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Protein

Proline iminopeptidase

Gene

pip

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically catalyzes the removal of N-terminal proline residues from peptides.

Catalytic activityi

Release of N-terminal proline from a peptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei113 – 1131Nucleophile
Active sitei268 – 2681
Active sitei296 – 2961Proton donor

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1431-MONOMER.
BRENDAi3.4.11.5. 5690.

Protein family/group databases

ESTHERiserma-impep. Proline_iminopeptidase.
MEROPSiS33.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline iminopeptidase (EC:3.4.11.5)
Short name:
PIP
Alternative name(s):
Prolyl aminopeptidase
Short name:
PAP
Gene namesi
Name:pip
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Proline iminopeptidasePRO_0000080845Add
BLAST

Interactioni

Subunit structurei

Monomer.

Chemistry

BindingDBiO32449.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207Combined sources
Beta strandi22 – 243Combined sources
Beta strandi26 – 338Combined sources
Beta strandi37 – 437Combined sources
Turni46 – 483Combined sources
Helixi53 – 586Combined sources
Turni61 – 633Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 743Combined sources
Helixi88 – 10114Combined sources
Beta strandi105 – 1128Combined sources
Helixi114 – 12512Combined sources
Helixi127 – 1293Combined sources
Beta strandi130 – 1378Combined sources
Helixi143 – 1508Combined sources
Helixi154 – 1563Combined sources
Helixi159 – 1668Combined sources
Helixi173 – 1753Combined sources
Helixi177 – 1859Combined sources
Helixi190 – 20516Combined sources
Beta strandi208 – 2114Combined sources
Helixi214 – 2207Combined sources
Helixi222 – 23716Combined sources
Helixi239 – 2413Combined sources
Helixi247 – 2504Combined sources
Helixi252 – 2554Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi269 – 2713Combined sources
Helixi273 – 28210Combined sources
Beta strandi286 – 2916Combined sources
Helixi301 – 31414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QTRX-ray2.32A1-317[»]
1WM1X-ray2.10A1-317[»]
1X2BX-ray2.40A1-317[»]
1X2EX-ray2.40A1-317[»]
ProteinModelPortaliO32449.
SMRiO32449. Positions 4-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32449.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006431. Pept_S33. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01249. pro_imino_pep_1. 1 hit.

Sequencei

Sequence statusi: Complete.

O32449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQLRGLYPP LAAYDSGWLD TGDGHRIYWE LSGNPNGKPA VFIHGGPGGG
60 70 80 90 100
ISPHHRQLFD PERYKVLLFD QRGCGRSRPH ASLDNNTTWH LVADIERLRE
110 120 130 140 150
MAGVEQWLVF GGSWGSTLAL AYAQTHPERV SEMVLRGIFT LRKQRLHWYY
160 170 180 190 200
QDGASRFFPE KWERVLSILS DDERKDVIAA YRQRLTSADP QVQLEAAKLW
210 220 230 240 250
SVWEGETVTL LPSRESASFG EDDFALAFAR IENHYFTHLG FLESDDQLLR
260 270 280 290 300
NVPLIRHIPA VIVHGRYDMA CQVQNAWDLA KAWPEAELHI VEGAGHSYDE
310
PGILHQLMIA TDRFAGK
Length:317
Mass (Da):36,084
Last modified:January 1, 1998 - v1
Checksum:i48A427C9B97D972D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87897 Genomic DNA. Translation: BAA23336.1.
PIRiJC5696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87897 Genomic DNA. Translation: BAA23336.1.
PIRiJC5696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QTRX-ray2.32A1-317[»]
1WM1X-ray2.10A1-317[»]
1X2BX-ray2.40A1-317[»]
1X2EX-ray2.40A1-317[»]
ProteinModelPortaliO32449.
SMRiO32449. Positions 4-317.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiO32449.
ChEMBLiCHEMBL1075256.

Protein family/group databases

ESTHERiserma-impep. Proline_iminopeptidase.
MEROPSiS33.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1431-MONOMER.
BRENDAi3.4.11.5. 5690.

Miscellaneous databases

EvolutionaryTraceiO32449.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR002410. Peptidase_S33.
IPR005944. Pro_iminopeptidase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006431. Pept_S33. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01249. pro_imino_pep_1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Prolyl aminopeptidase from Serratia marcescens: cloning of the enzyme gene and crystallization of the expressed enzyme."
    Kabashima T., Kitazono A., Kitano A., Ito K., Yoshimoto T.
    J. Biochem. 122:601-605(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens."
    Ito K., Inoue T., Kabashima T., Kanada N., Huang H.S., Ma X., Azmi N., Azab E., Yoshimoto T.
    J. Biochem. 128:673-678(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  3. "Crystal structure of prolyl aminopeptidase from Serratia marcescens."
    Yoshimoto T., Kabashima T., Uchikawa K., Inoue T., Tanaka N., Nakamura K.T., Tsuru M., Ito K.
    J. Biochem. 126:559-565(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).

Entry informationi

Entry nameiPIP_SERMA
AccessioniPrimary (citable) accession number: O32449
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: October 14, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.