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Q5B153

- GANA_EMENI

UniProt

Q5B153 - GANA_EMENI

Protein

Arabinogalactan endo-beta-1,4-galactanase A

Gene

galA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei153 – 1531Proton donorBy similarity
    Active sitei263 – 2631NucleophileBy similarity

    GO - Molecular functioni

    1. arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB
    2. glucosidase activity Source: InterPro

    GO - Biological processi

    1. pectin catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Protein family/group databases

    mycoCLAPiGAN53A_EMENI.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:galA
    ORF Names:AN5727
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome V

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 350333Arabinogalactan endo-beta-1,4-galactanase APRO_0000394951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 256
    Helixi29 – 346
    Helixi49 – 557
    Beta strandi60 – 656
    Helixi76 – 8813
    Beta strandi92 – 976
    Beta strandi100 – 1023
    Helixi120 – 14021
    Beta strandi146 – 1538
    Helixi154 – 1563
    Beta strandi158 – 1603
    Turni161 – 1633
    Helixi168 – 18316
    Beta strandi192 – 1987
    Helixi203 – 21513
    Beta strandi217 – 2193
    Beta strandi226 – 2305
    Beta strandi233 – 2353
    Helixi241 – 25515
    Beta strandi258 – 2636
    Helixi279 – 2813
    Helixi288 – 30518
    Beta strandi309 – 3135
    Helixi318 – 3203
    Turni321 – 3244
    Beta strandi325 – 3295
    Turni335 – 3373
    Helixi342 – 3454
    Helixi346 – 3505

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BF7X-ray2.00A1-350[»]
    ProteinModelPortaliQ5B153.
    SMRiQ5B153. Positions 18-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 53 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3867.
    HOGENOMiHOG000217077.
    KOiK01224.
    OrthoDBiEOG7CG78S.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR011683. Glyco_hydro_53.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07745. Glyco_hydro_53. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5B153-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILSSLLPLS LVTLTSAALT YRGADISSLL IEEDSGVAYK NLNGETQAFE    50
    LILANNGVNS IRQRIWVNPS DGSYNLEYNL ELAKRVQDAG MSVYLDLHLS 100
    DTWADPGDQA TPSGWSTTDI DTLAWQVYNY TLDVCNTFAE NNVAVEIVSI 150
    GNEIRNGLLH PLGSTDHYDN IARLLHSGAW GVKDSSLSTT PKILFHLDNG 200
    WDWDAQKYFY DTVLATGTLL STDFDLIGVS YYPFYNADAT LSSLKTSLTN 250
    LKSNYGKNVL VVETDWPVQC SSPEYAFPSD LSSIPFSADG QETFLGRLAD 300
    TLEDVGGVGI YYWEPGWVDN AGLGSSCEDN LMVDWRDRTV RESISVFGDL 350
    Length:350
    Mass (Da):38,572
    Last modified:June 15, 2010 - v2
    Checksum:i5FF6131E86E5CA3F
    GO

    Sequence cautioni

    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 databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490498 mRNA. Translation: ABF50874.1.
    AACD01000098 Genomic DNA. Translation: EAA62820.1. Sequence problems.
    BN001305 Genomic DNA. Translation: CBF81324.1. Sequence problems.
    RefSeqiXP_663331.1. XM_658239.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00003335; CADANIAP00003335; CADANIAG00003335.
    GeneIDi2872012.
    KEGGiani:AN5727.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490498 mRNA. Translation: ABF50874.1 .
    AACD01000098 Genomic DNA. Translation: EAA62820.1 . Sequence problems.
    BN001305 Genomic DNA. Translation: CBF81324.1 . Sequence problems.
    RefSeqi XP_663331.1. XM_658239.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BF7 X-ray 2.00 A 1-350 [» ]
    ProteinModelPortali Q5B153.
    SMRi Q5B153. Positions 18-350.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    mycoCLAPi GAN53A_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00003335 ; CADANIAP00003335 ; CADANIAG00003335 .
    GeneIDi 2872012.
    KEGGi ani:AN5727.2.

    Phylogenomic databases

    eggNOGi COG3867.
    HOGENOMi HOG000217077.
    KOi K01224.
    OrthoDBi EOG7CG78S.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR011683. Glyco_hydro_53.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF07745. Glyco_hydro_53. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiGANA_EMENI
    AccessioniPrimary (citable) accession number: Q5B153
    Secondary accession number(s): C8VFL3, Q1HFS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 55 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3