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A2QT85

- ABNA_ASPNC

UniProt

A2QT85 - ABNA_ASPNC

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Protein

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

Gene

abnA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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.

Pathwayi

GO - Molecular functioni

  1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: ASPGD

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. hemicellulose catabolic process Source: ASPGD
  3. xylan catabolic process Source: UniProtKB-KW
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 A (EC:3.2.1.99)
Alternative name(s):
Endo-1,5-alpha-L-arabinanase A
Short name:
ABN A
Gene namesi
Name:abnA
ORF Names:An09g01190
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 1L

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 321302Probable arabinan endo-1,5-alpha-L-arabinosidase APRO_5000220397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00007516.

Structurei

3D structure databases

ProteinModelPortaliA2QT85.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000292006.
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.

A2QT85-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MYRLLSVASV PLLASLVHGY ADPGACSGVC TTHDPGLIRR ESDGTYFLFS
60 70 80 90 100
TGNKISYVSA SSIEGPWTSV GSMLPDGSSI DLDGNDDLWA PDVSYVDGLY
110 120 130 140 150
YVYYAVSTFG SQDSAIGLAT SETMEYGSWT DHGSTGIASS SAKIYNAIDP
160 170 180 190 200
NLIYADGTYY INFGSFWDDI YQVPMKSTPT AAASSSYNLA YDPSGTHAEE
210 220 230 240 250
GSYMFQYGDY YYLFYSAGIC CGYDTSMPAS GEEYHIKVCR STSPTGDFVD
260 270 280 290 300
SDGTACTDGG GTMVLESHGE VYGPGGQGVY DDPNLGPVLY YHYMNTTIGY
310 320
ADSDAQFGWN TIDFSSGWPV V
Length:321
Mass (Da):34,483
Last modified:March 6, 2007 - v1
Checksum:i8D176BE3D62B15F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270193 Genomic DNA. Translation: CAK49041.1.
RefSeqiXP_001393437.1. XM_001393400.2.

Genome annotation databases

EnsemblFungiiCADANGAT00007653; CADANGAP00007516; CADANGAG00007653.
GeneIDi4983650.
KEGGiang:ANI_1_118084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270193 Genomic DNA. Translation: CAK49041.1 .
RefSeqi XP_001393437.1. XM_001393400.2.

3D structure databases

ProteinModelPortali A2QT85.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00007516.

Protein family/group databases

CAZyi GH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00007653 ; CADANGAP00007516 ; CADANGAG00007653 .
GeneIDi 4983650.
KEGGi ang:ANI_1_118084.

Phylogenomic databases

HOGENOMi HOG000292006.
KOi K06113.
OrthoDBi EOG761C4Q.

Enzyme and pathway databases

UniPathwayi UPA00667 .

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
InterProi IPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view ]
PANTHERi PTHR22925. PTHR22925. 1 hit.
Pfami PF04616. Glyco_hydro_43. 1 hit.
[Graphical view ]
PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMi SSF75005. SSF75005. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiABNA_ASPNC
AccessioniPrimary (citable) accession number: A2QT85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: October 1, 2014
This is version 45 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3