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Protein

Rhamnogalacturonase A

Gene

rhgA

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

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Has a positive effect in the apple hot-mash liquefaction process. 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 3.5. Unstable above pH 6.0.

Temperature dependencei

Optimum temperature is 30-50 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei215Proton donorBy similarity1
Active sitei290By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16264.
BRENDAi3.2.1.171. 488.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiRHG28B_ASPAC.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhamnogalacturonase A (EC:3.2.1.171)
Short name:
RGase A
Short name:
RHG A
Alternative name(s):
Rhamnogalacturonan hydrolase A
Gene namesi
Name:rhgA
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [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 – 18Add BLAST18
ChainiPRO_000002482519 – 440Rhamnogalacturonase AAdd BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 65
Glycosylationi50N-linked (GlcNAc...)1
Disulfide bondi217 ↔ 234
Glycosylationi317N-linked (GlcNAc...)1
Disulfide bondi340 ↔ 346
Disulfide bondi368 ↔ 377
Glycosylationi385O-linked (Man)1
Glycosylationi386O-linked (Man)1
Glycosylationi388O-linked (Man)1
Glycosylationi389O-linked (Man)1
Glycosylationi390O-linked (Man)1
Glycosylationi391O-linked (Man)1
Glycosylationi392O-linked (Man)1
Glycosylationi394O-linked (Man)1
Glycosylationi398O-linked (Man)1
Glycosylationi401O-linked (Man)1
Glycosylationi403O-linked (Man)1
Glycosylationi404O-linked (Man)1
Glycosylationi416O-linked (Man)1
Glycosylationi418O-linked (Man)1
Glycosylationi423O-linked (Man)1
Glycosylationi426O-linked (Man)1
Glycosylationi427O-linked (Man)1
Glycosylationi436O-linked (Man)1

Post-translational modificationi

The N-terminus is blocked.
N-glycosylated and may also be O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 36Combined sources7
Beta strandi38 – 40Combined sources3
Helixi41 – 44Combined sources4
Beta strandi49 – 53Combined sources5
Helixi55 – 65Combined sources11
Beta strandi70 – 73Combined sources4
Beta strandi75 – 80Combined sources6
Beta strandi84 – 88Combined sources5
Beta strandi90 – 96Combined sources7
Beta strandi98 – 102Combined sources5
Beta strandi107 – 122Combined sources16
Beta strandi124 – 126Combined sources3
Beta strandi129 – 131Combined sources3
Helixi135 – 138Combined sources4
Turni139 – 141Combined sources3
Beta strandi146 – 164Combined sources19
Beta strandi170 – 187Combined sources18
Beta strandi196 – 245Combined sources50
Beta strandi249 – 265Combined sources17
Beta strandi267 – 274Combined sources8
Beta strandi277 – 293Combined sources17
Beta strandi295 – 299Combined sources5
Beta strandi308 – 311Combined sources4
Beta strandi314 – 328Combined sources15
Turni330 – 332Combined sources3
Beta strandi335 – 339Combined sources5
Beta strandi346 – 362Combined sources17
Beta strandi364 – 375Combined sources12
Beta strandi388 – 393Combined sources6
Beta strandi415 – 417Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RMGX-ray2.00A19-440[»]
ProteinModelPortaliQ00001.
SMRiQ00001.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00001.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK18580.

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.

Q00001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALFLLALG SIPALVSGQL SGSVGPLTSA STKGATKTCN ILSYGAVADN
60 70 80 90 100
STDVGPAITS AWAACKSGGL VYIPSGNYAL NTWVTLTGGS ATAIQLDGII
110 120 130 140 150
YRTGTASGNM IAVTDTTDFE LFSSTSKGAV QGFGYVYHAE GTYGARILRL
160 170 180 190 200
TDVTHFSVHD VILVDAPAFH FTMDTCSDGE VYNMAIRGGN EGGLDGIDVW
210 220 230 240 250
GSNIWVHDVE VTNKDECVTV KSPANNILVE SIYCNWSGGC AMGSLGADTD
260 270 280 290 300
VTDIVYRNVY TWSSNQMYMI KSNGGSGTVS NVLLENFIGH GNAYSLDIDG
310 320 330 340 350
YWSSMTAVAG DGVQLNNITV KNWKGTEANG ATRPPIRVVC SDTAPCTDLT
360 370 380 390 400
LEDIAIWTES GSSELYLCRS AYGSGYCLKD SSSHTSYTTT STVTAAPSGY
410 420 430 440
SATTMAADLA TAFGLTASIP IPTIPTSFYP GLTPYSALAG
Length:440
Mass (Da):45,962
Last modified:November 1, 1996 - v1
Checksum:i3596371179A4F88F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3A → G in AAA64367 (PubMed:7961884).Curated1
Sequence conflicti11S → A in AAA64367 (PubMed:7961884).Curated1
Sequence conflicti161V → I in AAA64367 (PubMed:7961884).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80208 Genomic DNA. Translation: AAB35485.1.
X83525 Genomic DNA. Translation: CAA58507.2.
L35499 mRNA. Translation: AAA64367.1.
PIRiA55415.

Genome annotation databases

KEGGiag:AAA64367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S80208 Genomic DNA. Translation: AAB35485.1.
X83525 Genomic DNA. Translation: CAA58507.2.
L35499 mRNA. Translation: AAA64367.1.
PIRiA55415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RMGX-ray2.00A19-440[»]
ProteinModelPortaliQ00001.
SMRiQ00001.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiRHG28B_ASPAC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA64367.

Phylogenomic databases

KOiK18580.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16264.
BRENDAi3.2.1.171. 488.

Miscellaneous databases

EvolutionaryTraceiQ00001.

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...

Entry informationi

Entry nameiRHGA_ASPAC
AccessioniPrimary (citable) accession number: Q00001
Secondary accession number(s): Q00018
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 100 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, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.