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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 sitei154SubstrateBy similarity1
Active sitei156NucleophileBy similarity1
Binding sitei188SubstrateBy similarity1
Binding sitei213SubstrateBy similarity1
Active sitei217Proton donorBy similarity1
Binding sitei217SubstrateBy similarity1

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5079.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17By similarityAdd BLAST17
ChainiPRO_000000101718 – 411Alpha-N-acetylgalactosaminidaseAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi38 ↔ 80By similarity
Disulfide bondi42 ↔ 49By similarity
Glycosylationi124N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi127 ↔ 158By similarity
Glycosylationi177N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi187 ↔ 209By similarity
Glycosylationi201N-linked (GlcNAc...)Sequence analysis1
Modified residuei322PhosphoserineBy similarity1
Glycosylationi359N-linked (GlcNAc...)Sequence analysis1
Glycosylationi385N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ58DH9.
PRIDEiQ58DH9.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012508.

Structurei

3D structure databases

ProteinModelPortaliQ58DH9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni78 – 79Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ58DH9.
KOiK01204.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q58DH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLKTVLLLA LASQVLVLEN GLLRKPPMGW LAWERFRCNI DCSEDPKNCI
60 70 80 90 100
SEQLFMEMAD RLAQDGWRDL GYVYLNIDDC WIGGRDAKGN LVPDRKRFPH
110 120 130 140 150
GIAFLADYAH SLGLKLGIYE DLGNFTCMGY PGTTLDKVVQ DAQTFAEWKV
160 170 180 190 200
DMLKLDGCYS TPQERAEGYP KMAAALNATG RPIAFSCSWP AYEGGLPPKV
210 220 230 240 250
NYTLLADICN LWRNFDDIQD SWRSVLSVLD WFVTHQDVLQ PIAGPGHWND
260 270 280 290 300
PDMLLIGNFG LSFEQAQAQM ALWTVLAAPL FMSTDLRTIS AQNMDILQNP
310 320 330 340 350
LMIKINQDPL GIQGRRILKE KSHIEVYLRP LASEASAIVF FSRRMDMPYH
360 370 380 390 400
YHSSLARLNF SSSVVYEAQD VYTGDIISGL QDKTNFTVII NPSGVVMWYL
410
YPIRKLEIPQ Q
Length:411
Mass (Da):46,533
Last modified:April 26, 2005 - v1
Checksum:i69039FB69B869144
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021618 mRNA. Translation: AAX46465.1.
RefSeqiNP_001039814.1. NM_001046349.1.
UniGeneiBt.57867.

Genome annotation databases

GeneIDi533357.
KEGGibta:533357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021618 mRNA. Translation: AAX46465.1.
RefSeqiNP_001039814.1. NM_001046349.1.
UniGeneiBt.57867.

3D structure databases

ProteinModelPortaliQ58DH9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012508.

Chemistry databases

ChEMBLiCHEMBL5079.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Proteomic databases

PaxDbiQ58DH9.
PRIDEiQ58DH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi533357.
KEGGibta:533357.

Organism-specific databases

CTDi4668.

Phylogenomic databases

eggNOGiKOG2366. Eukaryota.
ENOG410XPF1. LUCA.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ58DH9.
KOiK01204.

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_BOVIN
AccessioniPrimary (citable) accession number: Q58DH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: April 26, 2005
Last modified: October 5, 2016
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.