Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P17872 (PME_ASPTU)

Last modified September 22, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pectinesterase
      Short name=PE
    EC=3.1.1.11
Alternative name(s):
    Pectin methylesterase
Gene names
Name: pme1
OrganismAspergillus tubingensis
Taxonomic identifier5068 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in maceration and soft-rotting of plant tissue.

Catalytic activity

Pectin + n H2O = n methanol + pectate.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.

Subcellular location

Secreted.

Sequence similarities

Belongs to the pectinesterase family.

Caution

Strain RH 5344 was previously said to be from A.niger.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl esterase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell wall modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcell wall

Inferred from electronic annotation. Source: InterPro

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartyl esterase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pectinesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 331314Pectinesterase
PRO_0000023473

Sites

Active site1611Proton donor By similarity
Active site1821Nucleophile By similarity
Binding site1381Substrate By similarity
Binding site2471Substrate By similarity
Binding site2491Substrate By similarity
Site1601Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P17872-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 25B52150884C797A

FASTA33135,715
        10         20         30         40         50         60 
MVKSILASVL FAATALAASR MTAPSGAIVV AKSGGDYDTI SAAVDALSTT STETQTIFIE 

        70         80         90        100        110        120 
EGSYDEQVYI PALSGKLIVY GQTEDTTTYT SNLVNITHAI ALADVDNDDE TATLRNYAEG 

       130        140        150        160        170        180 
SAIYNLNIAN TCGQACHQAL AVSAYASEQG YYACQFTGYQ DTLLAETGYQ VYAGTYIEGA 

       190        200        210        220        230        240 
VDFIFGQHAR AWFHECDIRV LEGPSSASIT ANGRSSESDD SYYVIHKSTV AAADGNDVSS 

       250        260        270        280        290        300 
GTYYLGRPWS QYARVCFQKT SMTDVINHLG WTEWSTSTPN TENVTFVEYG NTGTGAEGPR 

       310        320        330 
ANFSSELTEP ITISWLLGSD WEDWVDTSYI N 

« Hide

References

[1]"Nucleotide and derived amino acid sequence of a pectinesterase cDNA isolated from Aspergillus niger strain RH 5344."
Khanh N.Q., Albrecht H., Ruttkowski E., Loeffler F., Gottschalk M., Jany K.-D.
Nucleic Acids Res. 18:4262-4262(1990) [PubMed: 2377474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: RH 5344.
[2]"Characterization and expression of a genomic pectin methyl esterase-encoding gene in Aspergillus niger."
Khanh N.Q., Ruttkowski E., Leidinger K., Albrecht H., Gottschalk M.
Gene 106:71-77(1991) [PubMed: 1937044] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

X52902 mRNA. Translation: CAA37084.1.
X54145 Genomic DNA. Translation: CAA38084.1.
PIRJT0589.

3D structure databases

HSSPHSSP built from PDB template 1GQ8 based on UniProtKB P83218.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.1.11. 81712.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR018040. Pectinesterase_AS.
IPR000070. Pectinesterase_cat.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF01095. Pectinesterase. 1 hit.
[Graphical view]
PROSITEPS00800. PECTINESTERASE_1. 1 hit.
PS00503. PECTINESTERASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePME_ASPTU
AccessionPrimary (citable) accession number: P17872
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 22, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents