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Q5B153 (GANA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:
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:AN5727
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 length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endogalactanase involved in the degradation of plant cell wall polysaccharides, and more particularly of hairy regions of pectin. Ref.1

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Ref.1

Sequence caution

The sequence CBF81324.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA62820.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 350333Arabinogalactan endo-beta-1,4-galactanase A
PRO_0000394951

Sites

Active site1531Proton donor By similarity
Active site2631Nucleophile By similarity

Amino acid modifications

Glycosylation1291N-linked (GlcNAc...) Potential

Secondary structure

..................................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5B153 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 5FF6131E86E5CA3F

FASTA35038,572
        10         20         30         40         50         60 
MILSSLLPLS LVTLTSAALT YRGADISSLL IEEDSGVAYK NLNGETQAFE LILANNGVNS 

        70         80         90        100        110        120 
IRQRIWVNPS DGSYNLEYNL ELAKRVQDAG MSVYLDLHLS DTWADPGDQA TPSGWSTTDI 

       130        140        150        160        170        180 
DTLAWQVYNY TLDVCNTFAE NNVAVEIVSI GNEIRNGLLH PLGSTDHYDN IARLLHSGAW 

       190        200        210        220        230        240 
GVKDSSLSTT PKILFHLDNG WDWDAQKYFY DTVLATGTLL STDFDLIGVS YYPFYNADAT 

       250        260        270        280        290        300 
LSSLKTSLTN LKSNYGKNVL VVETDWPVQC SSPEYAFPSD LSSIPFSADG QETFLGRLAD 

       310        320        330        340        350 
TLEDVGGVGI YYWEPGWVDN AGLGSSCEDN LMVDWRDRTV RESISVFGDL 

« 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, BIOPHYSICOCHEMICAL PROPERTIES.
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490498 mRNA. Translation: ABF50874.1.
AACD01000098 Genomic DNA. Translation: EAA62820.1. Sequence problems.
BN001305 Genomic DNA. Translation: CBF81324.1. Sequence problems.
RefSeqXP_663331.1. XM_658239.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BF7X-ray2.00A1-350[»]
ProteinModelPortalQ5B153.
SMRQ5B153. Positions 18-350.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

mycoCLAPGAN53A_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00003335; CADANIAP00003335; CADANIAG00003335.
GeneID2872012.
KEGGani:AN5727.2.

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_EMENI
AccessionPrimary (citable) accession number: Q5B153
Secondary accession number(s): C8VFL3, Q1HFS6
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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries