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P48842

- GANA_ASPAC

UniProt

P48842 - GANA_ASPAC

Protein

Arabinogalactan endo-beta-1,4-galactanase

Gene

gal1

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 4.0-4.5.

    Temperature dependencei

    Optimum temperature is 40-65 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei152 – 1521Proton donorBy similarity
    Active sitei262 – 2621NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH53. Glycoside Hydrolase Family 53.
    mycoCLAPiGAN53A_ASPAC.

    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
    Gene namesi
    Name:gal1
    OrganismiAspergillus aculeatus
    Taxonomic identifieri5053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981D → N: Broadens pH profile by 1 unit towards the basic end of the scale. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Chaini17 – 350334Arabinogalactan endo-beta-1,4-galactanasePRO_0000012221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 246
    Helixi28 – 336
    Helixi48 – 558
    Beta strandi59 – 646
    Helixi75 – 8713
    Beta strandi91 – 966
    Beta strandi99 – 1013
    Helixi119 – 13921
    Beta strandi145 – 1528
    Helixi153 – 1553
    Beta strandi157 – 1593
    Turni160 – 1623
    Helixi167 – 18216
    Beta strandi191 – 1977
    Helixi202 – 21413
    Beta strandi216 – 2183
    Helixi220 – 2223
    Beta strandi225 – 2295
    Beta strandi232 – 2343
    Helixi240 – 25415
    Beta strandi258 – 2625
    Helixi278 – 2803
    Helixi287 – 30216
    Beta strandi307 – 3137
    Turni321 – 3244
    Beta strandi325 – 3295
    Turni335 – 3373
    Helixi343 – 3486

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FHLX-ray2.30A17-350[»]
    1FOBX-ray1.80A17-350[»]
    ProteinModelPortaliP48842.
    SMRiP48842. Positions 17-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48842.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 53 family.Curated

    Keywords - Domaini

    Signal

    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.

    P48842-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFASLLLAAL PLLTHAALTY RGADISSLLL LEDEGYSYKN LNGQTQALET    50
    ILADAGINSI RQRVWVNPSD GSYDLDYNLE LAKRVKAAGM SLYLDLHLSD 100
    TWADPSDQTT PSGWSTTDLG TLKWQLYNYT LEVCNTFAEN DIDIEIISIG 150
    NEIRAGLLWP LGETSSYSNI GALLHSGAWG VKDSNLATTP KIMIHLDDGW 200
    SWDQQNYFYE TVLATGELLS TDFDYFGVSY YPFYSASATL ASLKTSLANL 250
    QSTYDKPVVV VETNWPVSCP NPAYAFPSDL SSIPFSVAGQ QEFLEKLAAV 300
    VEATTDGLGV YYWEPAWIGN AGLGSSCADN LMVDYTTDEV YESIETLGEL 350
    Length:350
    Mass (Da):38,423
    Last modified:February 1, 1996 - v1
    Checksum:i9074249DFAB24CAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34599 mRNA. Translation: AAA32692.1.
    PIRiS51494.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34599 mRNA. Translation: AAA32692.1 .
    PIRi S51494.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHL X-ray 2.30 A 17-350 [» ]
    1FOB X-ray 1.80 A 17-350 [» ]
    ProteinModelPortali P48842.
    SMRi P48842. Positions 17-350.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH53. Glycoside Hydrolase Family 53.
    mycoCLAPi GAN53A_ASPAC.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P48842.

    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. "Expression cloning, purification and characterization of a beta-1,4-galactanase from Aspergillus aculeatus."
      Christgau S., Sandal T., Kofod L.V., Dalboege H.
      Curr. Genet. 27:135-141(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-44.
      Strain: KSM 510.
    2. "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: MUTAGENESIS OF ASP-198.
    3. "Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A."
      Ryttersgaard C., Lo Leggio L., Coutinho P.M., Henrissat B., Larsen S.
      Biochemistry 41:15135-15143(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiGANA_ASPAC
    AccessioniPrimary (citable) accession number: P48842
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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