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Q4WJ80 (GANA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable arabinogalactan endo-beta-1,4-galactanase A

EC=3.2.1.89
Alternative name(s):
Endo-1,4-beta-galactanase A
Short name=Galactanase A
Gene names
Name:galA
ORF Names:AFUA_1G06910
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin By similarity.

Catalytic activity

The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 53 family.

Sequence caution

The sequence EAL88402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 356335Probable arabinogalactan endo-beta-1,4-galactanase A
PRO_0000394946

Sites

Active site1571Proton donor By similarity
Active site2681Nucleophile By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WJ80 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 810E74AD6F3BB001

FASTA35639,105
        10         20         30         40         50         60 
MLGKTVLLPL LVLLCHSLAS ASLVYRGADI SSLLIEEKAG IEYKNVNGQT QPLENILKAN 

        70         80         90        100        110        120 
GVNSVRQRVW VNPSDGSYNL DYNVKLAKRV KAAGMSVYLD LHFSDTWADP SHQTTPRGWS 

       130        140        150        160        170        180 
TNDIGTLTWQ VYNYTMEVCN TFASNGIDVS IVAIGNEIRN GLLWPLGKPD NYANIANILH 

       190        200        210        220        230        240 
SAAFGVKDST LSPKPKIMIH LDNGWDWSAQ KFFYNRVLSS GANLVKSDFD LIGVSYYPFY 

       250        260        270        280        290        300 
NPSATLSALT TSLKNLRSTY GKDVLVVETD WPVSCPNPAY AFPSDLKDIP FSVAGQTTFV 

       310        320        330        340        350 
QRVANIVAQT PGGIGLYYWE PAWVQNAALG SSCADNLMVD WSTRQARTSL SVFATI 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000007 Genomic DNA. Translation: EAL88402.1. Different initiation.
RefSeqXP_750440.1. XM_745347.1.

3D structure databases

ProteinModelPortalQ4WJ80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00009093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00009093; CADAFUAP00009093; CADAFUAG00009093.
GeneID3507699.
KEGGafm:AFUA_1G06910.

Phylogenomic databases

eggNOGCOG3867.
HOGENOMHOG000217077.
KOK01224.
OrthoDBEOG7CG78S.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR011683. Glyco_hydro_53.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF07745. Glyco_hydro_53. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGANA_ASPFU
AccessionPrimary (citable) accession number: Q4WJ80
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 54 of the entry and version 2 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries