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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei138Substrate1
Active sitei140Nucleophile1
Binding sitei172Substrate1
Binding sitei197Substrate1
Active sitei201Proton donor1
Binding sitei201Substrate1

GO - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000010211 – 405Alpha-N-acetylgalactosaminidaseAdd BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi21 ↔ 631 Publication
Disulfide bondi25 ↔ 321 Publication
Disulfide bondi111 ↔ 1421 Publication
Glycosylationi161N-linked (GlcNAc...)1 Publication1
Disulfide bondi171 ↔ 1931 Publication
Glycosylationi185N-linked (GlcNAc...)1 Publication1
Glycosylationi369N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ90744.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9031.ENSGALP00000019396.

Structurei

Secondary structure

1405
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Helixi16 – 19Combined sources4
Turni25 – 27Combined sources3
Turni29 – 31Combined sources3
Beta strandi32 – 34Combined sources3
Helixi35 – 47Combined sources13
Helixi51 – 53Combined sources3
Beta strandi57 – 59Combined sources3
Turni79 – 81Combined sources3
Helixi85 – 94Combined sources10
Turni95 – 97Combined sources3
Beta strandi99 – 109Combined sources11
Beta strandi113 – 115Combined sources3
Helixi119 – 121Combined sources3
Helixi122 – 132Combined sources11
Beta strandi136 – 140Combined sources5
Helixi146 – 162Combined sources17
Beta strandi168 – 171Combined sources4
Helixi173 – 176Combined sources4
Turni181 – 183Combined sources3
Helixi186 – 192Combined sources7
Beta strandi194 – 197Combined sources4
Helixi206 – 218Combined sources13
Helixi220 – 222Combined sources3
Helixi224 – 226Combined sources3
Beta strandi231 – 234Combined sources4
Beta strandi242 – 244Combined sources3
Helixi247 – 259Combined sources13
Beta strandi264 – 266Combined sources3
Turni270 – 272Combined sources3
Helixi275 – 281Combined sources7
Helixi284 – 290Combined sources7
Beta strandi299 – 303Combined sources5
Beta strandi307 – 314Combined sources8
Beta strandi320 – 326Combined sources7
Beta strandi329 – 331Combined sources3
Beta strandi333 – 338Combined sources6
Helixi339 – 342Combined sources4
Beta strandi349 – 354Combined sources6
Turni355 – 357Combined sources3
Beta strandi360 – 365Combined sources6
Beta strandi368 – 374Combined sources7
Beta strandi379 – 386Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KTBX-ray1.90A1-405[»]
1KTCX-ray2.40A1-405[»]
ProteinModelPortaliQ90744.
SMRiQ90744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ90744.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni61 – 62Substrate binding2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ90744.
PhylomeDBiQ90744.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_27/36_CS.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 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.
PIRiS45522.
UniGeneiGga.4369.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KTBX-ray1.90A1-405[»]
1KTCX-ray2.40A1-405[»]
ProteinModelPortaliQ90744.
SMRiQ90744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000019396.

Chemistry databases

ChEMBLiCHEMBL5655.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Proteomic databases

PaxDbiQ90744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ90744.
PhylomeDBiQ90744.

Miscellaneous databases

EvolutionaryTraceiQ90744.

Family and domain databases

CDDicd14792. GH27. 1 hit.
Gene3Di2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_27/36_CS.
IPR013780. Glyco_hydro_b.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF16499. Melibiase_2. 1 hit.
[Graphical view]
PRINTSiPR00740. GLHYDRLASE27.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 96 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.