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Protein

Probable alpha-L-arabinofuranosidase axhA

Gene

axhA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 similarity

Catalytic activityi

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

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-arabinose metabolic process Source: InterPro
  2. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-L-arabinofuranosidase axhA (EC:3.2.1.55)
Alternative name(s):
Arabinoxylan arabinofuranohydrolase axhA
Gene namesi
Name:axhA
ORF Names:AO090701000885
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 5

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 328302Probable alpha-L-arabinofuranosidase axhAPRO_0000393534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00010936.

Structurei

3D structure databases

ProteinModelPortaliQ2U7D2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG81570.
HOGENOMiHOG000164911.
OMAiTGCIDQT.
OrthoDBiEOG74J9JT.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q2U7D2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKVTKKVLDQ SLCCTALLAL VGGAAAQCAL PSSYSWTSTG ALAEPKAGWA
60 70 80 90 100
ALKDFTNVVF NGQHIVYGSV ADTSGNYGSM NFGPFSDWSE MASASQNAMN
110 120 130 140 150
QGTVAPTLFY FAPKDVWILA YQWGPTSFSY KTSSDPTDAN GWSAAQPLFS
160 170 180 190 200
GTISDSDTGV IDQTVIGDDT NMYLFFAGDN GKIYRASMPI DNFPGDFGTQ
210 220 230 240 250
SEIILSDTKE NLFEAVQVYT VDGQNKYLMI VEAMGANGRY FRSFTADSLD
260 270 280 290 300
GEWTVQAGTE SQPFAGKANS GATWTNDISH GDLVRNNPDQ TMTVDPCNLQ
310 320
LLYQGRDPNA SGDYNLLPWK PGVLTLQV
Length:328
Mass (Da):35,364
Last modified:January 24, 2006 - v1
Checksum:i45C65D129AAAA8D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007164 Genomic DNA. Translation: BAE62533.1.
RefSeqiXP_001823666.1. XM_001823614.1.

Genome annotation databases

EnsemblFungiiCADAORAT00011162; CADAORAP00010936; CADAORAG00011162.
GeneIDi5995723.
KEGGiaor:AOR_1_1552114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007164 Genomic DNA. Translation: BAE62533.1.
RefSeqiXP_001823666.1. XM_001823614.1.

3D structure databases

ProteinModelPortaliQ2U7D2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00010936.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00011162; CADAORAP00010936; CADAORAG00011162.
GeneIDi5995723.
KEGGiaor:AOR_1_1552114.

Phylogenomic databases

eggNOGiNOG81570.
HOGENOMiHOG000164911.
OMAiTGCIDQT.
OrthoDBiEOG74J9JT.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiAXHA_ASPOR
AccessioniPrimary (citable) accession number: Q2U7D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 24, 2006
Last modified: January 7, 2015
This is version 40 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.