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Protein

Probable alpha-L-arabinofuranosidase axhA-1

Gene

axhA-1

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

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-1 (EC:3.2.1.55)
Alternative name(s):
Arabinoxylan arabinofuranohydrolase axhA-1
Gene namesi
Name:axhA-1
ORF Names:AN2632
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VI

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 327301Probable alpha-L-arabinofuranosidase axhA-1PRO_0000393536Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00010488.

Structurei

3D structure databases

ProteinModelPortaliQ5B9Z8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG81570.
HOGENOMiHOG000164911.
InParanoidiQ5B9Z8.
OrthoDBiEOG74J9JT.

Family and domain databases

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.

Q5B9Z8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFPVTKLTH VIAGVGLLLA GREVAAQCAL PSSYSWSSTN ALASPKSGWA
60 70 80 90 100
AIKDFTSVIY NGQHLVYASF ADTSGNYGSM NFSPFSDWSD MASASQNAMS
110 120 130 140 150
QAAVAPTLFY FAPKDIWILA YQWGPTSFSY KTSSDPTNPN GWSTPQPLFS
160 170 180 190 200
GTISDSATGC IDQTLIGDSS NMYLFFAGDN GKIYRASMPI DNFPGDFGTE
210 220 230 240 250
SEIIMSDTSN NLFEAVQVYT VDGQNQYLMI VEAIGANGRY FRSFTADSLD
260 270 280 290 300
GAWTAQAATE SQPFAGKANS GASWTNDISH GDLVRSNPDQ TMTIDPCNLQ
310 320
LLYQGRDPNA SGDYNLLPWV PGVLTLQ
Length:327
Mass (Da):35,180
Last modified:April 20, 2010 - v2
Checksum:i8FE0B1FCC3112F7B
GO

Sequence cautioni

The sequence CBF84318.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA62979.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000045 Genomic DNA. Translation: EAA62979.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF84318.1. Sequence problems.
RefSeqiXP_660236.1. XM_655144.1.

Genome annotation databases

EnsemblFungiiCADANIAT00010488; CADANIAP00010488; CADANIAG00010488.
GeneIDi2874537.
KEGGiani:AN2632.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000045 Genomic DNA. Translation: EAA62979.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF84318.1. Sequence problems.
RefSeqiXP_660236.1. XM_655144.1.

3D structure databases

ProteinModelPortaliQ5B9Z8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00010488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00010488; CADANIAP00010488; CADANIAG00010488.
GeneIDi2874537.
KEGGiani:AN2632.2.

Phylogenomic databases

eggNOGiNOG81570.
HOGENOMiHOG000164911.
InParanoidiQ5B9Z8.
OrthoDBiEOG74J9JT.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiAXHA1_EMENI
AccessioniPrimary (citable) accession number: Q5B9Z8
Secondary accession number(s): C8VHH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: January 7, 2015
This is version 47 of the entry and version 2 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.