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A2R511

- ABFB_ASPNC

UniProt

A2R511 - ABFB_ASPNC

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Protein

Probable alpha-L-arabinofuranosidase B

Gene

abfB

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).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 bondBy similarity
Binding sitei219 – 2191SubstrateBy similarity
Active sitei221 – 2211NucleophileBy similarity
Binding sitei222 – 2221Substrate; via amide nitrogenBy similarity
Binding sitei223 – 2231Substrate; via amide nitrogenBy similarity
Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
Active sitei297 – 2971Proton donorBy similarity
Binding sitei416 – 4161SubstrateBy similarity
Binding sitei418 – 4181Substrate; via amide nitrogenBy similarity
Binding sitei419 – 4191Substrate; via amide nitrogenBy similarity
Binding sitei435 – 4351SubstrateBy similarity
Binding sitei463 – 4631SubstrateBy similarity
Binding sitei465 – 4651Substrate; via amide nitrogenBy similarity
Binding sitei468 – 4681Substrate; via amide nitrogenBy similarity
Binding sitei488 – 4881SubstrateBy 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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 499481Probable alpha-L-arabinofuranosidase BPRO_5000221024Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00011686.

Structurei

3D structure databases

ProteinModelPortaliA2R511.
SMRiA2R511. Positions 19-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 335317CatalyticBy similarityAdd
BLAST
Regioni336 – 499164ABDBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 54 family.Curated

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.
IPR013320. ConA-like_dom.
[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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        10         20         30         40         50
MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY
60 70 80 90 100
QLQRGSDDTT TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH
110 120 130 140 150
LTQAPPGGFD GPDVDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE
160 170 180 190 200
ATGTATGDEP EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL
210 220 230 240 250
GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YSFVTAAVKG
260 270 280 290 300
GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN
310 320 330 340 350
GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV
360 370 380 390 400
SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ
410 420 430 440 450
CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAPLNGEGTS
460 470 480 490
LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS
Length:499
Mass (Da):52,509
Last modified:March 6, 2007 - v1
Checksum:iF1F6C21F601419C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
IPR013320. ConA-like_dom.
[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: October 29, 2014
This is version 53 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