A2QT85 (ABNA_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	abnA
ORF Names:	An09g01190

Organism

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

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	321 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	Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan By similarity.
Catalytic activity	Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Pathway	Glycan metabolism; L-arabinan degradation.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 43 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	arabinan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	arabinan endo-1,5-alpha-L-arabinosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 321	302	Probable arabinan endo-1,5-alpha-L-arabinosidase A		PRO_5000220397
Amino acid modifications
	Glycosylation	295	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	A2QT85 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 8D176BE3D62B15F0	FASTA	321	34,483
	10 20 30 40 50 60 MYRLLSVASV PLLASLVHGY ADPGACSGVC TTHDPGLIRR ESDGTYFLFS TGNKISYVSA 70 80 90 100 110 120 SSIEGPWTSV GSMLPDGSSI DLDGNDDLWA PDVSYVDGLY YVYYAVSTFG SQDSAIGLAT 130 140 150 160 170 180 SETMEYGSWT DHGSTGIASS SAKIYNAIDP NLIYADGTYY INFGSFWDDI YQVPMKSTPT 190 200 210 220 230 240 AAASSSYNLA YDPSGTHAEE GSYMFQYGDY YYLFYSAGIC CGYDTSMPAS GEEYHIKVCR 250 260 270 280 290 300 STSPTGDFVD SDGTACTDGG GTMVLESHGE VYGPGGQGVY DDPNLGPVLY YHYMNTTIGY 310 320 ADSDAQFGWN TIDFSSGWPV V

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270193 Genomic DNA. Translation: CAK49041.1.
RefSeq	XP_001393437.1. XM_001393400.2.
3D structure databases
ProteinModelPortal	A2QT85.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00007516.
Protein family/group databases
CAZy	GH43. Glycoside Hydrolase Family 43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00007653; CADANGAP00007516; CADANGAG00007653.
GeneID	4983650.
KEGG	ang:ANI_1_118084.
Phylogenomic databases
HOGENOM	HOG000292006.
KO	K06113.
OrthoDB	EOG43JGDJ.
Enzyme and pathway databases
UniPathway	UPA00667.
Family and domain databases
Gene3D	2.115.10.20. 1 hit.
InterPro	IPR006710. Glyco_hydro_43. IPR016840. Glyco_hydro_43_endo_a_Ara-ase. IPR023296. Glyco_hydro_beta-prop. [Graphical view]
PANTHER	PTHR22925. PTHR22925. 1 hit.
Pfam	PF04616. Glyco_hydro_43. 1 hit. [Graphical view]
PIRSF	PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAM	SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ABNA_ASPNC

Accession

Primary (citable) accession number: A2QT85

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program