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A2R511

- ABFB_ASPNC

UniProt

A2R511 - ABFB_ASPNC

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Protein

Probable alpha-L-arabinofuranosidase B

Gene
abfB, An15g02300
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan By similarity.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei176 – 1772Cis-peptide bond By similarity
Binding sitei219 – 2191Substrate By similarity
Active sitei221 – 2211Nucleophile By similarity
Binding sitei222 – 2221Substrate; via amide nitrogen By similarity
Binding sitei223 – 2231Substrate; via amide nitrogen By similarity
Binding sitei296 – 2961Substrate; via amide nitrogen By similarity
Active sitei297 – 2971Proton donor By similarity
Binding sitei416 – 4161Substrate By similarity
Binding sitei418 – 4181Substrate; via amide nitrogen By similarity
Binding sitei419 – 4191Substrate; via amide nitrogen By similarity
Binding sitei435 – 4351Substrate By similarity
Binding sitei463 – 4631Substrate By similarity
Binding sitei465 – 4651Substrate; via amide nitrogen By similarity
Binding sitei468 – 4681Substrate; via amide nitrogen By similarity
Binding sitei488 – 4881Substrate By similarity

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. arabinan metabolic process Source: ASPGD
  3. arabinose metabolic process Source: UniProtKB
  4. L-arabinose metabolic process Source: InterPro
  5. 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

CAZyiCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-L-arabinofuranosidase B (EC:3.2.1.55)
Short name:
ABF B
Short name:
Arabinosidase B
Gene namesi
Name:abfB
ORF Names:An15g02300
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 3R

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. intracellular Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 499481Probable alpha-L-arabinofuranosidase BPRO_5000221024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 31 By similarity
Disulfide bondi81 ↔ 86 By similarity
Glycosylationi83 – 831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi176 ↔ 177 By similarity
Glycosylationi202 – 2021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi401 ↔ 439 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00011686.

Structurei

3D structure databases

ProteinModelPortaliA2R511.
SMRiA2R511. Positions 19-499.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 335317Catalytic By similarityAdd
BLAST
Regioni336 – 499164ABD By similarityAdd
BLAST

Domaini

Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD) By similarity.

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000187007.
OrthoDBiEOG7DFXNQ.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PfamiPF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view]
SUPFAMiSSF110221. SSF110221. 1 hit.
SSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A2R511-1 [UniParc]FASTAAdd to Basket

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MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY    50
QLQRGSDDTT TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH 100
LTQAPPGGFD GPDVDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE 150
ATGTATGDEP EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL 200
GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YSFVTAAVKG 250
GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 300
GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV 350
SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ 400
CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAPLNGEGTS 450
LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS 499
Length:499
Mass (Da):52,509
Last modified:March 6, 2007 - v1
Checksum:iF1F6C21F601419C9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270337 Genomic DNA. Translation: CAK42333.1.
RefSeqiXP_001396769.1. XM_001396732.2.

Genome annotation databases

EnsemblFungiiCADANGAT00011909; CADANGAP00011686; CADANGAG00011909.
GeneIDi4987831.
KEGGiang:ANI_1_372134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270337 Genomic DNA. Translation: CAK42333.1 .
RefSeqi XP_001396769.1. XM_001396732.2.

3D structure databases

ProteinModelPortali A2R511.
SMRi A2R511. Positions 19-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00011686.

Protein family/group databases

CAZyi CBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00011909 ; CADANGAP00011686 ; CADANGAG00011909 .
GeneIDi 4987831.
KEGGi ang:ANI_1_372134.

Phylogenomic databases

HOGENOMi HOG000187007.
OrthoDBi EOG7DFXNQ.

Enzyme and pathway databases

UniPathwayi UPA00667 .

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view ]
Pfami PF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view ]
SUPFAMi SSF110221. SSF110221. 1 hit.
SSF49899. SSF49899. 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 nameiABFB_ASPNC
AccessioniPrimary (citable) accession number: A2R511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 51 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

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

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