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Protein

Alpha-L-arabinofuranosidase axhA-2

Gene

axhA-2

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan (By similarity).By similarity1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

pH dependencei

Optimum pH is 5.4.1 Publication

Temperature dependencei

Optimum temperature is 47 degrees Celsius.1 Publication

GO - Molecular functioni

  • alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

  • arabinose metabolic process Source: UniProtKB
  • L-arabinose metabolic process Source: InterPro
  • pectin catabolic process Source: UniProtKB
  • xylan catabolic process Source: UniProtKB-KW

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiGH62 Glycoside Hydrolase Family 62

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-arabinofuranosidase axhA-2 (EC:3.2.1.55)
Alternative name(s):
Arabinoxylan arabinofuranohydrolase axhA-2
Gene namesi
Name:axhA-2
ORF Names:AN7908
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome II
  • UP000005890 Componenti: Unassembled WGS sequence

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 – 22Sequence analysisAdd BLAST22
ChainiPRO_000039353723 – 325Alpha-L-arabinofuranosidase axhA-2Add BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi83N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ5AUX2

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003927

Structurei

Secondary structure

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 34Combined sources3
Beta strandi45 – 56Combined sources12
Beta strandi59 – 71Combined sources13
Beta strandi73 – 78Combined sources6
Beta strandi81 – 83Combined sources3
Helixi84 – 89Combined sources6
Beta strandi92 – 94Combined sources3
Beta strandi100 – 107Combined sources8
Helixi108 – 110Combined sources3
Beta strandi112 – 130Combined sources19
Beta strandi142 – 145Combined sources4
Beta strandi156 – 163Combined sources8
Beta strandi165 – 173Combined sources9
Beta strandi175 – 185Combined sources11
Helixi186 – 188Combined sources3
Beta strandi198 – 202Combined sources5
Turni205 – 207Combined sources3
Beta strandi210 – 217Combined sources8
Beta strandi225 – 232Combined sources8
Beta strandi234 – 246Combined sources13
Beta strandi252 – 264Combined sources13
Turni265 – 267Combined sources3
Beta strandi277 – 281Combined sources5
Helixi294 – 296Combined sources3
Beta strandi298 – 303Combined sources6
Beta strandi318 – 324Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5UBJX-ray1.70A1-325[»]
ProteinModelPortaliQ5AUX2
SMRiQ5AUX2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000164911
InParanoidiQ5AUX2
OMAiQWTRNDQ
OrthoDBiEOG092C438U

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR005193 GH62_arabinosidase
IPR023296 Glyco_hydro_beta-prop_sf
PANTHERiPTHR40631 PTHR40631, 1 hit
PfamiView protein in Pfam
PF03664 Glyco_hydro_62, 1 hit
SUPFAMiSSF75005 SSF75005, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q5AUX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNLSTWPTF AALLWSAPRV LAQCGLPSTY SWTSTGPLAE PKDGWASLKD
60 70 80 90 100
FTAVPYNGQY LVYATYHDTG TSWGSMNFGL FSNWSDMATA SQNAMTQSTV
110 120 130 140 150
APTLFYFEPK DVWILAYQWG PTAFSYLTSS DPTDANGWSS PQPLFSGSIS
160 170 180 190 200
DSDTGVIDQT VIGDSTTMYL FFAGDNGRIY RASMPIDQFP GDFGTESEII
210 220 230 240 250
LSDERNNLFE AVQVYTVSGQ SKDTYLMIVE AIGAQGRYFR SFTADSLGGS
260 270 280 290 300
WTPQAATESA PFAGKANSGA TWTDDISHGD LVRSTPDQTM SIDPCNLQLL
310 320
YQGRDPSLNP GYDLLPYRPG LLTLK
Length:325
Mass (Da):35,560
Last modified:April 26, 2005 - v1
Checksum:iCD0DC28566CB8064
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000135 Genomic DNA Translation: EAA59562.1
BN001302 Genomic DNA Translation: CBF73503.1
RefSeqiXP_681177.1, XM_676085.1

Genome annotation databases

EnsemblFungiiCADANIAT00003927; CADANIAP00003927; CADANIAG00003927
EAA59562; EAA59562; AN7908.2
GeneIDi2869048
KEGGiani:AN7908.2

Similar proteinsi

Entry informationi

Entry nameiAXHA2_EMENI
AccessioniPrimary (citable) accession number: Q5AUX2
Secondary accession number(s): C8V4U9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: May 23, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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

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