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Protein

Probable arabinan endo-1,5-alpha-L-arabinosidase D

Gene

abnD

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-Experimental evidence at transcript leveli

Functioni

Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).By similarity

Catalytic activityi

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

Pathway: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable arabinan endo-1,5-alpha-L-arabinosidase D (EC:3.2.1.99)
Alternative name(s):
Endo-1,5-alpha-L-arabinanase D
Short name:
ABN D
Gene namesi
Name:abnD
ORF Names:AN3044
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

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 356334Probable arabinan endo-1,5-alpha-L-arabinosidase DPRO_0000394640Add
BLAST
Propeptidei357 – 38327Removed in mature formSequence AnalysisPRO_0000394641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Lipidationi356 – 3561GPI-anchor amidated asparagineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5B8T6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3507.
HOGENOMiHOG000292006.
InParanoidiQ5B8T6.
KOiK06113.
OrthoDBiEOG761C4Q.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5B8T6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHITLPGLL LCLCLYLSVA PANPLNAHAR VSDTTAFPLP NEGHVVAHDP
60 70 80 90 100
SIVRHHEHFY LFKGGIHIPV FRASNLSGPW ERLGTVLNGP SLVQKQNQRR
110 120 130 140 150
PWAPMVTQWK NRFYCFYSIS QNGKRNSAIG VASSDSVEPG GWTDHGPLIN
160 170 180 190 200
TGHGPGSGVY PFNVSNAIDP AFFADPITGQ PYLQYGSYWK GIFQVPLAED
210 220 230 240 250
LLSVENATHP NTDHLVFLPK KKPKPNEGVF MSYRAPYYYA WFSHGQCCHF
260 270 280 290 300
KTQGFPKEGN EYSIRVGRST SVHGPFVDRD NKDLLNGGGS VVYGSNHGKV
310 320 330 340 350
YAPGGLGVLP GANGEPDVLY YHYHNASIGF AQGDARLGWN YLDYVDGWPV
360 370 380
PRAPSNPGNS LQPPSSVSLQ IVAFLCLVIL FTL
Length:383
Mass (Da):42,055
Last modified:June 15, 2010 - v2
Checksum:i32573F128157AE8A
GO

Sequence cautioni

The sequence CBF83510.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA63615.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490482 mRNA. Translation: ABF50858.1.
AACD01000051 Genomic DNA. Translation: EAA63615.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF83510.1. Sequence problems.
RefSeqiXP_660648.1. XM_655556.1.

Genome annotation databases

EnsemblFungiiCADANIAT00010035; CADANIAP00010035; CADANIAG00010035.
GeneIDi2873991.
KEGGiani:AN3044.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490482 mRNA. Translation: ABF50858.1.
AACD01000051 Genomic DNA. Translation: EAA63615.1. Sequence problems.
BN001306 Genomic DNA. Translation: CBF83510.1. Sequence problems.
RefSeqiXP_660648.1. XM_655556.1.

3D structure databases

ProteinModelPortaliQ5B8T6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00010035; CADANIAP00010035; CADANIAG00010035.
GeneIDi2873991.
KEGGiani:AN3044.2.

Phylogenomic databases

eggNOGiCOG3507.
HOGENOMiHOG000292006.
InParanoidiQ5B8T6.
KOiK06113.
OrthoDBiEOG761C4Q.

Enzyme and pathway databases

UniPathwayiUPA00667.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "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 nameiABND_EMENI
AccessioniPrimary (citable) accession number: Q5B8T6
Secondary accession number(s): C8VIS9, Q1HFU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 24, 2015
This is version 55 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.