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P83691

- GANA_HUMIN

UniProt

P83691 - GANA_HUMIN

Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene
N/A
Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351Proton donorBy similarity
    Active sitei245 – 2451NucleophileBy similarity

    GO - Molecular functioni

    1. arabinogalactan endo-1,4-beta-galactosidase activity Source: UniProtKB-EC
    2. glucosidase activity Source: InterPro
    3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: UniProtKB
    4. polysaccharide binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell wall macromolecule catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH53. Glycoside Hydrolase Family 53.
    mycoCLAPiGAN53A_HUMIN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arabinogalactan endo-beta-1,4-galactanase (EC:3.2.1.89)
    Alternative name(s):
    Endo-1,4-beta-galactanase
    Short name:
    Galactanase
    OrganismiHumicola insolens (Soft-rot fungus)
    Taxonomic identifieri34413 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    Subcellular locationi

    GO - Cellular componenti

    1. extraorganismal space Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Arabinogalactan endo-beta-1,4-galactanasePRO_0000057705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi12 – 176
    Helixi32 – 387
    Beta strandi43 – 486
    Helixi59 – 7113
    Beta strandi75 – 806
    Beta strandi83 – 853
    Helixi102 – 12322
    Beta strandi129 – 1357
    Beta strandi139 – 1424
    Turni143 – 1453
    Helixi150 – 16516
    Beta strandi174 – 1807
    Helixi185 – 19814
    Beta strandi199 – 2013
    Helixi203 – 2053
    Beta strandi208 – 2125
    Helixi223 – 23715
    Beta strandi240 – 2456
    Helixi261 – 2633
    Helixi270 – 28617
    Beta strandi290 – 2967
    Helixi301 – 3033
    Turni304 – 3074
    Beta strandi308 – 3125
    Beta strandi320 – 3223
    Helixi324 – 3274
    Helixi328 – 3314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HJQX-ray2.55A1-332[»]
    ProteinModelPortaliP83691.
    SMRiP83691. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP83691.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 53 family.1 Publication

    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.

    P83691-1 [UniParc]FASTAAdd to Basket

    « Hide

    ALQYKGVDWS SVMVEERAGV RYKNVNGQEK PLEYILAENG VNMVRQRVWV    50
    NPWDGNYNLD YNIQLARRAK AAGLGLYINF HYSDTWADPA HQTTPAGWPS 100
    DINNLAWKLY NYTLDSMNRF ADAGIQVDIV SIGNEITQGL LWPLGKTNNW 150
    YNIARLLHSA AWGVKDSRLN PKPKIMVHLD NGWNWDTQNW WYTNVLSQGP 200
    FEMSDFDMMG VSFYPFYSAS ATLDSLRRSL NNMVSRWGKE VAVVETNWPT 250
    SCPYPRYQFP ADVRNVPFSA AGQTQYIQSV ANVVSSVSKG VGLFYWEPAW 300
    IHNANLGSSC ADNTMFTPSG QALSSLSVFH RI 332
    Length:332
    Mass (Da):37,659
    Last modified:December 15, 2003 - v1
    Checksum:iF6DA01D0F24CA702
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HJQ X-ray 2.55 A 1-332 [» ]
    ProteinModelPortali P83691.
    SMRi P83691. Positions 1-332.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH53. Glycoside Hydrolase Family 53.
    mycoCLAPi GAN53A_HUMIN.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P83691.

    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. "Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum."
      Le Nours J., Ryttersgaard C., Lo Leggio L., Oestergaard P.R., Borchert T.V., Christensen L.L.H., Larsen S.
      Protein Sci. 12:1195-1204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-111.

    Entry informationi

    Entry nameiGANA_HUMIN
    AccessioniPrimary (citable) accession number: P83691
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has a pH range of 6.5-9.5 with optimum of 8.5; and a temperature optimum of 65 degrees Celsius at pH 6.5.1 Publication

    Keywords - Technical termi

    3D-structure

    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