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A2Q7E0

- ABFA_ASPNC

UniProt

A2Q7E0 - ABFA_ASPNC

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Protein

Probable alpha-L-arabinofuranosidase A

Gene

abfA

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

Functioni

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).By similarity

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. arabinose metabolic process Source: UniProtKB
  3. hemicellulose catabolic process Source: ASPGD
  4. L-arabinose metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH51. Glycoside Hydrolase Family 51.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-L-arabinofuranosidase A (EC:3.2.1.55)
Short name:
ABF A
Short name:
Arabinosidase A
Gene namesi
Name:abfA
ORF Names:An01g00330
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 2R

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 628603Probable alpha-L-arabinofuranosidase APRO_5000219287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00000030.

Structurei

3D structure databases

ProteinModelPortaliA2Q7E0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 51 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000115340.
KOiK01209.
OrthoDBiEOG725DS5.

Family and domain databases

InterProiIPR010720. Alpha-L-AF_C.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A2Q7E0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAFSALSGV SAVSLLLSLV QNAHGISLKV STQGGNSSSP ILYGFMFEDI
60 70 80 90 100
NHSGDGGIYG QMLQNPGLQG TAPNLTAWAA VGDATIAIDG DSPLTSAIPS
110 120 130 140 150
TIKLNIADDA TGAVGLTNEG YWGIPVDGSE FHSSFWIKGD YSGDITVRLV
160 170 180 190 200
GNYTGTEYGS TTITHTSTAD NFTQASVKFP TTKAPDGNVL YELTVDGSVA
210 220 230 240 250
AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLDDMKGSFL RFPGGNNLEG
260 270 280 290 300
NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP
310 320 330 340 350
VLGVWDGFAL ESGGNTPLTG DALTPYIDDV LNELEYILGD TSTTYGAWRA
360 370 380 390 400
ANGQEEPWNL TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA
410 420 430 440 450
STSEADCLPE SMPEGSWVDY HDYSTPDGLV GQFNYFDNLN RSVPYFIGEY
460 470 480 490 500
SRWEIDWPNM KGSVAEAVFM IGFERNSDVV KMAAYAPLLQ LINSTQWTPD
510 520 530 540 550
LIGYTQSPGD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF GPLYWVASSA
560 570 580 590 600
GDSYYMKLAN YGSETQDLTV SIPGTSTGKL TVLADSDPDA YNSDTQTLVT
610 620
PSESTVQASN GTFTFSLPAW AVAVLAAN
Length:628
Mass (Da):67,948
Last modified:March 6, 2007 - v1
Checksum:iD2961CCBB4195041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM269950 Genomic DNA. Translation: CAK43424.1.
RefSeqiXP_001388482.1. XM_001388445.1.

Genome annotation databases

EnsemblFungiiCADANGAT00000033; CADANGAP00000030; CADANGAG00000033.
GeneIDi4978177.
KEGGiang:ANI_1_42014.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM269950 Genomic DNA. Translation: CAK43424.1 .
RefSeqi XP_001388482.1. XM_001388445.1.

3D structure databases

ProteinModelPortali A2Q7E0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00000030.

Protein family/group databases

CAZyi GH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00000033 ; CADANGAP00000030 ; CADANGAG00000033 .
GeneIDi 4978177.
KEGGi ang:ANI_1_42014.

Phylogenomic databases

HOGENOMi HOG000115340.
KOi K01209.
OrthoDBi EOG725DS5.

Enzyme and pathway databases

UniPathwayi UPA00667 .

Family and domain databases

InterProi IPR010720. Alpha-L-AF_C.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF06964. Alpha-L-AF_C. 1 hit.
[Graphical view ]
SMARTi SM00813. Alpha-L-AF_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 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 nameiABFA_ASPNC
AccessioniPrimary (citable) accession number: A2Q7E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: October 1, 2014
This is version 42 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