Q5AZC8 (ABNB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arabinan endo-1,5-alpha-L-arabinosidase B
EC=3.2.1.99

Alternative name(s):
Endo-1,5-alpha-L-arabinanase B
Short name=ABN B

Gene names

Name:	abnB
ORF Names:	AN6352

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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. Ref.1
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 Reference proteome
Gene Ontology (GO)
Biological_process	arabinan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway pectin catabolic process Inferred from direct assay Ref.1. Source: UniProtKB 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 direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 400	384	Arabinan endo-1,5-alpha-L-arabinosidase B		PRO_0000394630
Amino acid modifications
	Glycosylation	24	1	N-linked (GlcNAc...) Potential
	Glycosylation	184	1	N-linked (GlcNAc...) Potential
	Glycosylation	372	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5AZC8 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: CD1896D99945C405	FASTA	400	43,235
	10 20 30 40 50 60 MAVIFVLFFL VSMALSARIR PSFNGTALSG TSNKHPFEPG PNTIFREEVP PSAAASGFPS 70 80 90 100 110 120 AHGTELRTHD PSIIKVGSIY YSYSVGPSIT IHQAFSLDGP WTEVGALLSG ESVIKKGDRK 130 140 150 160 170 180 APWAANTIYI NGRYYCYYSV SNSGCRDSAI GVASSAFPGP GEWTDHGLII QSGTGEGSDV 190 200 210 220 230 240 FPLNQSNTID PNVFVDGDGT AYLNFGSFWT GLWQVPLEEE LVTVKGLQDG TLDAVHLAAE 250 260 270 280 290 300 PGKVWRSKLA NSKAKTVSTS KTGSPICGDP TGGHPIEGGF MAYHAPYYYM WFSWGRCCEF 310 320 330 340 350 360 KDPAMRSNGK EYRIRVGRST SARGPFVDKQ GIDLVDGGGE TVYGSNGDVF APGGQGILTD 370 380 390 400 EFGDILYYHY LNSSVSYDFA DARLGYNRLE YVDGWPVAVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ490500 mRNA. Translation: ABF50876.1. AACD01000107 Genomic DNA. Translation: EAA58736.1. BN001301 Genomic DNA. Translation: CBF69642.1.
RefSeq	XP_663956.1. XM_658864.1.
3D structure databases
ProteinModelPortal	Q5AZC8.
ModBase	Search...
Protein family/group databases
CAZy	GH43. Glycoside Hydrolase Family 43.
mycoCLAP	ABN43B_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00006632; CADANIAP00006632; CADANIAG00006632.
GeneID	2871250.
KEGG	ani:AN6352.2.
Phylogenomic databases
eggNOG	COG3507.
HOGENOM	HOG000292006.
OMA	CRDSAIG.
OrthoDB	EOG4N605Q.
Enzyme and pathway databases
UniPathway	UPA00667.
Family and domain databases
Gene3D	2.115.10.20. 2 hits.
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

ABNB_EMENI

Accession

Primary (citable) accession number: Q5AZC8
Secondary accession number(s): C8V0Y7, Q1HFS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 26, 2005
Last modified:	March 6, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program