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Protein

Alpha-L-arabinofuranosidase 1

Gene

ASD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the coordinated dissolution of the cell wall matrix during abscission and in the secondary cell wall formation in xylem vessels. Prefers arabinoxylan, but may also use pectic arabinans as substrates.3 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.2 Publications

Kineticsi

  1. KM=0.48 mM for p-nitrophenyl-beta-D-xylopyranoside2 Publications
  2. KM=5.2 mM for (1,5)-alpha-L-arabinobiose (at 37 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 4.3.2 Publications

    Temperature dependencei

    Optimum temperature is 67 degrees Celsius.2 Publications

    GO - Molecular functioni

    • alpha-L-arabinofuranosidase activity Source: TAIR
    • xylan 1,4-beta-xylosidase activity Source: TAIR

    GO - Biological processi

    • L-arabinose metabolic process Source: InterPro
    • xylan catabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G10740-MONOMER.
    SABIO-RKQ9SG80.

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-L-arabinofuranosidase 1 (EC:3.2.1.55)
    Short name:
    AtASD1
    Alternative name(s):
    Beta-D-xylosidase (EC:3.2.1.-)
    Gene namesi
    Name:ASD1
    Synonyms:ARAF, ARAF1
    Ordered Locus Names:At3g10740
    ORF Names:T7M13.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G10740.

    Subcellular locationi

    GO - Cellular componenti

    • apoplast Source: TAIR
    • plant-type cell wall Source: TAIR
    • proteinaceous extracellular matrix Source: UniProtKB-SubCell
    • vacuole Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype; even in asd1 and asd2 double mutant.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 678645Alpha-L-arabinofuranosidase 1PRO_0000384371Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9SG80.
    PRIDEiQ9SG80.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, flowers, stems, siliques and seedlings. Observed in zones of cell proliferation, the vascular system and floral abscission zones. Expressed in the guard cells in stems, in xylem vessels and parenchyma cells surrounding the vessels, in the cambium and in the phloem, but not in the secondary xylem.3 Publications

    Inductioni

    Not induced by hormones or during leaf senescence.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G10740.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SG80.
    SMRiQ9SG80. Positions 229-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini152 – 23988CBM-cenCAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3534.
    HOGENOMiHOG000115340.
    InParanoidiQ9SG80.
    KOiK01209.
    OMAiTNEARDE.
    PhylomeDBiQ9SG80.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR010720. Alpha-L-AF_C.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SMARTiSM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9SG80-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDMESWKLLR SVCVLSFLLG SCFVYQSLRV VDAQEDPKPA VTLQVDASNG
    60 70 80 90 100
    GGRPIPETLF GIFFEEINHA GAGGLWAELV SNRGFEAGGQ NTPSNIWPWS
    110 120 130 140 150
    IVGDHSSIYV ATDRSSCFER NKIALRMDVL CDSKGCPSGG VGVYNPGYWG
    160 170 180 190 200
    MNIEEGKKYK VALYVRSTGD IDLSVSLTSS NGSRTLASEK IIASASDVSK
    210 220 230 240 250
    WIKKEVLLEA KATDPSARLQ LTTTKKGSIW IDQVSAMPVD THKGHGFRND
    260 270 280 290 300
    LFQMMADIKP RFIRFPGGCF VEGEWLSNAF RWKETVGPWE ERPGHFGDVW
    310 320 330 340 350
    KYWTDDGLGH FEFFQMAEDI GAAPIWVFNN GISHNDEVET ASIMPFVQEA
    360 370 380 390 400
    LDGIEFARGD ANSTWGSVRA KMGRQEPFEL KYVAIGNEDC GKTYYRGNYI
    410 420 430 440 450
    VFYDAIKKAY PDIKIISNCD GSSHPLDHPA DYYDYHIYTS ASNLFSMYHQ
    460 470 480 490 500
    FDRTSRKGPK AFVSEYAVTG KDAGTGSLLA SLAEAAFLIG LEKNSDIVEM
    510 520 530 540 550
    ASYAPLFVNT NDRRWNPDAI VFNSSHLYGT PSYWVQRFFA ESSGATLLTS
    560 570 580 590 600
    TLKGNSTSLV ASAISWKNNG KDYIRIKAVN FGANSENMQV LVTGLDPNVM
    610 620 630 640 650
    RVSGSKKTVL TSTNVMDENS FSQPEKVVPH ESLLELAEED MTVVLPPHSF
    660 670
    SSFDLLKESA KIRMPISDSS SHQKTTTV
    Length:678
    Mass (Da):75,045
    Last modified:May 1, 2000 - v1
    Checksum:i8116546072E6CA9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511L → P in AAN28883 (PubMed:14593172).Curated
    Sequence conflicti251 – 2511L → P in AAK50089 (PubMed:14593172).Curated
    Sequence conflicti253 – 2542QM → HL in AAO92261 (PubMed:14512381).Curated
    Sequence conflicti453 – 4531R → G in AAO92261 (PubMed:14512381).Curated
    Sequence conflicti499 – 4991E → D in AAO92261 (PubMed:14512381).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY243509 mRNA. Translation: AAO92261.1.
    AC011708 Genomic DNA. Translation: AAF19575.1.
    CP002686 Genomic DNA. Translation: AEE74949.1.
    AF372949 mRNA. Translation: AAK50089.1.
    AY143944 mRNA. Translation: AAN28883.1.
    AK222175 mRNA. Translation: BAD95302.1.
    AK220766 mRNA. Translation: BAD93969.1.
    RefSeqiNP_187685.1. NM_111911.4.
    UniGeneiAt.20271.

    Genome annotation databases

    EnsemblPlantsiAT3G10740.1; AT3G10740.1; AT3G10740.
    GeneIDi820243.
    KEGGiath:AT3G10740.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY243509 mRNA. Translation: AAO92261.1.
    AC011708 Genomic DNA. Translation: AAF19575.1.
    CP002686 Genomic DNA. Translation: AEE74949.1.
    AF372949 mRNA. Translation: AAK50089.1.
    AY143944 mRNA. Translation: AAN28883.1.
    AK222175 mRNA. Translation: BAD95302.1.
    AK220766 mRNA. Translation: BAD93969.1.
    RefSeqiNP_187685.1. NM_111911.4.
    UniGeneiAt.20271.

    3D structure databases

    ProteinModelPortaliQ9SG80.
    SMRiQ9SG80. Positions 229-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT3G10740.1.

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.

    Proteomic databases

    PaxDbiQ9SG80.
    PRIDEiQ9SG80.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G10740.1; AT3G10740.1; AT3G10740.
    GeneIDi820243.
    KEGGiath:AT3G10740.

    Organism-specific databases

    TAIRiAT3G10740.

    Phylogenomic databases

    eggNOGiCOG3534.
    HOGENOMiHOG000115340.
    InParanoidiQ9SG80.
    KOiK01209.
    OMAiTNEARDE.
    PhylomeDBiQ9SG80.

    Enzyme and pathway databases

    BioCyciARA:AT3G10740-MONOMER.
    SABIO-RKQ9SG80.

    Miscellaneous databases

    PROiQ9SG80.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR010720. Alpha-L-AF_C.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SMARTiSM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Two alpha-L-arabinofuranosidase genes in Arabidopsis thaliana are differentially expressed during vegetative growth and flower development."
      Fulton L.M., Cobbett C.S.
      J. Exp. Bot. 54:2467-2477(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY HORMONES.
      Strain: cv. Columbia.
    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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-678.
      Strain: cv. Columbia.
    6. "Purification and characterization of enzymes exhibiting beta-D-xylosidase activities in stem tissues of Arabidopsis."
      Minic Z., Rihouey C., Do C.T., Lerouge P., Jouanin L.
      Plant Physiol. 135:867-878(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    7. "Purification, functional characterization, cloning, and identification of mutants of a seed-specific arabinan hydrolase in Arabidopsis."
      Minic Z., Do C.-T., Rihouey C., Morin H., Lerouge P., Jouanin L.
      J. Exp. Bot. 57:2339-2351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Cell wall modifications in Arabidopsis plants with altered alpha-L-arabinofuranosidase activity."
      Chavez Montes R.A., Ranocha P., Martinez Y., Minic Z., Jouanin L., Marquis M., Saulnier L., Fulton L.M., Cobbett C.S., Bitton F., Renou J.-P., Jauneau A., Goffner D.
      Plant Physiol. 147:63-77(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiASD1_ARATH
    AccessioniPrimary (citable) accession number: Q9SG80
    Secondary accession number(s): Q56W72
    , Q570E2, Q84RC5, Q94JT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: May 1, 2000
    Last modified: June 24, 2015
    This is version 88 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.