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Q90744

- NAGAB_CHICK

UniProt

Q90744 - NAGAB_CHICK

Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids By similarity.By similarity

    Catalytic activityi

    Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381Substrate
    Active sitei140 – 1401Nucleophile
    Binding sitei172 – 1721Substrate
    Binding sitei197 – 1971Substrate
    Active sitei201 – 2011Proton donor
    Binding sitei201 – 2011Substrate

    GO - Molecular functioni

    1. alpha-N-acetylgalactosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH27. Glycoside Hydrolase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
    Alternative name(s):
    Alpha-galactosidase B
    Gene namesi
    Name:NAGA
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    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
    Chaini1 – 405405Alpha-N-acetylgalactosaminidasePRO_0000001021Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 631 Publication
    Disulfide bondi25 ↔ 321 Publication
    Disulfide bondi111 ↔ 1421 Publication
    Glycosylationi161 – 1611N-linked (GlcNAc...)1 Publication
    Disulfide bondi171 ↔ 1931 Publication
    Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
    Glycosylationi369 – 3691N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ90744.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000019396.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 155
    Helixi16 – 194
    Turni25 – 273
    Turni29 – 313
    Beta strandi32 – 343
    Helixi35 – 4713
    Helixi51 – 533
    Beta strandi57 – 593
    Turni79 – 813
    Helixi85 – 9410
    Turni95 – 973
    Beta strandi99 – 10911
    Beta strandi113 – 1153
    Helixi119 – 1213
    Helixi122 – 13211
    Beta strandi136 – 1405
    Helixi146 – 16217
    Beta strandi168 – 1714
    Helixi173 – 1764
    Turni181 – 1833
    Helixi186 – 1927
    Beta strandi194 – 1974
    Helixi206 – 21813
    Helixi220 – 2223
    Helixi224 – 2263
    Beta strandi231 – 2344
    Beta strandi242 – 2443
    Helixi247 – 25913
    Beta strandi264 – 2663
    Turni270 – 2723
    Helixi275 – 2817
    Helixi284 – 2907
    Beta strandi299 – 3035
    Beta strandi307 – 3148
    Beta strandi320 – 3267
    Beta strandi329 – 3313
    Beta strandi333 – 3386
    Helixi339 – 3424
    Beta strandi349 – 3546
    Turni355 – 3573
    Beta strandi360 – 3656
    Beta strandi368 – 3747
    Beta strandi379 – 3868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KTBX-ray1.90A1-405[»]
    1KTCX-ray2.40A1-405[»]
    ProteinModelPortaliQ90744.
    SMRiQ90744. Positions 1-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ90744.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni61 – 622Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 27 family.Curated

    Phylogenomic databases

    eggNOGiNOG68897.
    HOGENOMiHOG000161224.
    HOVERGENiHBG001989.
    InParanoidiQ90744.
    PhylomeDBiQ90744.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02065. Melibiase. 1 hit.
    [Graphical view]
    PRINTSiPR00740. GLHYDRLASE27.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q90744-1 [UniParc]FASTAAdd to Basket

    « Hide

    LENGLARTPP MGWLAWERFR CNVNCREDPR QCISEMLFME MADRIAEDGW    50
    RELGYKYINI DDCWAAKQRD AEGRLVPDPE RFPRGIKALA DYVHARGLKL 100
    DIYGDLGRLT CGGYPGTTLD RVEQDAQTFA EWGVDMLKLD GCYSSGKEQA 150
    QGYPQMARAL NSTGRPIVYS CSWPAYQGGL PPKVNYTLLG EICNLWRNYD 200
    DIQDSWDSVL SIVDWFFTNQ DVLQPFAGPG HWNDPDMLII GNFGLSYEQS 250
    RSQMALWTIM AAPLLMSTDL RTISPSAKKI LQNRLMIQIN QDPLGIQGRR 300
    IIKEGSHIEV FLRPLSQAAS ALVFFSRRTD MPFRYTTSLA KLGFPMGAAY 350
    EVQDVYSGKI ISGLKTGDNF TVIINPSGVV MWYLCPKALL IQQQAPGGPS 400
    RLPLL 405
    Length:405
    Mass (Da):45,615
    Last modified:November 1, 1996 - v1
    Checksum:iE1EC0061739C305C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18754 mRNA. Translation: AAA16614.1.
    PIRiS45522.
    UniGeneiGga.4369.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18754 mRNA. Translation: AAA16614.1 .
    PIRi S45522.
    UniGenei Gga.4369.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KTB X-ray 1.90 A 1-405 [» ]
    1KTC X-ray 2.40 A 1-405 [» ]
    ProteinModelPortali Q90744.
    SMRi Q90744. Positions 1-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000019396.

    Chemistry

    ChEMBLi CHEMBL5655.

    Protein family/group databases

    CAZyi GH27. Glycoside Hydrolase Family 27.

    Proteomic databases

    PaxDbi Q90744.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG68897.
    HOGENOMi HOG000161224.
    HOVERGENi HBG001989.
    InParanoidi Q90744.
    PhylomeDBi Q90744.

    Miscellaneous databases

    EvolutionaryTracei Q90744.
    PROi Q90744.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR013780. Glyco_hydro_13_b.
    IPR002241. Glyco_hydro_27.
    IPR000111. Glyco_hydro_GHD.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02065. Melibiase. 1 hit.
    [Graphical view ]
    PRINTSi PR00740. GLHYDRLASE27.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00512. ALPHA_GALACTOSIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence of a chicken alpha-N-acetylgalactosamindase gene."
      Davis M.O., Hata J., Smith D., Walker J.C.
      Biochim. Biophys. Acta 1216:296-298(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. "The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases."
      Garman S.C., Hannick L., Zhu A., Garboczi D.N.
      Structure 10:425-434(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH N-ACETYLGALACTOSAMINE, GLYCOSYLATION AT ASN-161; ASN-185 AND ASN-369, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiNAGAB_CHICK
    AccessioniPrimary (citable) accession number: Q90744
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3