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Q00017 (RHA1_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhamnogalacturonan acetylesterase

Short name=RGAE
EC=3.1.1.86
Gene names
Name:rha1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B). Ref.1

Catalytic activity

Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of alpha-D-galacturonic acid in rhamnogalacturonan I. Ref.1

Post-translational modification

Carbohydrate at Asn-199 is composed of GlcNAc and Man.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionhydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1
Chain18 – 250233Rhamnogalacturonan acetylesterase
PRO_0000017852

Sites

Active site261Nucleophile Probable
Active site2091
Active site2121

Amino acid modifications

Glycosylation1211N-linked (GlcNAc...) Ref.3 Ref.4 Ref.5
Glycosylation1991N-linked (GlcNAc...) (high mannose) Ref.3 Ref.4 Ref.5
Disulfide bond105 ↔ 113 Ref.5
Disulfide bond231 ↔ 249 Ref.5

Secondary structure

............................................. 250
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00017 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C30676A3A876A38B

FASTA25026,351
        10         20         30         40         50         60 
MKTAALAPLF FLPSALATTV YLAGDSTMAK NGGGSGTNGW GEYLASYLSA TVVNDAVAGR 

        70         80         90        100        110        120 
SARSYTREGR FENIADVVTA GDYVIVEFGH NDGGSLSTDN GRTDCSGTGA EVCYSVYDGV 

       130        140        150        160        170        180 
NETILTFPAY LENAAKLFTA KGAKVILSSQ TPNNPWETGT FVNSPTRFVE YAELAAEVAG 

       190        200        210        220        230        240 
VEYVDHWSYV DSIYETLGNA TVNSYFPIDH THTSPAGAEV VAEAFLKAVV CTGTSLKSVL 

       250 
TTTSFEGTCL 

« Hide

References

[1]"Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Synergism between rhamnogalacturonan degrading enzymes."
Kauppinen S., Christgau S., Kofod L.V., Halkier T., Doerreich K., Dalboege H.
J. Biol. Chem. 270:27172-27178(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-45, FUNCTION, CATALYTIC ACTIVITY.
Strain: KSM 510.
[2]"Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus."
Moelgaard A., Petersen J.F.W., Kauppinen S., Dalboege H., Johnsen A.H., Navarro Poulsen J.-C., Larsen S.
Acta Crystallogr. D 54:1026-1029(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[3]"Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases."
Moelgaard A., Kauppinen S., Larsen S.
Structure 8:373-383(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND ASN-199, STRUCTURE OF CARBOHYDRATE.
[4]"A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase."
Moelgaard A., Larsen S.
Acta Crystallogr. D 58:111-119(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), GLYCOSYLATION AT ASN-121 AND ASN-199, STRUCTURE OF CARBOHYDRATE.
[5]"Short strong hydrogen bonds in proteins: a case study of rhamnogalacturonan acetylesterase."
Langkilde A., Kristensen S.M., Lo Leggio L., Molgaard A., Jensen J.H., Houk A.R., Navarro Poulsen J.C., Kauppinen S., Larsen S.
Acta Crystallogr. D 64:851-863(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 18-250, DISULFIDE BONDS, GLYCOSYLATION AT ASN-121 AND ASN-199.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89714 Genomic DNA. Translation: CAA61858.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEOX-ray1.55A18-250[»]
1DEXX-ray1.90A18-250[»]
1K7CX-ray1.12A18-250[»]
1PP4X-ray2.50A/B18-250[»]
3C1UX-ray1.33A18-250[»]
ProteinModelPortalQ00017.
SMRQ00017. Positions 18-250.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16189.

Family and domain databases

Gene3D3.40.50.1110. 1 hit.
InterProIPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ00017.

Entry information

Entry nameRHA1_ASPAC
AccessionPrimary (citable) accession number: Q00017
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references