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Reviewed, UniProtKB/Swiss-Prot Q90744 (NAGAB_CHICK)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha-N-acetylgalactosaminidase
    EC=3.2.1.49
Alternative name(s):
    Alpha-galactosidase B
Gene names
Name: NAGA
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

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Ontologies

Keywords
   Cellular componentLysosome
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-N-acetylgalactosaminidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Alpha-N-acetylgalactosaminidase
PRO_0000001021

Sites

Active site1401Nucleophile By similarity
Active site2011Proton donor By similarity

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...)
Glycosylation1851N-linked (GlcNAc...)
Glycosylation3691N-linked (GlcNAc...)
Disulfide bond21 ↔ 63
Disulfide bond25 ↔ 32
Disulfide bond111 ↔ 142
Disulfide bond171 ↔ 193

Secondary structure

1 ................................................................................ 405
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q90744-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E1EC0061739C305C

FASTA40545,615
        10         20         30         40         50         60 
LENGLARTPP MGWLAWERFR CNVNCREDPR QCISEMLFME MADRIAEDGW RELGYKYINI 

        70         80         90        100        110        120 
DDCWAAKQRD AEGRLVPDPE RFPRGIKALA DYVHARGLKL DIYGDLGRLT CGGYPGTTLD 

       130        140        150        160        170        180 
RVEQDAQTFA EWGVDMLKLD GCYSSGKEQA QGYPQMARAL NSTGRPIVYS CSWPAYQGGL 

       190        200        210        220        230        240 
PPKVNYTLLG EICNLWRNYD DIQDSWDSVL SIVDWFFTNQ DVLQPFAGPG HWNDPDMLII 

       250        260        270        280        290        300 
GNFGLSYEQS RSQMALWTIM AAPLLMSTDL RTISPSAKKI LQNRLMIQIN QDPLGIQGRR 

       310        320        330        340        350        360 
IIKEGSHIEV FLRPLSQAAS ALVFFSRRTD MPFRYTTSLA KLGFPMGAAY EVQDVYSGKI 

       370        380        390        400 
ISGLKTGDNF TVIINPSGVV MWYLCPKALL IQQQAPGGPS RLPLL

« Hide

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References

[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: 8241271] [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: 12005440] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

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Cross-references

Sequence databases

L18754 mRNA. Translation: AAA16614.1.
IPIIPI00585886.
PIRS45522.
UniGeneGga.4369

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KTBX-ray1.90A1-405[»]
1KTCX-ray2.40A1-405[»]
ModBaseSearch...

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

Genome annotation databases

EnsemblENSGALG00000011900. Gallus gallus. [Contig view]

Phylogenomic databases

HOGENOMQ90744.
HOVERGENQ90744.

Enzyme and pathway databases

BRENDA3.2.1.49. 4.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
ProDomPD002572. Glyco_hydro_GHD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameNAGAB_CHICK
AccessionPrimary (citable) accession number: Q90744
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents