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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)DescriptionActionsGraphical viewLength
Active sitei255Sequence analysis1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Or 21Sequence analysisAdd BLAST20
ChainiPRO_000002489721 – 378Pectin lyase BAdd BLAST358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi83 ↔ 102
Disulfide bondi92 ↔ 225
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1
Glycosylationi251N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi322 ↔ 330

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ00205.
PRIDEiQ00205.

Structurei

Secondary structure

1378
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 31Combined sources3
Turni36 – 39Combined sources4
Helixi48 – 56Combined sources9
Beta strandi57 – 59Combined sources3
Beta strandi61 – 65Combined sources5
Beta strandi67 – 70Combined sources4
Turni72 – 75Combined sources4
Beta strandi77 – 83Combined sources7
Beta strandi94 – 96Combined sources3
Helixi98 – 100Combined sources3
Helixi101 – 105Combined sources5
Beta strandi111 – 116Combined sources6
Helixi117 – 119Combined sources3
Beta strandi127 – 133Combined sources7
Beta strandi139 – 142Combined sources4
Beta strandi145 – 148Combined sources4
Beta strandi154 – 158Combined sources5
Beta strandi160 – 164Combined sources5
Beta strandi174 – 179Combined sources6
Beta strandi183 – 187Combined sources5
Beta strandi189 – 195Combined sources7
Beta strandi197 – 200Combined sources4
Beta strandi206 – 212Combined sources7
Beta strandi214 – 216Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi225 – 230Combined sources6
Beta strandi233 – 235Combined sources3
Beta strandi238 – 246Combined sources9
Beta strandi248 – 252Combined sources5
Beta strandi261 – 269Combined sources9
Beta strandi271 – 282Combined sources12
Beta strandi286 – 292Combined sources7
Beta strandi294 – 302Combined sources9
Beta strandi307 – 311Combined sources5
Helixi316 – 319Combined sources4
Helixi320 – 322Combined sources3
Helixi323 – 326Combined sources4
Beta strandi334 – 337Combined sources4
Helixi346 – 352Combined sources7
Helixi363 – 365Combined sources3
Helixi366 – 373Combined sources8

3D structure databases

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

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Proteomic databases

PaxDbiQ00205.
PRIDEiQ00205.

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...

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 2, 2016
This is version 82 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.