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Protein

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

Gene

xgeA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: -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 (Probable).1 Publication

Catalytic activityi

Xyloglucan + H2O = xyloglucan oligosaccharides.

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is between 50 and 60 degrees Celsius.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16908
BRENDAi3.2.1.151 518

Protein family/group databases

CAZyiGH12 Glycoside Hydrolase Family 12
mycoCLAPiXEG12A_ASPNG

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
Synonyms:XEG12A
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_500021405017 – 241Xyloglucan-specific endo-beta-1,4-glucanase AAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi47N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA1XP58
SMRiA1XP58
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IWF9 Eukaryota
ENOG4111FV6 LUCA

Family and domain databases

Gene3Di2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR002594 GH12
PANTHERiPTHR34002 PTHR34002, 1 hit
PfamiView protein in Pfam
PF01670 Glyco_hydro_12, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit

Sequencei

Sequence statusi: Complete.

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

A1XP58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLALSALL SLASAASISR RSDFCGQWDT ATAGDFILYN DLWGEDNASS
60 70 80 90 100
GSQCTGVDSA SGSEIAWHTS WSWEGGSSDV KSYANAALQF TGTQLSSISS
110 120 130 140 150
IPSTWKWTYS GSDIVADVAY DMFLGSTADA SSDEYEIMVW LAALGGAGPI
160 170 180 190 200
SSTGSTIATP TINGVTWDLY TGPNGDTTVY SFVAQSTTED FSGDLNDFFT
210 220 230 240
YLVDNEGVSD SLYLTTLEAG TEPFTGSDAE LKVSEYSVSI E
Length:241
Mass (Da):25,456
Last modified:February 6, 2007 - v1
Checksum:iFE4E5CD2B9CB46A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ486529 mRNA Translation: ABF46829.1

Similar proteinsi

Entry informationi

Entry nameiXGEA_ASPNG
AccessioniPrimary (citable) accession number: A1XP58
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: February 6, 2007
Last modified: January 31, 2018
This is version 47 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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