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P48981

- BGAL_MALDO

UniProt

P48981 - BGAL_MALDO

Protein

Beta-galactosidase

Gene
N/A
Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Involved in cell wall degradation. Degrades polysaccharides containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-beta-D-galactanase.

    Catalytic activityi

    Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei182 – 1821Proton donorSequence Analysis
    Active sitei251 – 2511NucleophileSequence Analysis

    GO - Molecular functioni

    1. beta-galactosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase (EC:3.2.1.23)
    Alternative name(s):
    Acid beta-galactosidase
    Short name:
    Lactase
    Exo-(1-->4)-beta-D-galactanase
    OrganismiMalus domestica (Apple) (Pyrus malus)
    Taxonomic identifieri3750 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 731708Beta-galactosidasePRO_0000012197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP48981.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008979. Galactose-bd-like.
    IPR019801. Glyco_hydro_35_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR001944. Glycoside_Hdrlase_35.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR23421. PTHR23421. 1 hit.
    PfamiPF01301. Glyco_hydro_35. 1 hit.
    [Graphical view]
    PRINTSiPR00742. GLHYDRLASE35.
    SUPFAMiSSF49785. SSF49785. 3 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P48981-1 [UniParc]FASTAAdd to Basket

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    MGVGIQTMWS ILLLFSCIFS AASASVSYDH KAIIINGQKR ILISGSIHYP    50
    RSTPEMWPDL IQKAKDGGLD VIQTYVFWNG HEPSPGNYYF EERYDLVKFI 100
    KLVQQEGLFV NLRIGPYVCA EWNFGGFPVW LKYVPGIAFR TDNEPFKAAM 150
    QKFTEKIVSM MKAEKLFQTQ GGPIILSQIE NEFGPVEWEI GAPGKAYTKW 200
    AAQMAVGLDT GVPWIMCKQE DAPDPVIDTC NGFYCENFKP NKDYKPKMWT 250
    EVWTGWYTEF GGAVPTRPAE DVAFSVARFI QSGGSFLNYY MYHGGTNFGR 300
    TAGGPFMATS YDYDAPLDEY GLPREPKWGH LRDLHKAIKS CESALVSVDP 350
    SVTKLGSNQE AHVFKSESDC AAFLANYDAK YSVKVSFGGG QYDLPPWSIS 400
    ILPDCKTEVY NTAKVGSQSS QVQMTPVHSG FPWQSFIEET TSSDETDTTT 450
    LDGLYEQINI TRDTTDYLWY MTDITIGSDE AFLKNGKSPL LTIFSAGHAL 500
    NVFINGQLSG TVYGSLENPK LSFSQNVNLR SGINKLALLS ISVGLPNVGT 550
    HFETWNAGVL GPITLKGLNS GTWDMSGWKW TYKTGLKGEA LGLHTVTGSS 600
    SVEWVEGPSM AEKQPLTWYK ATFNAPPGDA PLALDMGSMG KGQIWINGQS 650
    VGRHWPGYIA RGSCGDCSYA GTYDDKKCRT HCGEPSQRWY HIPRSWLTPT 700
    GNLLVVFEEW GGDPSRISLV ERGTALDAKK L 731
    Length:731
    Mass (Da):80,996
    Last modified:February 1, 1996 - v1
    Checksum:iFAB65D24A0D30BD4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29451 mRNA. Translation: AAA62324.1.
    PIRiT17002.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29451 mRNA. Translation: AAA62324.1 .
    PIRi T17002.

    3D structure databases

    ProteinModelPortali P48981.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008979. Galactose-bd-like.
    IPR019801. Glyco_hydro_35_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR001944. Glycoside_Hdrlase_35.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR23421. PTHR23421. 1 hit.
    Pfami PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SUPFAMi SSF49785. SSF49785. 3 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Apple beta-galactosidase. Activity against cell wall polysaccharides and characterization of a related cDNA clone."
      Ross G.S., Wegrzyn T., Macrae E.A., Redgwell R.J.
      Plant Physiol. 106:521-528(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Granny Smith.
      Tissue: Fruit cortical tissue.

    Entry informationi

    Entry nameiBGAL_MALDO
    AccessioniPrimary (citable) accession number: P48981
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3