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Reviewed, UniProtKB/Swiss-Prot Q00205 (PLYB_ASPNG)

Last modified April 14, 2009. Version 54. 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

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Names and origin

Protein namesRecommended name:
    Pectin lyase B
      Short name=PLB
    EC=4.2.2.10
Gene names
Name: pelB
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

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Ontologies

Keywords
   DomainSignal
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Molecular functionpectin lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020Or 21 Potential
Chain21 – 378358Pectin lyase B
PRO_0000024897

Sites

Active site2551 Potential

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Disulfide bond83 ↔ 102
Disulfide bond92 ↔ 225
Disulfide bond322 ↔ 330

Secondary structure

1 ............................................................................. 378
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q00205-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4FF321AF2B0B72FF

FASTA37839,703
        10         20         30         40         50         60 
MHYKLLFAAA AASLASAVSA AGVVGAAEGF AHGVTGGGSA SPVYPTTTDE LVSYLGDNEP 

        70         80         90        100        110        120 
RVIILDRTFD FTGTEGTETT TGCAPWGTAS QCQVAINLHS WCDNYQASAP KVSVTDKAGI 

       130        140        150        160        170        180 
LPITVNSNKS IVGQGTKGVI KGKGLRVVSG AKNVIIQNIA VTDINPKYVW GGDAITVDDS 

       190        200        210        220        230        240 
DLVWIDHVTT ARIGRQHIVL GTSADNRVTI SYSLIDGRSD YSATCNGHHY WGVYLDGSND 

       250        260        270        280        290        300 
MVTLKGNYFY NLSGRMPKVQ GNTLLHAVNN LFHNFDGHAF EIGTGGYVLA EGNVFQDVNI 

       310        320        330        340        350        360 
VVETPISGQL FSSPDANTNQ QCASVFGRSC QLNAFGNSGS MSGSDTSIIS KFAGKTIAAA 

       370 
HPPGNIAQWT MKNAGQGK

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References

[1]"Characterization of the Aspergillus niger pelB gene: structure and regulation of expression."
Kusters-Van Someren M., Flipphi M., de Graaff L., van den Broeck H., Kester H., Hinnen A., Visser J.
Mol. Gen. Genet. 234:113-120(1992) [PubMed: 1495474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"The tree-dimensional structure of Aspergillus niger pectin lyase B at 1.7-A resolution."
Vitali J., Schick B., Kester H.C., Visser J., Jurnak F.
Plant Physiol. 116:69-80(1998) [PubMed: 9449837] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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Cross-references

Sequence databases

X65552 Genomic DNA. Translation: CAA46521.1.
PIRS23573.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QCXX-ray1.70A21-378[»]
ModBaseSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Enzyme and pathway databases

BRENDA4.2.2.10. 277.

Family and domain databases

InterProIPR002022. Amb_allergen.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePLYB_ASPNG
AccessionPrimary (citable) accession number: Q00205
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 14, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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