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Q54SC9

- HEXA2_DICDI

UniProt

Q54SC9 - HEXA2_DICDI

Protein

Beta-hexosaminidase subunit A2

Gene

hexa2

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei314 – 3141Proton donorBy similarity

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_210507. Glycosphingolipid metabolism.
    REACT_220518. Keratan sulfate degradation.
    REACT_221941. CS/DS degradation.
    REACT_226217. Hyaluronan uptake and degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase subunit A2 (EC:3.2.1.52)
    Alternative name(s):
    Beta-N-acetylhexosaminidase subunit A2
    N-acetyl-beta-glucosaminidase subunit A2
    Gene namesi
    Name:hexa2
    ORF Names:DDB_G0282539
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0282539. nagB.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 541520Beta-hexosaminidase subunit A2PRO_0000331236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ54SC9.

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDBDRAFT_0204822.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54SC9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    KOiK12373.
    OMAiSATCKEP.
    PhylomeDBiQ54SC9.

    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.

    Q54SC9-1 [UniParc]FASTAAdd to Basket

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    MINKFLTIFL IFSIVIIKVL SQSSNEQPLN VVPYPQEVTM IGCNIPLSVG    50
    SISIKSNIES TILSISISRY QSLFFPFVSN NVLKDSSSNI ELSLIIASDD 100
    ETLELGIDES YFLLVNQDTY QIKANTIYGA MRGLETFKQM VVYDVVENSY 150
    SLTCAEVVDY PTYQWRGLLV DNARHFLPKN MVLHIIDSMG YNKFNTMHWH 200
    LIDTVAFPVE SKTYPKLTEA LLGPGAIITH DDILEVVAYA KTYGIRVIPE 250
    FDVPGHSASW GVGYPELLSN CPGYPQSSIP LDCSNPYTYS FLENFFSEIA 300
    PLFQDSYFHT GGDELVIDCW ANDTSIQKWM KTNNYNTSDA FQYFEDQLDV 350
    ILKSINRTKI AWNDVLQHGV KFDKETTLVQ TWTNINDLRD VLAAGYKTIT 400
    SFFFYLDRQS PTGNHYHYEW QDTWEDFYAS DPRLNITSNA ENILGGEATM 450
    FGEQVSTVNW DARVWPRAIG ISERLWSATE INNITLALPR IGQFSCDMSR 500
    RGISSGPLFP DFCSLPDDLS FSFKPVYQLS KDEIKLILKK K 541
    Length:541
    Mass (Da):61,533
    Last modified:May 24, 2005 - v1
    Checksum:iF670234F1DD3D075
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000047 Genomic DNA. Translation: EAL66129.1.
    RefSeqiXP_640110.1. XM_635018.1.

    Genome annotation databases

    EnsemblProtistsiDDB0304517; DDB0304517; DDB_G0282539.
    GeneIDi8623642.
    KEGGiddi:DDB_G0282539.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000047 Genomic DNA. Translation: EAL66129.1 .
    RefSeqi XP_640110.1. XM_635018.1.

    3D structure databases

    ProteinModelPortali Q54SC9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDBDRAFT_0204822.

    Proteomic databases

    PRIDEi Q54SC9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0304517 ; DDB0304517 ; DDB_G0282539 .
    GeneIDi 8623642.
    KEGGi ddi:DDB_G0282539.

    Organism-specific databases

    dictyBasei DDB_G0282539. nagB.

    Phylogenomic databases

    eggNOGi COG3525.
    KOi K12373.
    OMAi SATCKEP.
    PhylomeDBi Q54SC9.

    Enzyme and pathway databases

    Reactomei REACT_210507. Glycosphingolipid metabolism.
    REACT_220518. Keratan sulfate degradation.
    REACT_221941. CS/DS degradation.
    REACT_226217. Hyaluronan uptake and degradation.

    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. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.

    Entry informationi

    Entry nameiHEXA2_DICDI
    AccessioniPrimary (citable) accession number: Q54SC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    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