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A7WM73

- HEXO1_ARATH

UniProt

A7WM73 - HEXO1_ARATH

Protein

Beta-hexosaminidase 1

Gene

HEXO1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
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    Functioni

    Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, pyridylaminated chitobiose, p-nitrophenyl-beta-N-acetylglucosaminide, p-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-GlcNAc), p-nitrophenyl-2-acetamido-2-deoxy-beta-D-galactopyranoside (pNP-GalNAc), 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc), and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside (MU-GlcNAc-6SO4) as substrates. Removes terminal GlcNAc residues from alpha1,3- and alpha1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Required for the presence of paucimannosidic N-glycans in glycoproteins of roots and, to a lower extent, of leaves.3 Publications

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

    Enzyme regulationi

    Inhibited by N-acetylcastanospermine, 2-acet-amido-1,2-dideoxynojirimycin and PUGNAc.1 Publication

    Kineticsi

    1. KM=0.7 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)2 Publications

    Vmax=151 µmol/min/mg enzyme with pNP-GlcNAc as substrate (at pH 4.6 and 37 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 4-5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei332 – 3321Proton donorBy similarity

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: TAIR
    2. hexosaminidase activity Source: TAIR

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G55260-MONOMER.
    ReactomeiREACT_187588. Hyaluronan uptake and degradation.
    REACT_187659. Glycosphingolipid metabolism.
    REACT_187663. Keratan sulfate degradation.
    REACT_215132. CS/DS degradation.

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase 1 (EC:3.2.1.52)
    Alternative name(s):
    Beta-GlcNAcase 1
    Beta-N-acetylhexosaminidase 1
    Beta-hexosaminidase 2
    Short name:
    AtHEX2
    N-acetyl-beta-glucosaminidase 1
    Gene namesi
    Name:HEXO1
    Synonyms:HEX2
    Ordered Locus Names:At3g55260
    ORF Names:T26I12.140
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G55260.

    Subcellular locationi

    Vacuole 2 Publications

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. plant-type cell wall Source: TAIR
    3. vacuole Source: TAIR

    Keywords - Cellular componenti

    Vacuole

    Pathology & Biotechi

    Disruption phenotypei

    Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and, to a lower extent, in leaves.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 541521Beta-hexosaminidase 1PRO_0000420286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi295 ↔ 337By similarity
    Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi511 ↔ 538By similarity

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiA7WM73.
    PRIDEiA7WM73.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, flowers and siliques.1 Publication

    Gene expression databases

    GenevestigatoriA7WM73.

    Interactioni

    Protein-protein interaction databases

    IntActiA7WM73. 1 interaction.
    STRINGi3702.AT3G55260.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliA7WM73.
    SMRiA7WM73. Positions 29-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    HOGENOMiHOG000157972.
    InParanoidiA7WM73.
    KOiK12373.
    OMAiWTPVNWE.
    PhylomeDBiA7WM73.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view]
    PfamiPF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSiPR00738. GLHYDRLASE20.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A7WM73-1 [UniParc]FASTAAdd to Basket

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    MSTNLLRLIL LFITLSITSS LSTPSPADSP PYLWPLPAEF SFGNETLSVD    50
    PTVTLIVAGN GGGSLIIRAA FDRYMGIIFK HASGRGSLLS RIRFLKMVEY 100
    DITSLKIVVH SDSEELQLGV DESYTLMVSK KNEQSIVGAA TIEANTVYGA 150
    LRGLETFSQL CAFDYITKSV QIYKAPWYIQ DKPRFGYRGL LIDTSRHYLP 200
    IDVIKQIIES MSFAKLNVLH WHIVDEQSFP LETPTYPNLW KGAYSRWERY 250
    TVEDASEIVR FAKMRGINVM AEVDVPGHAE SWGTGYPDLW PSLSCREPLD 300
    VTKNFTFDVI SGILADMRKI FPFELFHLGG DEVNTDCWKN TTHVKEWLQG 350
    RNFTTKDAYK YFVLRAQQIA ISKNWTPVNW EETFSSFGKD LDPRTVIQNW 400
    LVSDICQKAV AKGFRCIFSN QGYWYLDHLD VPWEEVYNTE PLNGIEDPSL 450
    QKLVIGGEVC MWGETADTSV VLQTIWPRAA AAAERMWSTR EAVSKGNITL 500
    TALPRLHYFR CLLNNRGVPA APVDNFYARR PPLGPGSCYA Q 541
    Length:541
    Mass (Da):61,230
    Last modified:October 23, 2007 - v1
    Checksum:i441D48C6F1FCCF56
    GO

    Sequence cautioni

    The sequence AAM61367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB75760.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841G → V in AAM61367. 1 PublicationCurated
    Sequence conflicti181 – 1811D → G in BAE99290. 1 PublicationCurated
    Sequence conflicti347 – 3471W → R in BAE99290. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM493720 mRNA. Translation: CAM35467.1.
    AL132954 Genomic DNA. Translation: CAB75760.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79360.1.
    AK227260 mRNA. Translation: BAE99290.1.
    AY084801 mRNA. Translation: AAM61367.1. Different initiation.
    BT000920 mRNA. Translation: AAN41320.1.
    PIRiT47665.
    RefSeqiNP_567017.2. NM_115384.3.
    UniGeneiAt.21628.

    Genome annotation databases

    EnsemblPlantsiAT3G55260.1; AT3G55260.1; AT3G55260.
    GeneIDi824692.
    KEGGiath:AT3G55260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM493720 mRNA. Translation: CAM35467.1 .
    AL132954 Genomic DNA. Translation: CAB75760.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE79360.1 .
    AK227260 mRNA. Translation: BAE99290.1 .
    AY084801 mRNA. Translation: AAM61367.1 . Different initiation.
    BT000920 mRNA. Translation: AAN41320.1 .
    PIRi T47665.
    RefSeqi NP_567017.2. NM_115384.3.
    UniGenei At.21628.

    3D structure databases

    ProteinModelPortali A7WM73.
    SMRi A7WM73. Positions 29-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A7WM73. 1 interaction.
    STRINGi 3702.AT3G55260.1-P.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    Proteomic databases

    PaxDbi A7WM73.
    PRIDEi A7WM73.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G55260.1 ; AT3G55260.1 ; AT3G55260 .
    GeneIDi 824692.
    KEGGi ath:AT3G55260.

    Organism-specific databases

    TAIRi AT3G55260.

    Phylogenomic databases

    eggNOGi COG3525.
    HOGENOMi HOG000157972.
    InParanoidi A7WM73.
    KOi K12373.
    OMAi WTPVNWE.
    PhylomeDBi A7WM73.

    Enzyme and pathway databases

    BioCyci ARA:AT3G55260-MONOMER.
    Reactomei REACT_187588. Hyaluronan uptake and degradation.
    REACT_187659. Glycosphingolipid metabolism.
    REACT_187663. Keratan sulfate degradation.
    REACT_215132. CS/DS degradation.

    Miscellaneous databases

    PROi A7WM73.

    Gene expression databases

    Genevestigatori A7WM73.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view ]
    Pfami PF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Enzymatic properties and subcellular localization of Arabidopsis beta-N-acetylhexosaminidases."
      Strasser R., Bondili J.S., Schoberer J., Svoboda B., Liebminger E., Glossl J., Altmann F., Steinkellner H., Mach L.
      Plant Physiol. 145:5-16(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, GENE FAMILY, NOMENCLATURE.
    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. "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 (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-541.
    6. "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] OF 97-541.
      Strain: cv. Columbia.
    7. "Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and insects."
      Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J., Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.
      J. Biol. Chem. 282:27825-27840(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REVIEW.
    8. "Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana."
      Liebminger E., Veit C., Pabst M., Batoux M., Zipfel C., Altmann F., Mach L., Strasser R.
      J. Biol. Chem. 286:10793-10802(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiHEXO1_ARATH
    AccessioniPrimary (citable) accession number: A7WM73
    Secondary accession number(s): Q0WUA8, Q8LFK0, Q9M3C5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 63 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