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Q5AZC8 (ABNB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarabinan 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_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 400384Arabinan endo-1,5-alpha-L-arabinosidase B
PRO_0000394630

Amino acid modifications

Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AZC8 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: CD1896D99945C405

FASTA40043,235
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqXP_663956.1. XM_658864.1.

3D structure databases

ProteinModelPortalQ5AZC8.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH43. Glycoside Hydrolase Family 43.
mycoCLAPABN43B_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00006632; CADANIAP00006632; CADANIAG00006632.
GeneID2871250.
KEGGani:AN6352.2.

Phylogenomic databases

eggNOGCOG3507.
HOGENOMHOG000292006.
KOK06113.
OMAHAYESAD.
OrthoDBEOG761C4Q.

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D2.115.10.20. 2 hits.
InterProIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERPTHR22925. PTHR22925. 1 hit.
PfamPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMSSF75005. SSF75005. 2 hits.
ProtoNetSearch...

Entry information

Entry nameABNB_EMENI
AccessionPrimary (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: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries