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O74288 (ABFB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. Feed History...

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

Names and origin

Protein namesRecommended name:
Alpha-N-arabinofuranosidase B
Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55
Gene names
Name:abfB
ORF Names:AN1571
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-N-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. Ref.1 Ref.4

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted Ref.1.

Induction

Expressed in presence of L-arabinol and repressed in presence of glucose and glycerol. Expression is also pH regulated probably through the action of the pacC transcription factor and is higher at acidic pHs. Ref.1

Domain

Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD) By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 54 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.8. Ref.4

Temperature dependence:

Optimum temperature is 65 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 510486Alpha-N-arabinofuranosidase B
PRO_0000394609

Regions

Region25 – 342318Catalytic By similarity
Region343 – 510168ABD By similarity

Sites

Active site2271Nucleophile By similarity
Active site3041Proton donor By similarity
Binding site2251Substrate By similarity
Binding site2281Substrate; via amide nitrogen By similarity
Binding site3031Substrate; via amide nitrogen By similarity
Binding site4271Substrate By similarity
Binding site4291Substrate; via amide nitrogen By similarity
Binding site4301Substrate; via amide nitrogen By similarity
Binding site4461Substrate By similarity
Binding site4751Substrate By similarity
Binding site4771Substrate; via amide nitrogen By similarity
Binding site4801Substrate; via amide nitrogen By similarity
Binding site5001Substrate By similarity

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 37 By similarity
Disulfide bond87 ↔ 92 By similarity
Disulfide bond182 ↔ 183Uncommon non-proline cis-peptide bond By similarity
Disulfide bond412 ↔ 450 By similarity

Sequences

Sequence LengthMass (Da)Tools
O74288 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 54011DA6AD3BFC22

FASTA51052,942
        10         20         30         40         50         60 
MTMSRSSRSS VLALALATGS LVAAGPCDIY SSGGTPCIAA HSTTRALYSS YNGPLYQVQR 

        70         80         90        100        110        120 
ASDGTTTTIT PLSAGGVADA SAQDAFCENT TCLITIIYDQ SGNGNDLTQA PPGGFNGPDV 

       130        140        150        160        170        180 
GGYDNLAGAI GAPVTLNGKK AYGVFVSPGT GYRNNEAIGT ATGDEPEGMY AVLDGTHYND 

       190        200        210        220        230        240 
GCCFDYGNAE TSSLDTGNGH MEAIYYGTNT AWGYGAGNGP WIMADLENGL FSGQSSDYNA 

       250        260        270        280        290        300 
GDPSISYRFV TAILKGGPNL WALRGGNAAS GSLSTYYNGI RPTDASGYNP MSKEGAIILG 

       310        320        330        340        350        360 
IGGDNSVSAQ GTFYEGAMTD GYPDDATENS VQADIVAAKY ATTSLISGPA LTVGDTVSLK 

       370        380        390        400        410        420 
VTTSGYDTRY IAHTGSTINT QVVSSSSSST LKQQASWTVR TGLASTAAAN GCVSFESVDT 

       430        440        450        460        470        480 
PGSYIRHSNF ALLLNANDGT KLFSEDATFC PQDSFNDDGT NSIRSWNYPT RYWRHYENVL 

       490        500        510 
YVASNGGVNT FDAATAFTDD VSWVVADGFA

« Hide

References

« Hide 'large scale' references
[1]"The abfB gene encoding the major alpha-L-arabinofuranosidase of Aspergillus nidulans: nucleotide sequence, regulation and construction of a disrupted strain."
Gielkens M., Gonzalez-Candelas L., Sanchez-Torres P., van de Vondervoort P., de Graaff L., Visser J., Ramon D.
Microbiology 145:735-741(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, FUNCTION.
Strain: ArgB2, biA1 and MetG1.
[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.
[4]"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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13759 Genomic DNA. Translation: CAA74084.1.
AACD01000025 Genomic DNA. Translation: EAA64278.1.
BN001307 Genomic DNA. Translation: CBF85134.1.
RefSeqXP_659175.1. XM_654083.1.

3D structure databases

ProteinModelPortalO74288.
SMRO74288. Positions 25-510.
ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00008202.

Protein family/group databases

CAZyCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPABF54B_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008202; CADANIAP00008202; CADANIAG00008202.
GeneID2875522.
KEGGani:AN1571.2.

Phylogenomic databases

eggNOGNOG83819.
HOGENOMHOG000187007.
OMANGHMEAI.
OrthoDBEOG4N33X5.

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PfamPF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view]
SUPFAMSSF110221. AbfB. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABFB_EMENI
AccessionPrimary (citable) accession number: O74288
Secondary accession number(s): C8VN12, Q5BD09
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents