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Q00017

- RHA1_ASPAC

UniProt

Q00017 - RHA1_ASPAC

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Protein

Rhamnogalacturonan acetylesterase

Gene

rha1

Organism
Aspergillus aculeatus
Status
Reviewed - 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 – 235
Turni26 – 283
Turni30 – 334
Helixi40 – 434
Helixi45 – 473
Beta strandi48 – 547
Helixi62 – 676
Helixi70 – 778
Beta strandi83 – 864
Helixi96 – 983
Beta strandi105 – 1106
Beta strandi112 – 1176
Beta strandi120 – 1267
Helixi127 – 14014
Beta strandi144 – 1485
Turni155 – 1584
Helixi167 – 17913
Beta strandi182 – 1843
Helixi186 – 19712
Helixi199 – 2046
Beta strandi207 – 2115
Helixi215 – 23218
Helixi235 – 2395

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
X89714 Genomic DNA. Translation: CAA61858.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89714 Genomic DNA. Translation: CAA61858.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DEO X-ray 1.55 A 18-250 [» ]
1DEX X-ray 1.90 A 18-250 [» ]
1K7C X-ray 1.12 A 18-250 [» ]
1PP4 X-ray 2.50 A/B 18-250 [» ]
3C1U X-ray 1.33 A 18-250 [» ]
ProteinModelPortali Q00017.
SMRi Q00017. Positions 18-250.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16189.

Miscellaneous databases

EvolutionaryTracei Q00017.

Family and domain databases

Gene3Di 3.40.50.1110. 1 hit.
InterProi IPR001087. Lipase_GDSL.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
Pfami PF00657. Lipase_GDSL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 70 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