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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)DescriptionActionsGraphical viewLength
Active sitei113Nucleophile1
Active sitei2681
Active sitei296Proton donor1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000808451 – 317Proline iminopeptidaseAdd BLAST317

Interactioni

Subunit structurei

Monomer.

Chemistry databases

BindingDBiO32449.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 20Combined sources7
Beta strandi22 – 24Combined sources3
Beta strandi26 – 33Combined sources8
Beta strandi37 – 43Combined sources7
Turni46 – 48Combined sources3
Helixi53 – 58Combined sources6
Turni61 – 63Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 74Combined sources3
Helixi88 – 101Combined sources14
Beta strandi105 – 112Combined sources8
Helixi114 – 125Combined sources12
Helixi127 – 129Combined sources3
Beta strandi130 – 137Combined sources8
Helixi143 – 150Combined sources8
Helixi154 – 156Combined sources3
Helixi159 – 166Combined sources8
Helixi173 – 175Combined sources3
Helixi177 – 185Combined sources9
Helixi190 – 205Combined sources16
Beta strandi208 – 211Combined sources4
Helixi214 – 220Combined sources7
Helixi222 – 237Combined sources16
Helixi239 – 241Combined sources3
Helixi247 – 250Combined sources4
Helixi252 – 255Combined sources4
Beta strandi260 – 265Combined sources6
Beta strandi269 – 271Combined sources3
Helixi273 – 282Combined sources10
Beta strandi286 – 291Combined sources6
Helixi301 – 314Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO32449.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 296AB hydrolase-1Sequence analysisAdd BLAST256

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QTRX-ray2.32A1-317[»]
1WM1X-ray2.10A1-317[»]
1X2BX-ray2.40A1-317[»]
1X2EX-ray2.40A1-317[»]
ProteinModelPortaliO32449.
SMRiO32449.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiO32449.
ChEMBLiCHEMBL1075256.

Protein family/group databases

ESTHERiserma-impep. Proline_iminopeptidase.
MEROPSiS33.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

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...

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: November 2, 2016
This is version 98 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.