Q2U8C6 (ABNA_ASPOR) 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:	AO090701000481

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	319 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 – 319	300	Probable arabinan endo-1,5-alpha-L-arabinosidase A		PRO_0000394621
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2U8C6 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 5861C4ECF5978DF4	FASTA	319	34,094
	10 20 30 40 50 60 MYLQSSLALV LLRAAVVHGY ANPGACSGAC NIHDPSLIQN GDGTYYRFST GNNISFASAS 70 80 90 100 110 120 SIEGPWTALG SVLPGGSSID NSGRYDPWAP DVQKVGDLYY LYYAVSSFGT QESAIGLATS 130 140 150 160 170 180 ETMEEGTWTD KGSIVTSTTG DQYNAIDANL LVDGSANYLT FGSFWQDIFQ VTLNGDATSS 190 200 210 220 230 240 TSTPVNVAFD PATTHPVEGA YLYKYGDYYY LFYSWGTCCG YDTSRPAEGE EYKIKVCRSS 250 260 270 280 290 300 TPTGNFVDAS GVACTDGGGT VVLESHDNVY GPGGQGVYTD PNLGPVLYYH YVDTTIGYAD 310 SQKLFGWNAI DFSSGWPSV

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007164 Genomic DNA. Translation: BAE62189.1.
RefSeq	XP_001823322.1. XM_001823270.1.
3D structure databases
ProteinModelPortal	Q2U8C6.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00010592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00010811; CADAORAP00010592; CADAORAG00010811.
GeneID	5995379.
KEGG	aor:AOR_1_882114.
Phylogenomic databases
eggNOG	COG3507.
HOGENOM	HOG000292006.
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_ASPOR

Accession

Primary (citable) accession number: Q2U8C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program