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Protein

Xyloglucan-specific endo-beta-1,4-glucanase A

Gene

xgeA

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Specific for xyloglucan and does not hydrolyze other cell wall components.2 Publications

Catalytic activityi

Xyloglucan + H2O = xyloglucan oligosaccharides.

pH dependencei

Optimum pH is 3.4. Stability declines sharply below pH 2.8 and above pH 5.0.1 Publication

Temperature dependencei

Optimum temperature is below 30 degrees Celsius. Is very stable below 35 degrees Celsius, but at 50 degrees Celsius, it loses 80 percent of its activity within 2 h.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16602.
BRENDAi3.2.1.151. 488.

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiXEG12A_ASPAC.

Names & Taxonomyi

Protein namesi
Recommended name:
Xyloglucan-specific endo-beta-1,4-glucanase A (EC:3.2.1.151)
Alternative name(s):
Xyloglucanase A
Xyloglucanendohydrolase A
Gene namesi
Name:xgeA
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence analysisAdd
BLAST
Chaini15 – 238224Xyloglucan-specific endo-beta-1,4-glucanase APRO_5000054062Add
BLAST

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Beta strandi29 – 324Combined sources
Beta strandi35 – 384Combined sources
Helixi44 – 463Combined sources
Beta strandi47 – 5913Combined sources
Beta strandi62 – 7312Combined sources
Beta strandi75 – 773Combined sources
Beta strandi82 – 865Combined sources
Helixi93 – 953Combined sources
Beta strandi100 – 12526Combined sources
Beta strandi130 – 14112Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi162 – 17110Combined sources
Beta strandi174 – 18310Combined sources
Beta strandi186 – 1916Combined sources
Helixi193 – 20210Combined sources
Beta strandi209 – 23527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VL8X-ray1.90A15-238[»]
3VL9X-ray1.20A/B15-238[»]
3VLBX-ray2.70B/D21-238[»]
ProteinModelPortaliO94218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK18576.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O94218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLLSLAT LASAASLQRR SDFCGQWDTA TAGDFTLYND LWGESAGTGS
60 70 80 90 100
QCTGVDSYSG DTIAWHTSWS WSGGSSSVKS YVNAALTFTP TQLNCISSIP
110 120 130 140 150
TTWKWSYSGS SIVADVAYDT FLAETASGSS KYEIMVWLAA LGGAGPISST
160 170 180 190 200
GSTIATPTIA GVNWKLYSGP NGDTTVYSFV ADSTTESFSG DLNDFFTYLV
210 220 230
DNEGVSDELY LTTLEAGTEP FTGSNAKLTV SEYSISIE
Length:238
Mass (Da):25,159
Last modified:May 1, 1999 - v1
Checksum:iFCCA6746D9AEC1B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043595 mRNA. Translation: AAD02275.1.
AY160774 mRNA. Translation: AAO20340.1.

Genome annotation databases

KEGGiag:AAD02275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043595 mRNA. Translation: AAD02275.1.
AY160774 mRNA. Translation: AAO20340.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VL8X-ray1.90A15-238[»]
3VL9X-ray1.20A/B15-238[»]
3VLBX-ray2.70B/D21-238[»]
ProteinModelPortaliO94218.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.
mycoCLAPiXEG12A_ASPAC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAD02275.

Phylogenomic databases

KOiK18576.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16602.
BRENDAi3.2.1.151. 488.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
[Graphical view]
PfamiPF01670. Glyco_hydro_12. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme."
    Pauly M., Andersen L.N., Kauppinen S., Kofod L.V., York W.S., Albersheim P., Darvill A.
    Glycobiology 9:93-100(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: KSM 510.
  2. "Enhancement of growth and cellulose accumulation by overexpression of xyloglucanase in poplar."
    Park Y.W., Baba K., Furuta Y., Iida I., Sameshima K., Arai M., Hayashi T.
    FEBS Lett. 564:183-187(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-238, FUNCTION.

Entry informationi

Entry nameiXGEA_ASPAC
AccessioniPrimary (citable) accession number: O94218
Secondary accession number(s): Q6YBY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 1, 1999
Last modified: April 13, 2016
This is version 72 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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.