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Protein

Probable rhamnogalacturonase A

Gene

rhgA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei217 – 2171Proton donorBy similarity
Active sitei292 – 2921By 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

Names & Taxonomyi

Protein namesi
Recommended name:
Probable rhamnogalacturonase A (EC:3.2.1.171)
Short name:
RGase A
Short name:
RHG A
Gene namesi
Name:rhgA
ORF Names:AO090038000552
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:AO090038000552.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 467448Probable rhamnogalacturonase APRO_0000394384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 66By similarity
Disulfide bondi219 ↔ 236By similarity
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi342 ↔ 348By similarity
Disulfide bondi370 ↔ 379By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2U293.
SMRiQ2U293. Positions 20-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217527.
KOiK18580.
OMAiVWGSNIW.
OrthoDBiEOG78H43F.

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.

Q2U293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSLSLISLA LLSPLLVNAQ LSGHVGPLTS SSSKASTKTC NVQDYGAKAD
60 70 80 90 100
KETDIGSAIE KAWDDCAEGG VVYIPSGDYA MFSRLKLSGG KASAIQLDGI
110 120 130 140 150
IYRTGSDGGN LFMIEHSSDF EFFSSTSQGA IQGLGYEFHK DGSLNGPRLL
160 170 180 190 200
RFYDVTDFSV HDVALVDSPA FHLSLDTCKN AEIYNMAIRG GDSGGLDGVD
210 220 230 240 250
IWSENVWVHD VEVTNKDECV TVKSPAKNIL VENIYCNWSG GCAMGSLGAD
260 270 280 290 300
TNISDVVYRN VYTWKSNQMY MIKSNGGSGS VSNLVLENFI GHGNAYSLDI
310 320 330 340 350
DGEWSSMSTV SGDGVQLNNI TVRNWKGTEE DGAARGPIKV VCAEKAPCTD
360 370 380 390 400
ITIDDFALWT ESGDEQTYSC ENGFGSGFCL QDGDGTSSYS TVITETAAPT
410 420 430 440 450
GYEASSMSND LSTAFGTDAS IPIPTIPTSF FPGATPYSAL AGAASGNAAK
460
ATSSATASRF RHRRGSH
Length:467
Mass (Da):49,455
Last modified:January 24, 2006 - v1
Checksum:iE592B56DD69EFC5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007169 Genomic DNA. Translation: BAE64322.1.
RefSeqiXP_001825455.1. XM_001825403.1.

Genome annotation databases

EnsemblFungiiCADAORAT00009306; CADAORAP00009119; CADAORAG00009306.
GeneIDi5997550.
KEGGiaor:AOR_1_936074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007169 Genomic DNA. Translation: BAE64322.1.
RefSeqiXP_001825455.1. XM_001825403.1.

3D structure databases

ProteinModelPortaliQ2U293.
SMRiQ2U293. Positions 20-442.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00009306; CADAORAP00009119; CADAORAG00009306.
GeneIDi5997550.
KEGGiaor:AOR_1_936074.

Organism-specific databases

EuPathDBiFungiDB:AO090038000552.

Phylogenomic databases

HOGENOMiHOG000217527.
KOiK18580.
OMAiVWGSNIW.
OrthoDBiEOG78H43F.

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. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiRHGA_ASPOR
AccessioniPrimary (citable) accession number: Q2U293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: May 11, 2016
This is version 63 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

Complete proteome, Reference proteome

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.