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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei215 – 2151Proton donorBy similarity
Active sitei290 – 2901By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 440422Rhamnogalacturonase APRO_0000024825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 65
Glycosylationi50 – 501N-linked (GlcNAc...)
Disulfide bondi217 ↔ 234
Glycosylationi317 – 3171N-linked (GlcNAc...)
Disulfide bondi340 ↔ 346
Disulfide bondi368 ↔ 377
Glycosylationi385 – 3851O-linked (Man)
Glycosylationi386 – 3861O-linked (Man)
Glycosylationi388 – 3881O-linked (Man)
Glycosylationi389 – 3891O-linked (Man)
Glycosylationi390 – 3901O-linked (Man)
Glycosylationi391 – 3911O-linked (Man)
Glycosylationi392 – 3921O-linked (Man)
Glycosylationi394 – 3941O-linked (Man)
Glycosylationi398 – 3981O-linked (Man)
Glycosylationi401 – 4011O-linked (Man)
Glycosylationi403 – 4031O-linked (Man)
Glycosylationi404 – 4041O-linked (Man)
Glycosylationi416 – 4161O-linked (Man)
Glycosylationi418 – 4181O-linked (Man)
Glycosylationi423 – 4231O-linked (Man)
Glycosylationi426 – 4261O-linked (Man)
Glycosylationi427 – 4271O-linked (Man)
Glycosylationi436 – 4361O-linked (Man)

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 367Combined sources
Beta strandi38 – 403Combined sources
Helixi41 – 444Combined sources
Beta strandi49 – 535Combined sources
Helixi55 – 6511Combined sources
Beta strandi70 – 734Combined sources
Beta strandi75 – 806Combined sources
Beta strandi84 – 885Combined sources
Beta strandi90 – 967Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi107 – 12216Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi129 – 1313Combined sources
Helixi135 – 1384Combined sources
Turni139 – 1413Combined sources
Beta strandi146 – 16419Combined sources
Beta strandi170 – 18718Combined sources
Beta strandi196 – 24550Combined sources
Beta strandi249 – 26517Combined sources
Beta strandi267 – 2748Combined sources
Beta strandi277 – 29317Combined sources
Beta strandi295 – 2995Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi314 – 32815Combined sources
Turni330 – 3323Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi346 – 36217Combined sources
Beta strandi364 – 37512Combined sources
Beta strandi388 – 3936Combined sources
Beta strandi415 – 4173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RMGX-ray2.00A19-440[»]
ProteinModelPortaliQ00001.
SMRiQ00001. Positions 19-440.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31A → G in AAA64367 (PubMed:7961884).Curated
Sequence conflicti11 – 111S → A in AAA64367 (PubMed:7961884).Curated
Sequence conflicti161 – 1611V → I in AAA64367 (PubMed:7961884).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RMGX-ray2.00A19-440[»]
ProteinModelPortaliQ00001.
SMRiQ00001. Positions 19-440.
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: May 11, 2016
This is version 98 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.