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Protein

Rhamnogalacturonase A

Gene

rhgA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. Active against linseed rhamnogalacturonan.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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei215 – 2151Proton donorBy similarity
Active sitei290 – 2901By 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

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
ORF Names:AN9134
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VI
  • UP000005890 Componenti: Partially assembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AN9134.

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 – 507486Rhamnogalacturonase APRO_0000394385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 64By similarity
Disulfide bondi217 ↔ 234By similarity
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi340 ↔ 346By similarity
Disulfide bondi368 ↔ 377By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5ARE6.
SMRiQ5ARE6. Positions 18-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217527.
InParanoidiQ5ARE6.
KOiK18580.
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.

Q5ARE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYVSRLLLFL APLLVKGQLS GSVGPLTSVS SKSQTKTCNV LDYGAVADKS
60 70 80 90 100
TDIGPALSSA WDECADGGVV YIPPGDYAIE TWVKLSGGKA CAIQLDGIIY
110 120 130 140 150
RTGTDGGNMI MIEHTSDFEF FSSTSKGAFQ GYGYEFHAKG SSDGPRILRL
160 170 180 190 200
YDVSDFSVHD VALVDSPLFH FSMDTCSNGE VYNMAIRGGN MGGLDGIDVW
210 220 230 240 250
STNVWIHDVE VTNKDECVTV KSPSKNILVE NIYCNWSGGC AMGSLGTDTD
260 270 280 290 300
ISDIVYRNVY TWKSNQMYMV KSNGGSGTVS NLVLENFIGH GNAYSLDIDS
310 320 330 340 350
AWSSMSTIEG DGVELKNVTI RNWKGTEADG SQRGPIKVKC ASGAPCTDVT
360 370 380 390 400
VEDFAMWTES GDEQTYVCEN AFGDGFCLAD GDGTSTFTTT LTASAAPSGY
410 420 430 440 450
SAPSMDADLE TAFGTDSEIP IPTIPTSFYP GATPYSALAG ASVSSSQVPA
460 470 480 490 500
ASSSAEAKFV ASPATSSPTA TSTAISSVDP VSAATTTATS HGHGKSHHKH

QCRAHRH
Length:507
Mass (Da):53,449
Last modified:May 18, 2010 - v2
Checksum:iAE6347D789F560C1
GO

Sequence cautioni

The sequence CBF82482.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA61967.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490522 mRNA. Translation: ABF50898.1.
AACD01000169 Genomic DNA. Translation: EAA61967.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF82482.1. Sequence problems.
RefSeqiXP_682403.1. XM_677311.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009476; CADANIAP00009476; CADANIAG00009476.
EAA61967; EAA61967; AN9134.2.
GeneIDi2867999.
KEGGiani:AN9134.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490522 mRNA. Translation: ABF50898.1.
AACD01000169 Genomic DNA. Translation: EAA61967.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF82482.1. Sequence problems.
RefSeqiXP_682403.1. XM_677311.1.

3D structure databases

ProteinModelPortaliQ5ARE6.
SMRiQ5ARE6. Positions 18-440.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009476; CADANIAP00009476; CADANIAG00009476.
EAA61967; EAA61967; AN9134.2.
GeneIDi2867999.
KEGGiani:AN9134.2.

Organism-specific databases

EuPathDBiFungiDB:AN9134.

Phylogenomic databases

HOGENOMiHOG000217527.
InParanoidiQ5ARE6.
KOiK18580.
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

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiRHGA_EMENI
AccessioniPrimary (citable) accession number: Q5ARE6
Secondary accession number(s): C8VK67, Q1HFQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 68 of the entry and version 2 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.