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Protein

Rhamnogalacturonase B

Gene

rhgB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins.1 Publication

Catalytic activityi

Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end.

pH dependencei

Optimum pH is 4.1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei219 – 2191Proton donorBy similarity
Active sitei294 – 2941By similarity

GO - Molecular functioni

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • pectin catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiRHG28B_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhamnogalacturonase B (EC:3.2.1.171)
Short name:
RGase B
Short name:
RHG B
Gene namesi
Name:rhgB
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 – 2121Sequence analysisAdd
BLAST
Chaini22 – 558537Rhamnogalacturonase BPRO_0000394388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 68By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi221 ↔ 238By similarity
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi344 ↔ 350By similarity
Disulfide bondi372 ↔ 381By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP87161.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00011136.

Structurei

3D structure databases

ProteinModelPortaliP87161.
SMRiP87161. Positions 22-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi442 – 52281Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHX4. Eukaryota.
ENOG4110FN4. LUCA.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P87161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLDKLSVLS FLGLAPIFAA AQLSGSVGPL TSASTKAATK TCNVLDYGAK
60 70 80 90 100
ADKSTDLGAP LASAFADCKS GGLVYVPSGD YALSTWARLS GGEAWALQID
110 120 130 140 150
GIIYRTGTDG GNMIYIEHSS DFELFSSTSE GAMQGLGYEF HADDNWSGPR
160 170 180 190 200
LLRLYEVTDF SVHDFILVDS PSFHFSLDTC TNGEIYNMAI RGGNHGGLDG
210 220 230 240 250
IDVWSNNIWV HDVEVTNKDE CVTVKGPSKN ILIESIYCNW SGGCGMGSFG
260 270 280 290 300
SDTNVSDITY RNIYTWSSNN MMLIKSNGGS GFVENVLLEN FIGHGNAYSL
310 320 330 340 350
DIDSYWASMS AVDGDGVQLS NITVKNWKGT EAYGAERGPV KVVCADGAPC
360 370 380 390 400
YDITIEDFAM WTEEGDSQWY SCESAYGSGY CLQDSDDHVS YSVTTSTVSS
410 420 430 440 450
APSGYSATSM AADLTTDFGS TVSIPIPTIP TSFYPGATPY SALMANSAST
460 470 480 490 500
AAASSIASHA TVHSSSASVA ASVPSAVAPS ESIPAATSAV VSSAAAIAPS
510 520 530 540 550
PAVGAQEGST TSAPSFAAPS GAGNSPQGPT GASGFGEKGQ QGEQGEQGEQ

GEQGVCYV
Length:558
Mass (Da):57,903
Last modified:July 1, 1997 - v1
Checksum:i34665B5E66ED0655
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94221 Genomic DNA. Translation: CAA63912.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94221 Genomic DNA. Translation: CAA63912.1.

3D structure databases

ProteinModelPortaliP87161.
SMRiP87161. Positions 22-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00011136.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiRHG28B_ASPNG.

Proteomic databases

PaxDbiP87161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IHX4. Eukaryota.
ENOG4110FN4. LUCA.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of two rhamnogalacturonan hydrolase genes from Aspergillus niger."
    Suykerbuyk M.E., Kester H.C., Schaap P.J., Stam H., Musters W., Visser J.
    Appl. Environ. Microbiol. 63:2507-2515(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Entry informationi

Entry nameiRHGB_ASPNG
AccessioniPrimary (citable) accession number: P87161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: July 1, 1997
Last modified: November 11, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.