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Q90744 (NAGAB_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subunit structure

Homodimer. Ref.2

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Ontologies

Keywords
   Cellular componentLysosome
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Alpha-N-acetylgalactosaminidase
PRO_0000001021

Regions

Region61 – 622Substrate binding

Sites

Active site1401Nucleophile
Active site2011Proton donor
Binding site1381Substrate
Binding site1721Substrate
Binding site1971Substrate
Binding site2011Substrate

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Ref.2
Glycosylation1851N-linked (GlcNAc...) Ref.2
Glycosylation3691N-linked (GlcNAc...) Ref.2
Disulfide bond21 ↔ 63 Ref.2
Disulfide bond25 ↔ 32 Ref.2
Disulfide bond111 ↔ 142 Ref.2
Disulfide bond171 ↔ 193 Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q90744 [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

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) IN COMPLEX WITH N-ACETYLGALACTOSAMINE, GLYCOSYLATION AT ASN-161; ASN-185 AND ASN-369, SUBUNIT, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L18754 mRNA. Translation: AAA16614.1.
IPIIPI00585886.
PIRS45522.
UniGeneGga.4369.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTBX-ray1.90A1-405[»]
1KTCX-ray2.40A1-405[»]
ProteinModelPortalQ90744.
SMRQ90744. Positions 1-388.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ90744.

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGveNOG11773.
GeneTreeENSGT00390000008751.
HOGENOMHBG424315.
HOVERGENHBG001989.
InParanoidQ90744.
OrthoDBEOG4S1T77.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[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.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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: October 19, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

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