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Protein

Rhamnogalacturonan acetylesterase

Gene

rha1

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 6.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei26 – 261Nucleophile1 Publication
Active sitei209 – 20911 Publication
Active sitei212 – 21211 Publication

GO - Molecular functioni

  1. hydrolase activity, acting on ester bonds Source: InterPro

GO - Biological processi

  1. lipid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16189.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhamnogalacturonan acetylesterase (EC:3.1.1.86)
Short name:
RGAE
Gene namesi
Name:rha1
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 250233Rhamnogalacturonan acetylesterasePRO_0000017852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi105 ↔ 1131 Publication
Glycosylationi121 – 1211N-linked (GlcNAc...)3 Publications
Glycosylationi199 – 1991N-linked (GlcNAc...) (high mannose)3 Publications
Disulfide bondi231 ↔ 2491 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 235Combined sources
Turni26 – 283Combined sources
Turni30 – 334Combined sources
Helixi40 – 434Combined sources
Helixi45 – 473Combined sources
Beta strandi48 – 547Combined sources
Helixi62 – 676Combined sources
Helixi70 – 778Combined sources
Beta strandi83 – 864Combined sources
Helixi96 – 983Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi120 – 1267Combined sources
Helixi127 – 14014Combined sources
Beta strandi144 – 1485Combined sources
Turni155 – 1584Combined sources
Helixi167 – 17913Combined sources
Beta strandi182 – 1843Combined sources
Helixi186 – 19712Combined sources
Helixi199 – 2046Combined sources
Beta strandi207 – 2115Combined sources
Helixi215 – 23218Combined sources
Helixi235 – 2395Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEOX-ray1.55A18-250[»]
1DEXX-ray1.90A18-250[»]
1K7CX-ray1.12A18-250[»]
1PP4X-ray2.50A/B18-250[»]
3C1UX-ray1.33A18-250[»]
ProteinModelPortaliQ00017.
SMRiQ00017. Positions 18-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00017.

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00017-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTAALAPLF FLPSALATTV YLAGDSTMAK NGGGSGTNGW GEYLASYLSA
60 70 80 90 100
TVVNDAVAGR SARSYTREGR FENIADVVTA GDYVIVEFGH NDGGSLSTDN
110 120 130 140 150
GRTDCSGTGA EVCYSVYDGV NETILTFPAY LENAAKLFTA KGAKVILSSQ
160 170 180 190 200
TPNNPWETGT FVNSPTRFVE YAELAAEVAG VEYVDHWSYV DSIYETLGNA
210 220 230 240 250
TVNSYFPIDH THTSPAGAEV VAEAFLKAVV CTGTSLKSVL TTTSFEGTCL
Length:250
Mass (Da):26,351
Last modified:November 1, 1996 - v1
Checksum:iC30676A3A876A38B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89714 Genomic DNA. Translation: CAA61858.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89714 Genomic DNA. Translation: CAA61858.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEOX-ray1.55A18-250[»]
1DEXX-ray1.90A18-250[»]
1K7CX-ray1.12A18-250[»]
1PP4X-ray2.50A/B18-250[»]
3C1UX-ray1.33A18-250[»]
ProteinModelPortaliQ00017.
SMRiQ00017. Positions 18-250.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16189.

Miscellaneous databases

EvolutionaryTraceiQ00017.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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, ACTIVE SITE.
  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.

Entry informationi

Entry nameiRHA1_ASPAC
AccessioniPrimary (citable) accession number: Q00017
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 71 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.