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Protein

Xyloglucan endotransglucosylase/hydrolase protein 31

Gene

XTH31

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

Functioni

Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Involved in the accumulation of hemicelluloses. Has a high XEH activity and only a slight XET activity in vitro, but the main in planta activity seems to be XET, thus controlling aluminum sensitivity (PubMed:23204407, PubMed:23104861, PubMed:25446234). Acceptor preferences are XXXGol = XXFGol > XXLGol > XLLGol = XLFGol (PubMed:25446234).3 Publications

Catalytic activityi

Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.1 Publication
Xyloglucan + H2O = xyloglucan oligosaccharides.2 Publications

Kineticsi

KM for xyloglucan as donor substrate is 1.6 mg/ml. KM is quoted in mg/ml, not µM, because XTHs are able to utilise any segment of the polysaccharide chain equally well, not just one site per molecule as with the acceptor.1 Publication

  1. KM=86 µM for XXXGol1 Publication

    pH dependencei

    Optimum pH is 5 for the XET activity. Optimum pH is 4.5 - 4.75 for the XEH activity.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei114 – 1141NucleophileBy similarity
    Active sitei118 – 1181Proton donorBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • cellular glucan metabolic process Source: InterPro
    • cell wall macromolecule catabolic process Source: TAIR
    • cell wall organization Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Transferase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciARA:AT3G44990-MONOMER.

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xyloglucan endotransglucosylase/hydrolase protein 311 Publication (EC:2.4.1.2071 Publication, EC:3.2.1.1511 Publication)
    Short name:
    At-XTH311 Publication
    Short name:
    AtXTR8
    Short name:
    XTH-31
    Gene namesi
    Name:XTH311 Publication
    Synonyms:ATXG, XTR8
    Ordered Locus Names:At3g44990
    ORF Names:F14D17.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G44990.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Apoplast, Cell membrane, Cell wall, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Reduced growth, decreased cell wall xyloglucan content and increased aluminum resistance (PubMed:23204407). No visible phenotype under normal growth conditions (PubMed:23104861).2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 293273Xyloglucan endotransglucosylase/hydrolase protein 31PRO_0000011831Add
    BLAST

    Post-translational modificationi

    Contains at least one intrachain disulfide bond essential for its enzymatic activity.By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP93046.
    PRIDEiP93046.

    Expressioni

    Tissue specificityi

    Predominantly expressed in root (PubMed:11673616, Ref. 1). Weakly expressed in influorescence stems (PubMed:11673616). Expressed in root tips and elongation zones, stems, young leaves, flowers and siliques (PubMed:23204407). Expressed in root, hypocotyl, and etiolated whole seedlings (PubMed:23104861).4 Publications

    Developmental stagei

    Expressed in germinating seeds from 24 hours after imbibation, and reaches a maximum level at 72 hours. After 96 hours, it then decreases.1 Publication

    Inductioni

    Up-regulated by gibberellins (Probable). Not induced by auxin (Ref. 1). Down-regulated by aluminum (PubMed:21285327, PubMed:23204407).Curated3 Publications

    Interactioni

    Subunit structurei

    Interacts with XTH17. The formation of an XTH17-XTH31 dimer may be required for XET activity.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT3G44990.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP93046.
    SMRiP93046. Positions 18-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG324158.
    HOGENOMiHOG000236368.
    InParanoidiP93046.
    KOiK08235.
    OMAiYPGNHDE.
    PhylomeDBiP93046.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR000757. Glyco_hydro_16.
    IPR016455. XET.
    IPR010713. XET_C.
    [Graphical view]
    PfamiPF00722. Glyco_hydro_16. 1 hit.
    PF06955. XET_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005604. XET. 1 hit.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P93046-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALSLIFLAL LVLCPSSGHS QRSPSPGYYP SSRVPTSPFD REFRTLWGSQ
    60 70 80 90 100
    HQRREQDVVT LWLDKSTGSG FKSLRPYRSG YFGASIKLQP GFTAGVDTSL
    110 120 130 140 150
    YLSNNQEHPG DHDEVDIEFL GTTPGKPYSL QTNVFVRGSG DRNVIGREMK
    160 170 180 190 200
    FTLWFDPTQD FHHYAILWNP NQIVFFVDDV PIRTYNRKNE AIFPTRPMWV
    210 220 230 240 250
    YGSIWDASDW ATENGRIKAD YRYQPFVAKY KNFKLAGCTA DSSSSCRPPS
    260 270 280 290
    PAPMRNRGLS RQQMAALTWA QRNFLVYNYC HDPKRDHTQT PEC
    Length:293
    Mass (Da):33,541
    Last modified:November 28, 2003 - v2
    Checksum:iD999B4C62C5ABCA8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111L → V in CAA63553 (Ref. 1) Curated
    Sequence conflicti260 – 2601S → T in CAA63553 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X92975 mRNA. Translation: CAA63553.1.
    AL353992 Genomic DNA. Translation: CAB89314.1.
    CP002686 Genomic DNA. Translation: AEE77976.1.
    AY056163 mRNA. Translation: AAL07012.1.
    AY136454 mRNA. Translation: AAM97119.1.
    BT006326 mRNA. Translation: AAP13434.1.
    PIRiT48975.
    RefSeqiNP_190085.1. NM_114368.2.
    UniGeneiAt.20372.

    Genome annotation databases

    EnsemblPlantsiAT3G44990.1; AT3G44990.1; AT3G44990.
    GeneIDi823634.
    KEGGiath:AT3G44990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X92975 mRNA. Translation: CAA63553.1.
    AL353992 Genomic DNA. Translation: CAB89314.1.
    CP002686 Genomic DNA. Translation: AEE77976.1.
    AY056163 mRNA. Translation: AAL07012.1.
    AY136454 mRNA. Translation: AAM97119.1.
    BT006326 mRNA. Translation: AAP13434.1.
    PIRiT48975.
    RefSeqiNP_190085.1. NM_114368.2.
    UniGeneiAt.20372.

    3D structure databases

    ProteinModelPortaliP93046.
    SMRiP93046. Positions 18-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT3G44990.1.

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Proteomic databases

    PaxDbiP93046.
    PRIDEiP93046.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G44990.1; AT3G44990.1; AT3G44990.
    GeneIDi823634.
    KEGGiath:AT3G44990.

    Organism-specific databases

    GeneFarmi2646. 265.
    TAIRiAT3G44990.

    Phylogenomic databases

    eggNOGiNOG324158.
    HOGENOMiHOG000236368.
    InParanoidiP93046.
    KOiK08235.
    OMAiYPGNHDE.
    PhylomeDBiP93046.

    Enzyme and pathway databases

    BioCyciARA:AT3G44990-MONOMER.

    Miscellaneous databases

    PROiP93046.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR000757. Glyco_hydro_16.
    IPR016455. XET.
    IPR010713. XET_C.
    [Graphical view]
    PfamiPF00722. Glyco_hydro_16. 1 hit.
    PF06955. XET_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005604. XET. 1 hit.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A new cDNA encoding a xyloglucan endo-transglycosylase-related polypeptide (AtXTR8) preferentially expressed in seedling, root and stem of Arabidopsis thaliana."
      Aubert D., Herzog M.
      Plant Sci. 121:187-196(1996)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Tissue: Seed.
    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. "A comprehensive expression analysis of all members of a gene family encoding cell-wall enzymes allowed us to predict cis-regulatory regions involved in cell-wall construction in specific organs of Arabidopsis."
      Yokoyama R., Nishitani K.
      Plant Cell Physiol. 42:1025-1033(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature."
      Rose J.K.C., Braam J., Fry S.C., Nishitani K.
      Plant Cell Physiol. 43:1421-1435(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    7. "Cell wall hemicellulose contributes significantly to aluminum adsorption and root growth in Arabidopsis."
      Yang J.L., Zhu X.F., Peng Y.X., Zheng C., Li G.X., Liu Y., Shi Y.Z., Zheng S.J.
      Plant Physiol. 155:1885-1892(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ALUMINUM.
    8. "XTH31, encoding an in vitro XEH/XET-active enzyme, regulates aluminum sensitivity by modulating in vivo XET action, cell wall xyloglucan content, and aluminum binding capacity in Arabidopsis."
      Zhu X.F., Shi Y.Z., Lei G.J., Fry S.C., Zhang B.C., Zhou Y.H., Braam J., Jiang T., Xu X.Y., Mao C.Z., Pan Y.J., Yang J.L., Wu P., Zheng S.J.
      Plant Cell 24:4731-4747(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ALUMINUM.
    9. "Group III-A XTH genes of Arabidopsis encode predominant xyloglucan endohydrolases that are dispensable for normal growth."
      Kaewthai N., Gendre D., Eklof J.M., Ibatullin F.M., Ezcurra I., Bhalerao R.P., Brumer H.
      Plant Physiol. 161:440-454(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    10. "Distinct catalytic capacities of two aluminium-repressed Arabidopsis thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31, heterologously produced in Pichia."
      Shi Y.Z., Zhu X.F., Miller J.G., Gregson T., Zheng S.J., Fry S.C.
      Phytochemistry 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Xyloglucan endotransglucosylase-hydrolase17 interacts with xyloglucan endotransglucosylase-hydrolase31 to confer xyloglucan endotransglucosylase action and affect aluminum sensitivity in Arabidopsis."
      Zhu X.F., Wan J.X., Sun Y., Shi Y.Z., Braam J., Li G.X., Zheng S.J.
      Plant Physiol. 165:1566-1574(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XTH17.

    Entry informationi

    Entry nameiXTH31_ARATH
    AccessioniPrimary (citable) accession number: P93046
    Secondary accession number(s): Q9LXH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: November 28, 2003
    Last modified: June 24, 2015
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In contrast to group 1 and group 2 endotransglucosylase/hydrolase proteins, it may not contain the ligase activity, and may catalyze endohydrolysis xyloglucan polymers only.

    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.