A2R511 (ABFB_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable alpha-N-arabinofuranosidase B
Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55

Gene names

Name:	abfB
ORF Names:	An15g02300

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Alpha-N-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 activity	Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Pathway	Glycan metabolism; L-arabinan degradation.
Subcellular location	Secreted By similarity.
Domain	Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD) By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 54 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro arabinan metabolic process Inferred from electronic annotation. Source: InterPro polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	alpha-N-arabinofuranosidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 499	481	Probable alpha-N-arabinofuranosidase B		PRO_5000221024
Regions
	Region	19 – 335	317	Catalytic By similarity
	Region	336 – 499	164	ABD By similarity
Sites
	Active site	221	1	Nucleophile By similarity
	Active site	297	1	Proton donor By similarity
	Binding site	219	1	Substrate By similarity
	Binding site	222	1	Substrate; via amide nitrogen By similarity
	Binding site	223	1	Substrate; via amide nitrogen By similarity
	Binding site	296	1	Substrate; via amide nitrogen By similarity
	Binding site	416	1	Substrate By similarity
	Binding site	418	1	Substrate; via amide nitrogen By similarity
	Binding site	419	1	Substrate; via amide nitrogen By similarity
	Binding site	435	1	Substrate By similarity
	Binding site	463	1	Substrate By similarity
	Binding site	465	1	Substrate; via amide nitrogen By similarity
	Binding site	468	1	Substrate; via amide nitrogen By similarity
	Binding site	488	1	Substrate By similarity
Amino acid modifications
	Glycosylation	83	1	N-linked (GlcNAc...) Potential
	Glycosylation	202	1	N-linked (GlcNAc...) Potential
	Disulfide bond	21 ↔ 31		By similarity
	Disulfide bond	81 ↔ 86		By similarity
	Disulfide bond	176 ↔ 177		Uncommon non-proline cis-peptide bond By similarity
	Disulfide bond	401 ↔ 439		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2R511 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: F1F6C21F601419C9	FASTA	499	52,509
	10 20 30 40 50 60 MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT 70 80 90 100 110 120 TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDVDGYDNL 130 140 150 160 170 180 ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE ATGTATGDEP EGMYAVLDGT HYNDACCFDY 190 200 210 220 230 240 GNAETSSTDT GAGHMEAIYL GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS 250 260 270 280 290 300 YSFVTAAVKG GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 310 320 330 340 350 360 GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV SLRVTTPGYT 370 380 390 400 410 420 TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE 430 440 450 460 470 480 LLLNANDGTK QFHEDATFCP QAPLNGEGTS LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD 490 SKTSFNNDVS FEIETAFAS

References

[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: 17259976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270337 Genomic DNA. Translation: CAK42333.1.
RefSeq	XP_001396769.1. XM_001396732.2.
3D structure databases
ProteinModelPortal	A2R511.
SMR	A2R511. Positions 19-499.
ModBase	Search...
Protein family/group databases
CAZy	CBM42. Carbohydrate-Binding Module Family 42. GH54. Glycoside Hydrolase Family 54.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00011909; CADANGAP00011686; CADANGAG00011909.
GeneID	4987831.
GenomeReviews	Gene locus abfB in contig AM270994_GR.
KEGG	ang:ANI_1_372134.
Phylogenomic databases
GeneTree	EFGT00050000004879.
HOGENOM	HBG327897.
OrthoDB	EOG4N33X5.
Family and domain databases
InterPro	IPR015289. A-L-arabinofuranosidase_B_cat. IPR007934. AbfB. IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. [Graphical view]
Gene3D	G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
KO	K01209.
Pfam	PF05270. AbfB. 1 hit. PF09206. ArabFuran-catal. 1 hit. [Graphical view]
SUPFAM	SSF110221. AbfB. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ABFB_ASPNC

Accession

Primary (citable) accession number: A2R511

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	March 6, 2007
Last modified:	November 16, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program