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Protein

Pectin lyase B

Gene

pelB

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

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei255 – 2551Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectin lyase B (EC:4.2.2.10)
Short name:
PLB
Gene namesi
Name:pelB
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Or 21Sequence analysisAdd
BLAST
Chaini21 – 378358Pectin lyase BPRO_0000024897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi83 ↔ 102
Disulfide bondi92 ↔ 225
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence analysis
Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence analysis
Disulfide bondi322 ↔ 330

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ00205.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Turni36 – 394Combined sources
Helixi48 – 569Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 655Combined sources
Beta strandi67 – 704Combined sources
Turni72 – 754Combined sources
Beta strandi77 – 837Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 1055Combined sources
Beta strandi111 – 1166Combined sources
Helixi117 – 1193Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi238 – 2469Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi261 – 2699Combined sources
Beta strandi271 – 28212Combined sources
Beta strandi286 – 2927Combined sources
Beta strandi294 – 3029Combined sources
Beta strandi307 – 3115Combined sources
Helixi316 – 3194Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 3264Combined sources
Beta strandi334 – 3374Combined sources
Helixi346 – 3527Combined sources
Helixi363 – 3653Combined sources
Helixi366 – 3738Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QCXX-ray1.70A21-378[»]
ProteinModelPortaliQ00205.
SMRiQ00205. Positions 21-378.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00205.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHYKLLFAAA AASLASAVSA AGVVGAAEGF AHGVTGGGSA SPVYPTTTDE
60 70 80 90 100
LVSYLGDNEP RVIILDRTFD FTGTEGTETT TGCAPWGTAS QCQVAINLHS
110 120 130 140 150
WCDNYQASAP KVSVTDKAGI LPITVNSNKS IVGQGTKGVI KGKGLRVVSG
160 170 180 190 200
AKNVIIQNIA VTDINPKYVW GGDAITVDDS DLVWIDHVTT ARIGRQHIVL
210 220 230 240 250
GTSADNRVTI SYSLIDGRSD YSATCNGHHY WGVYLDGSND MVTLKGNYFY
260 270 280 290 300
NLSGRMPKVQ GNTLLHAVNN LFHNFDGHAF EIGTGGYVLA EGNVFQDVNI
310 320 330 340 350
VVETPISGQL FSSPDANTNQ QCASVFGRSC QLNAFGNSGS MSGSDTSIIS
360 370
KFAGKTIAAA HPPGNIAQWT MKNAGQGK
Length:378
Mass (Da):39,703
Last modified:November 1, 1996 - v1
Checksum:i4FF321AF2B0B72FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65552 Genomic DNA. Translation: CAA46521.1.
PIRiS23573.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65552 Genomic DNA. Translation: CAA46521.1.
PIRiS23573.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QCXX-ray1.70A21-378[»]
ProteinModelPortaliQ00205.
SMRiQ00205. Positions 21-378.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Proteomic databases

PaxDbiQ00205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ00205.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiPELB_ASPNG
AccessioniPrimary (citable) accession number: Q00205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.