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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)DescriptionActionsGraphical viewLength
Active sitei26Nucleophile1 Publication1
Active sitei2091 Publication1
Active sitei2121 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16189.
BRENDAi3.1.1.86. 488.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000001785218 – 250Rhamnogalacturonan acetylesteraseAdd BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi105 ↔ 1131 Publication
Glycosylationi121N-linked (GlcNAc...)3 Publications1
Glycosylationi199N-linked (GlcNAc...) (high mannose)3 Publications1
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

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 23Combined sources5
Turni26 – 28Combined sources3
Turni30 – 33Combined sources4
Helixi40 – 43Combined sources4
Helixi45 – 47Combined sources3
Beta strandi48 – 54Combined sources7
Helixi62 – 67Combined sources6
Helixi70 – 77Combined sources8
Beta strandi83 – 86Combined sources4
Helixi96 – 98Combined sources3
Beta strandi105 – 110Combined sources6
Beta strandi112 – 117Combined sources6
Beta strandi120 – 126Combined sources7
Helixi127 – 140Combined sources14
Beta strandi144 – 148Combined sources5
Turni155 – 158Combined sources4
Helixi167 – 179Combined sources13
Beta strandi182 – 184Combined sources3
Helixi186 – 197Combined sources12
Helixi199 – 204Combined sources6
Beta strandi207 – 211Combined sources5
Helixi215 – 232Combined sources18
Helixi235 – 239Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00017.

Family & Domainsi

Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK15530.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
PfamiPF13472. Lipase_GDSL_2. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.

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.

Genome annotation databases

KEGGiag:CAA61858.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA61858.

Phylogenomic databases

KOiK15530.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16189.
BRENDAi3.1.1.86. 488.

Miscellaneous databases

EvolutionaryTraceiQ00017.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
PfamiPF13472. Lipase_GDSL_2. 1 hit.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 81 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

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.