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Q90744

- NAGAB_CHICK

UniProt

Q90744 - NAGAB_CHICK

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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. lysosome Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
LENGLARTPP MGWLAWERFR CNVNCREDPR QCISEMLFME MADRIAEDGW
60 70 80 90 100
RELGYKYINI DDCWAAKQRD AEGRLVPDPE RFPRGIKALA DYVHARGLKL
110 120 130 140 150
DIYGDLGRLT CGGYPGTTLD RVEQDAQTFA EWGVDMLKLD GCYSSGKEQA
160 170 180 190 200
QGYPQMARAL NSTGRPIVYS CSWPAYQGGL PPKVNYTLLG EICNLWRNYD
210 220 230 240 250
DIQDSWDSVL SIVDWFFTNQ DVLQPFAGPG HWNDPDMLII GNFGLSYEQS
260 270 280 290 300
RSQMALWTIM AAPLLMSTDL RTISPSAKKI LQNRLMIQIN QDPLGIQGRR
310 320 330 340 350
IIKEGSHIEV FLRPLSQAAS ALVFFSRRTD MPFRYTTSLA KLGFPMGAAY
360 370 380 390 400
EVQDVYSGKI ISGLKTGDNF TVIINPSGVV MWYLCPKALL IQQQAPGGPS

RLPLL
Length:405
Mass (Da):45,615
Last modified:November 1, 1996 - v1
Checksum:iE1EC0061739C305C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18754 mRNA. Translation: AAA16614.1.
PIRiS45522.
UniGeneiGga.4369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18754 mRNA. Translation: AAA16614.1 .
PIRi S45522.
UniGenei Gga.4369.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 85 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