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Q9LFA6

- BGAL2_ARATH

UniProt

Q9LFA6 - BGAL2_ARATH

Protein

Beta-galactosidase 2

Gene

BGAL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (03 May 2011)
      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 sitei185 – 1851Proton donorSequence Analysis
    Active sitei254 – 2541NucleophileSequence 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:AT3G52840-MONOMER.

    Protein family/group databases

    CAZyiGH35. Glycoside Hydrolase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactosidase 2 (EC:3.2.1.23)
    Short name:
    Lactase 2
    Gene namesi
    Name:BGAL2
    Ordered Locus Names:At3g52840
    ORF Names:F8J2.10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G52840.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: TAIR

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 727700Beta-galactosidase 2PRO_5000065878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9LFA6.
    PRIDEiQ9LFA6.

    Expressioni

    Tissue specificityi

    Ubiquitous, with higher expression levels in roots and siliques.2 Publications

    Inductioni

    By sugar starvation.1 Publication

    Gene expression databases

    GenevestigatoriQ9LFA6.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G52840.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LFA6.
    SMRiQ9LFA6. Positions 26-725.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 35 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1874.
    HOGENOMiHOG000239919.
    InParanoidiQ9LFA6.
    KOiK12309.
    OMAiGGAIPNR.

    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.

    Q9LFA6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSMHFRNKAW IILAILCFSS LIHSTEAVVT YDHKALIING QRRILISGSI    50
    HYPRSTPEMW PDLIKKAKEG GLDVIQTYVF WNGHEPSPGN YYFQDRYDLV 100
    KFTKLVHQAG LYLDLRIGPY VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK 150
    IAMQKFTKKI VDMMKEEKLF ETQGGPIILS QIENEYGPMQ WEMGAAGKAY 200
    SKWTAEMALG LSTGVPWIMC KQEDAPYPII DTCNGFYCEG FKPNSDNKPK 250
    LWTENWTGWF TEFGGAIPNR PVEDIAFSVA RFIQNGGSFM NYYMYYGGTN 300
    FDRTAGVFIA TSYDYDAPID EYGLLREPKY SHLKELHKVI KLCEPALVSV 350
    DPTITSLGDK QEIHVFKSKT SCAAFLSNYD TSSAARVMFR GFPYDLPPWS 400
    VSILPDCKTE YYNTAKIRAP TILMKMIPTS TKFSWESYNE GSPSSNEAGT 450
    FVKDGLVEQI SMTRDKTDYF WYFTDITIGS DESFLKTGDN PLLTIFSAGH 500
    ALHVFVNGLL AGTSYGALSN SKLTFSQNIK LSVGINKLAL LSTAVGLPNA 550
    GVHYETWNTG ILGPVTLKGV NSGTWDMSKW KWSYKIGLRG EAMSLHTLAG 600
    SSAVKWWIKG FVVKKQPLTW YKSSFDTPRG NEPLALDMNT MGKGQVWVNG 650
    HNIGRHWPAY TARGNCGRCN YAGIYNEKKC LSHCGEPSQR WYHVPRSWLK 700
    PFGNLLVIFE EWGGDPSGIS LVKRTAK 727
    Length:727
    Mass (Da):82,015
    Last modified:May 3, 2011 - v2
    Checksum:i21FF54744E67F5C5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121I → F in AAN60229. 1 PublicationCurated
    Sequence conflicti220 – 2201C → S in CAB86888. (PubMed:11130713)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270298 mRNA. Translation: CAB64738.1.
    AL132969 Genomic DNA. Translation: CAB86888.1.
    CP002686 Genomic DNA. Translation: AEE78999.1.
    AF367327 mRNA. Translation: AAK32914.1.
    BT000511 mRNA. Translation: AAN18080.1.
    AF083670 mRNA. Translation: AAN60229.1.
    PIRiT47541.
    RefSeqiNP_190852.2. NM_115144.3.
    UniGeneiAt.702.

    Genome annotation databases

    EnsemblPlantsiAT3G52840.1; AT3G52840.1; AT3G52840.
    GeneIDi824450.
    KEGGiath:AT3G52840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ270298 mRNA. Translation: CAB64738.1 .
    AL132969 Genomic DNA. Translation: CAB86888.1 .
    CP002686 Genomic DNA. Translation: AEE78999.1 .
    AF367327 mRNA. Translation: AAK32914.1 .
    BT000511 mRNA. Translation: AAN18080.1 .
    AF083670 mRNA. Translation: AAN60229.1 .
    PIRi T47541.
    RefSeqi NP_190852.2. NM_115144.3.
    UniGenei At.702.

    3D structure databases

    ProteinModelPortali Q9LFA6.
    SMRi Q9LFA6. Positions 26-725.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G52840.1-P.

    Protein family/group databases

    CAZyi GH35. Glycoside Hydrolase Family 35.

    Proteomic databases

    PaxDbi Q9LFA6.
    PRIDEi Q9LFA6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G52840.1 ; AT3G52840.1 ; AT3G52840 .
    GeneIDi 824450.
    KEGGi ath:AT3G52840.

    Organism-specific databases

    GeneFarmi 490. 90.
    TAIRi AT3G52840.

    Phylogenomic databases

    eggNOGi COG1874.
    HOGENOMi HOG000239919.
    InParanoidi Q9LFA6.
    KOi K12309.
    OMAi GGAIPNR.

    Enzyme and pathway databases

    BioCyci ARA:AT3G52840-MONOMER.

    Gene expression databases

    Genevestigatori Q9LFA6.

    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. "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 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(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. "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
      Stracke R., Palme K.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-569.
    6. "Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana."
      Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.
      Plant Cell Physiol. 47:55-63(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "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.
    8. "Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis."
      Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N.
      Plant Cell Physiol. 48:405-413(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiBGAL2_ARATH
    AccessioniPrimary (citable) accession number: Q9LFA6
    Secondary accession number(s): Q8H7H7, Q9SCW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 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