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Q9MAJ7

- BGAL5_ARATH

UniProt

Q9MAJ7 - BGAL5_ARATH

Protein

Beta-galactosidase 5

Gene

BGAL5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei187 – 1871Proton donorSequence Analysis
    Active sitei256 – 2561NucleophileSequence 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

    Enzyme and pathway databases

    BioCyciARA:AT1G45130-MONOMER.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase 5 (EC:3.2.1.23)
    Short name:
    Lactase 5
    Gene namesi
    Name:BGAL5
    Ordered Locus Names:At1g45130
    ORF Names:F27F5.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G45130.

    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 – 732709Beta-galactosidase 5PRO_5000065880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9MAJ7.
    PRIDEiQ9MAJ7.

    Expressioni

    Tissue specificityi

    Expressed in leaves and flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9MAJ7.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT1G45130.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9MAJ7.
    SMRiQ9MAJ7. Positions 30-730.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000239919.
    InParanoidiQ9MAJ7.
    OMAiTYDKKAI.
    PhylomeDBiQ9MAJ7.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR025300. BetaGal_jelly_roll_dom.
    IPR008979. 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.
    PfamiPF13364. BetaGal_dom4_5. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view]
    PRINTSiPR00742. GLHYDRLASE35.
    SUPFAMiSSF49785. SSF49785. 2 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.

    Q9MAJ7-1 [UniParc]FASTAAdd to Basket

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    MGTTILVLSK ILTFLLTTML IGSSVIQCSS VTYDKKAIVI NGHRRILLSG    50
    SIHYPRSTPE MWEDLIKKAK DGGLDVIDTY VFWNGHEPSP GTYNFEGRYD 100
    LVRFIKTIQE VGLYVHLRIG PYVCAEWNFG GFPVWLKYVD GISFRTDNGP 150
    FKSAMQGFTE KIVQMMKEHR FFASQGGPII LSQIENEFEP DLKGLGPAGH 200
    SYVNWAAKMA VGLNTGVPWV MCKEDDAPDP IINTCNGFYC DYFTPNKPYK 250
    PTMWTEAWSG WFTEFGGTVP KRPVEDLAFG VARFIQKGGS YINYYMYHGG 300
    TNFGRTAGGP FITTSYDYDA PIDEYGLVQE PKYSHLKQLH QAIKQCEAAL 350
    VSSDPHVTKL GNYEEAHVFT AGKGSCVAFL TNYHMNAPAK VVFNNRHYTL 400
    PAWSISILPD CRNVVFNTAT VAAKTSHVQM VPSGSILYSV ARYDEDIATY 450
    GNRGTITARG LLEQVNVTRD TTDYLWYTTS VDIKASESFL RGGKWPTLTV 500
    DSAGHAVHVF VNGHFYGSAF GTRENRKFSF SSQVNLRGGA NKIALLSVAV 550
    GLPNVGPHFE TWATGIVGSV VLHGLDEGNK DLSWQKWTYQ AGLRGESMNL 600
    VSPTEDSSVD WIKGSLAKQN KQPLTWYKAY FDAPRGNEPL ALDLKSMGKG 650
    QAWINGQSIG RYWMAFAKGD CGSCNYAGTY RQNKCQSGCG EPTQRWYHVP 700
    RSWLKPKGNL LVLFEELGGD ISKVSVVKRS VN 732
    Length:732
    Mass (Da):81,444
    Last modified:October 1, 2000 - v1
    Checksum:i0442C83D04F7CBC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti453 – 4531R → P in CAB64741. 1 PublicationCurated
    Sequence conflicti571 – 5711V → A in CAB64741. 1 PublicationCurated
    Sequence conflicti633 – 6331A → V in AAL24206. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270301 mRNA. Translation: CAB64741.1.
    AC007915 Genomic DNA. Translation: AAF69162.1.
    CP002684 Genomic DNA. Translation: AEE32082.1.
    AY058098 mRNA. Translation: AAL24206.1.
    AY069911 mRNA. Translation: AAL47461.1.
    AY093977 mRNA. Translation: AAM16238.1.
    RefSeqiNP_175127.1. NM_103587.2.
    UniGeneiAt.24850.
    At.69432.

    Genome annotation databases

    EnsemblPlantsiAT1G45130.1; AT1G45130.1; AT1G45130.
    GeneIDi841080.
    KEGGiath:AT1G45130.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270301 mRNA. Translation: CAB64741.1 .
    AC007915 Genomic DNA. Translation: AAF69162.1 .
    CP002684 Genomic DNA. Translation: AEE32082.1 .
    AY058098 mRNA. Translation: AAL24206.1 .
    AY069911 mRNA. Translation: AAL47461.1 .
    AY093977 mRNA. Translation: AAM16238.1 .
    RefSeqi NP_175127.1. NM_103587.2.
    UniGenei At.24850.
    At.69432.

    3D structure databases

    ProteinModelPortali Q9MAJ7.
    SMRi Q9MAJ7. Positions 30-730.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G45130.1-P.

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9MAJ7.
    PRIDEi Q9MAJ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G45130.1 ; AT1G45130.1 ; AT1G45130 .
    GeneIDi 841080.
    KEGGi ath:AT1G45130.

    Organism-specific databases

    GeneFarmi 494. 90.
    TAIRi AT1G45130.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000239919.
    InParanoidi Q9MAJ7.
    OMAi TYDKKAI.
    PhylomeDBi Q9MAJ7.

    Enzyme and pathway databases

    BioCyci ARA:AT1G45130-MONOMER.

    Gene expression databases

    Genevestigatori Q9MAJ7.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR025300. BetaGal_jelly_roll_dom.
    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 PF13364. BetaGal_dom4_5. 1 hit.
    PF01301. Glyco_hydro_35. 1 hit.
    [Graphical view ]
    PRINTSi PR00742. GLHYDRLASE35.
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The beta-galactosidases are encoding by a multigene family in Arabidopsis thaliana."
      Gy I., Kreis M., Lecharny A.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35."
      Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.
      Phytochemistry 68:1510-1520(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGAL5_ARATH
    AccessioniPrimary (citable) accession number: Q9MAJ7
    Secondary accession number(s): Q93Z63, Q9SCV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 92 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3