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Q8L7S6

- HEXO3_ARATH

UniProt

Q8L7S6 - HEXO3_ARATH

Protein

Beta-hexosaminidase 3

Gene

HEXO3

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 86 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Has a broad substrate specificity. Can use synthetic substrates such as pyridylaminated chitotriose, 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 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

    Slightly inhibited by N-acetylcastanospermine.1 Publication

    Kineticsi

    1. KM=2.2 mM for pNP-GlcNAc (at pH 4.6 and 37 degrees Celsius)2 Publications

    Vmax=50.3 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 sitei329 – 3291Proton 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:AT1G65590-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 3 (EC:3.2.1.52)
    Alternative name(s):
    Beta-GlcNAcase 3
    Beta-N-acetylhexosaminidase 3
    Beta-hexosaminidase 1
    Short name:
    AtHEX1
    N-acetyl-beta-glucosaminidase 3
    Gene namesi
    Name:HEXO3
    Synonyms:HEX1
    Ordered Locus Names:At1g65590
    ORF Names:F5I14.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G65590.

    Subcellular locationi

    Cell membrane 2 Publications

    GO - Cellular componenti

    1. cell wall Source: TAIR
    2. plant-type cell wall Source: TAIR
    3. plasma membrane Source: TAIR

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Reduced amounts of paucimannosidic N-glycans-containg glycoproteins in roots and leaves.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 535511Beta-hexosaminidase 3PRO_0000420288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi292 ↔ 334By similarity
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi506 ↔ 532By similarity

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8L7S6.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    GenevestigatoriQ8L7S6.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L7S6.
    SMRiQ8L7S6. Positions 34-521.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000157972.
    InParanoidiQ8L7S6.
    KOiK12373.
    OMAiSATCKEP.
    PhylomeDBiQ8L7S6.

    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.

    Q8L7S6-1 [UniParc]FASTAAdd to Basket

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    MRGSGAKIAG VLPLFMLFIA GTISAFEDIE RLRIWPLPAQ VSHGGRRMYL    50
    SGDFKLVTEG SKYGDASGIL KEGFDRMLGV VRLSHVISGD RNSSGTGGSA 100
    LLQGLHVIIS SSTDELEYGA DESYKLVVPS PEKPSYAQLE AKSVYGALHG 150
    LQTFSQLCHF NLKKKVIEIL MTPWNIIDQP RFSYRGLLID TSRHYLPLPV 200
    IKNVIDSMTY AKLNVLHWHI VDTQSFPLEI PSYPKLWNGA YSSSQRYTFE 250
    DAAEIVNYAR RRGIHVLAEI DVPGHALSWG KGYPALWPSK NCQEPLDVSS 300
    DFTFKVIDGI LSDFSKIFKF KFVHLGGDEV NTTCWSATPR IAQWLKKHRM 350
    SEKEAYQYFV LRAQKIALSH GYEIINWEET FINFGSKLNR KTVVHNWLNT 400
    GLVENVTASG LRCIVSNQEF WYLDHIDAPW QGFYANEPFQ NITDKKQQSL 450
    VLGGEVCMWG EHIDASDIEQ TIWPRAAAAA ERLWTPYAKL AKNPNNVTTR 500
    LAHFRCLLNQ RGVAAAPLVG GGRVVPFEPG SCLAQ 535
    Length:535
    Mass (Da):60,014
    Last modified:October 1, 2002 - v1
    Checksum:i9295E14DB073F966
    GO

    Sequence cautioni

    The sequence AAB60911.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC001229 Genomic DNA. Translation: AAB60911.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE34399.1.
    AY128283 mRNA. Translation: AAM91092.1.
    BT000831 mRNA. Translation: AAN33206.1.
    PIRiA96681.
    RefSeqiNP_176737.2. NM_105233.4.
    UniGeneiAt.24164.

    Genome annotation databases

    EnsemblPlantsiAT1G65590.1; AT1G65590.1; AT1G65590.
    GeneIDi842871.
    KEGGiath:AT1G65590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC001229 Genomic DNA. Translation: AAB60911.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE34399.1 .
    AY128283 mRNA. Translation: AAM91092.1 .
    BT000831 mRNA. Translation: AAN33206.1 .
    PIRi A96681.
    RefSeqi NP_176737.2. NM_105233.4.
    UniGenei At.24164.

    3D structure databases

    ProteinModelPortali Q8L7S6.
    SMRi Q8L7S6. Positions 34-521.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    Proteomic databases

    PRIDEi Q8L7S6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G65590.1 ; AT1G65590.1 ; AT1G65590 .
    GeneIDi 842871.
    KEGGi ath:AT1G65590.

    Organism-specific databases

    TAIRi AT1G65590.

    Phylogenomic databases

    HOGENOMi HOG000157972.
    InParanoidi Q8L7S6.
    KOi K12373.
    OMAi SATCKEP.
    PhylomeDBi Q8L7S6.

    Enzyme and pathway databases

    BioCyci ARA:AT1G65590-MONOMER.
    Reactomei REACT_187588. Hyaluronan uptake and degradation.
    REACT_187659. Glycosphingolipid metabolism.
    REACT_187663. Keratan sulfate degradation.
    REACT_215132. CS/DS degradation.

    Gene expression databases

    Genevestigatori Q8L7S6.

    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. "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.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "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.
    5. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE.
    6. "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 nameiHEXO3_ARATH
    AccessioniPrimary (citable) accession number: Q8L7S6
    Secondary accession number(s): O04477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 86 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