Q5B8T6 (ABND_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable arabinan endo-1,5-alpha-L-arabinosidase D
EC=3.2.1.99

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

Gene names

Name:	abnD
ORF Names:	AN3044

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	383 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 By similarity.
Catalytic activity	Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Pathway	Glycan metabolism; L-arabinan degradation.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor Potential.
Sequence similarities	Belongs to the glycosyl hydrolase 43 family.
Sequence caution	The sequence CBF83510.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA63615.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation Xylan degradation
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference 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	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane 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 – 22	22	Potential
	Chain	23 – 356	334	Probable arabinan endo-1,5-alpha-L-arabinosidase D		PRO_0000394640
	Propeptide	357 – 383	27	Removed in mature form Potential		PRO_0000394641
Amino acid modifications
	Lipidation	356	1	GPI-anchor amidated asparagine Potential
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	163	1	N-linked (GlcNAc...) Potential
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Glycosylation	325	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5B8T6 [UniParc]. Last modified June 15, 2010. Version 2. Checksum: 32573F128157AE8A	FASTA	383	42,055
	10 20 30 40 50 60 MVHITLPGLL LCLCLYLSVA PANPLNAHAR VSDTTAFPLP NEGHVVAHDP SIVRHHEHFY 70 80 90 100 110 120 LFKGGIHIPV FRASNLSGPW ERLGTVLNGP SLVQKQNQRR PWAPMVTQWK NRFYCFYSIS 130 140 150 160 170 180 QNGKRNSAIG VASSDSVEPG GWTDHGPLIN TGHGPGSGVY PFNVSNAIDP AFFADPITGQ 190 200 210 220 230 240 PYLQYGSYWK GIFQVPLAED LLSVENATHP NTDHLVFLPK KKPKPNEGVF MSYRAPYYYA 250 260 270 280 290 300 WFSHGQCCHF KTQGFPKEGN EYSIRVGRST SVHGPFVDRD NKDLLNGGGS VVYGSNHGKV 310 320 330 340 350 360 YAPGGLGVLP GANGEPDVLY YHYHNASIGF AQGDARLGWN YLDYVDGWPV PRAPSNPGNS 370 380 LQPPSSVSLQ IVAFLCLVIL FTL

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]. 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	DQ490482 mRNA. Translation: ABF50858.1. AACD01000051 Genomic DNA. Translation: EAA63615.1. Sequence problems. BN001306 Genomic DNA. Translation: CBF83510.1. Sequence problems.
RefSeq	XP_660648.1. XM_655556.1.
3D structure databases
ProteinModelPortal	Q5B8T6.
ModBase	Search...
Protein-protein interaction databases
STRING	162425.CADANIAP00010035.
Protein family/group databases
CAZy	GH43. Glycoside Hydrolase Family 43.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00010035; CADANIAP00010035; CADANIAG00010035.
GeneID	2873991.
KEGG	ani:AN3044.2.
Phylogenomic databases
eggNOG	COG3507.
HOGENOM	HOG000292006.
OrthoDB	EOG4N605Q.
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

ABND_EMENI

Accession

Primary (citable) accession number: Q5B8T6
Secondary accession number(s): C8VIS9, Q1HFU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	June 15, 2010
Last modified:	April 3, 2013
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program