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Protein

Rhamnogalacturonase A

Gene

rhgA

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 3.6.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161Proton donorBy 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.
mycoCLAPiRHG28A_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhamnogalacturonase A (EC:3.2.1.171)
Short name:
RGase A
Short name:
RHG A
Gene namesi
Name:rhgA
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 – 1818Sequence analysisAdd
BLAST
Chaini19 – 446428Rhamnogalacturonase APRO_0000394383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 65By similarity
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence analysis
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence analysis
Disulfide bondi218 ↔ 235By similarity
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi341 ↔ 347By similarity
Disulfide bondi369 ↔ 378By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP87160.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00009366.

Structurei

3D structure databases

ProteinModelPortaliP87160.
SMRiP87160. Positions 19-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi385 – 42743Thr-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.

P87160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALPILALA LAPLLVNGQL SGSVGPLTSA HSKAATKTCN VLDYGAVADN
60 70 80 90 100
STDIGSALSE AWDACSDGGL IYIPPGDYAM DTWVSLSGGK ATAIILDGTI
110 120 130 140 150
YRTGTDGGNM ILVENSSDFE LYSNSSSGAV QGFGYVYHRE GDLDGPRILR
160 170 180 190 200
LQDVSNFAVH DIILVDAPAF HFVMDDCSDG EVYNMAIRGG NSGGLDGIDV
210 220 230 240 250
WGSNIWVHDV EVTNKDECVT VKGPANNILV ESIYCNWSGG CAMGSLGADT
260 270 280 290 300
DITDILYRNV YTWSSNQMYM IKSNGGSGTV NNTLLENFIG RGNRYSLDVD
310 320 330 340 350
SYWSSMTAVD GDGVQLSNIT FKNWKGTEAD GAERGPIKVV CSDTAPCTDI
360 370 380 390 400
TIEDFAMWTE SGDEQTYTCE SAYGDGFCLE DSDSTTSYTT TQTVTTAPSG
410 420 430 440
YSATTMAADL TTDFGTTASI PIPTIPTSFY PGLTAISPLA SAATTA
Length:446
Mass (Da):47,045
Last modified:July 1, 1997 - v1
Checksum:iD3772360D4464FA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94220 Genomic DNA. Translation: CAA63911.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94220 Genomic DNA. Translation: CAA63911.1.

3D structure databases

ProteinModelPortaliP87160.
SMRiP87160. Positions 19-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00009366.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiRHG28A_ASPNG.

Proteomic databases

PaxDbiP87160.

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 nameiRHGA_ASPNG
AccessioniPrimary (citable) accession number: P87160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: July 1, 1997
Last modified: November 11, 2015
This is version 71 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.