.a022800;
RA Ito K., Inoue T., Kabashima T., Kanada N., Huang H.S., Ma X., Azmi N.,
RA Azab E., Yoshimoto T.;
RT "Substrate recognition mechanism of prolyl aminopeptidase from Serratia
RT marcescens.";
RL J. Biochem. 128:673-678(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
RX PubMed=10467172; DOI=10.1093/oxfordjournals.jbchem.a022486;
RA Yoshimoto T., Kabashima T., Uchikawa K., Inoue T., Tanaka N.,
RA Nakamura K.T., Tsuru M., Ito K.;
RT "Crystal structure of prolyl aminopeptidase from Serratia marcescens.";
RL J. Biochem. 126:559-565(1999).
CC -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline
CC residues from peptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; D87897; BAA23336.1; -; Genomic_DNA.
DR PIR; JC5696; JC5696.
DR PDB; 1QTR; X-ray; 2.32 A; A=1-317.
DR PDB; 1WM1; X-ray; 2.10 A; A=1-317.
DR PDB; 1X2B; X-ray; 2.40 A; A=1-317.
DR PDB; 1X2E; X-ray; 2.40 A; A=1-317.
DR PDBsum; 1QTR; -.
DR PDBsum; 1WM1; -.
DR PDBsum; 1X2B; -.
DR PDBsum; 1X2E; -.
DR AlphaFoldDB; O32449; -.
DR SMR; O32449; -.
DR STRING; 273526.SMDB11_1211; -.
DR BindingDB; O32449; -.
DR ChEMBL; CHEMBL1075256; -.
DR DrugBank; DB07391; (2S)-2-AMINO-1-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)PROPAN-1-ONE.
DR DrugBank; DB08576; 1-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)-2-(METHYLAMINO)ETHANONE.
DR DrugBank; DB03833; 2-Prolyl-5-Tert-Butyl-[1,3,4]Oxadiazole.
DR ESTHER; serma-impep; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR BRENDA; 3.4.11.5; 5690.
DR EvolutionaryTrace; O32449; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR PANTHER; PTHR43722; PTHR43722; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Protease.
FT CHAIN 1..317
FT /note="Proline iminopeptidase"
FT /id="PRO_0000080845"
FT DOMAIN 41..296
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 113
FT /note="Nucleophile"
FT ACT_SITE 268
FT ACT_SITE 296
FT /note="Proton donor"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1WM1"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1WM1"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1QTR"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1WM1"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:1WM1"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:1WM1"
SQ SEQUENCE 317 AA; 36084 MW; 48A427C9B97D972D CRC64;
MEQLRGLYPP LAAYDSGWLD TGDGHRIYWE LSGNPNGKPA VFIHGGPGGG ISPHHRQLFD
PERYKVLLFD QRGCGRSRPH ASLDNNTTWH LVADIERLRE MAGVEQWLVF GGSWGSTLAL
AYAQTHPERV SEMVLRGIFT LRKQRLHWYY QDGASRFFPE KWERVLSILS DDERKDVIAA
YRQRLTSADP QVQLEAAKLW SVWEGETVTL LPSRESASFG EDDFALAFAR IENHYFTHLG
FLESDDQLLR NVPLIRHIPA VIVHGRYDMA CQVQNAWDLA KAWPEAELHI VEGAGHSYDE
PGILHQLMIA TDRFAGK
