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P00798 (PENP_PENJA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penicillopepsin

EC=3.4.23.20
Alternative name(s):
Peptidase A
OrganismPenicillium janthinellum (Penicillium vitale)
Taxonomic identifier5079 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.

Sequence similarities

Belongs to the peptidase A1 family.

Caution

The sequence shown is derived from the best amino acid sequence data as modified by the X-ray data.

Ontologies

Keywords
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Penicillopepsin
PRO_0000199515

Sites

Active site331 Ref.2
Active site2131 Ref.2

Amino acid modifications

Disulfide bond249 ↔ 283

Secondary structure

......................................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00798 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: B4124268364CBA3B

FASTA32333,461
        10         20         30         40         50         60 
AASGVATNTP TANDEEYITP VTIGGTTLNL NFDTGSADLW VFSTELPASQ QSGHSVYNPS 

        70         80         90        100        110        120 
ATGKELSGYT WSISYGDGSS ASGNVFTDSV TVGGVTAHGQ AVQAAQQISA QFQQDTNNDG 

       130        140        150        160        170        180 
LLGLAFSSIN TVQPQSQTTF FDTVKSSLAQ PLFAVALKHQ QPGVYDFGFI DSSKYTGSLT 

       190        200        210        220        230        240 
YTGVDNSQGF WSFNVDSYTA GSQSGDGFSG IADTGTTLLL LDDSVVSQYY SQVSGAQQDS 

       250        260        270        280        290        300 
NAGGYVFDCS TNLPDFSVSI SGYTATVPGS LINYGPSGDG STCLGGIQSN SGIGFSIFGD 

       310        320 
IFLKSQYVVF DSDGPQLGFA PQA 

« Hide

References

[1]"Structure and refinement of penicillopepsin at 1.8-A resolution."
James M.N.G., Sielecki A.R.
J. Mol. Biol. 163:299-361(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[2]"Amino acid sequence around the active site aspartic acid in penicillopepsin."
Sodek J., Hofmann T.
Can. J. Biochem. 48:1014-1016(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[3]Ding J., Fraser M.E., Meyer J.H., Bartlett P.A., James M.N.G.
Submitted (JUL-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
[4]"Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes."
Khan A.R., Parrish J.C., Fraser M.E., Smith W.W., Bartlett P.A., James M.N.G.
Biochemistry 37:16839-16845(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRPEPLBJ. A00991.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1APTX-ray1.80E1-323[»]
1APUX-ray1.80E1-323[»]
1APVX-ray1.80E1-323[»]
1APWX-ray1.80E1-323[»]
1BXOX-ray0.95A1-323[»]
1BXQX-ray1.41A1-323[»]
1PPKX-ray1.80E1-323[»]
1PPLX-ray1.70E1-323[»]
1PPMX-ray1.70E1-323[»]
2WEAX-ray1.25A1-323[»]
2WEBX-ray1.50A1-323[»]
2WECX-ray1.50A1-323[»]
2WEDX-ray1.50A1-323[»]
3APPX-ray1.80A1-323[»]
ProteinModelPortalP00798.
SMRP00798. Positions 1-323.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00798.
ChEMBLCHEMBL4254.

Protein family/group databases

MEROPSA01.011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00798.

Entry information

Entry namePENP_PENJA
AccessionPrimary (citable) accession number: P00798
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: December 11, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references