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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541SubstrateBy similarity
Active sitei156 – 1561NucleophileBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei213 – 2131SubstrateBy similarity
Active sitei217 – 2171Proton donorBy similarity
Binding sitei217 – 2171SubstrateBy similarity

GO - Molecular functioni

  1. alpha-N-acetylgalactosaminidase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB
  2. glycolipid catabolic process Source: UniProtKB
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
ProteomesiUP000009136: Unplaced

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717By similarityAdd
BLAST
Chaini18 – 411394Alpha-N-acetylgalactosaminidasePRO_0000001017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 80By similarity
Disulfide bondi42 ↔ 49By similarity
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi127 ↔ 158By similarity
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi187 ↔ 209By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Modified residuei322 – 3221PhosphoserineBy similarity
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi385 – 3851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiQ58DH9.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ58DH9.
SMRiQ58DH9. Positions 18-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 792Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 27 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG68897.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ58DH9.
KOiK01204.

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.

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.
SMRiQ58DH9. Positions 18-402.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL5079.

Protein family/group databases

CAZyiGH27. Glycoside Hydrolase Family 27.

Proteomic databases

PRIDEiQ58DH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi533357.
KEGGibta:533357.

Organism-specific databases

CTDi4668.

Phylogenomic databases

eggNOGiNOG68897.
HOGENOMiHOG000161224.
HOVERGENiHBG001989.
InParanoidiQ58DH9.
KOiK01204.

Miscellaneous databases

NextBioi20876014.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

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: March 4, 2015
This is version 68 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

External Data

Dasty 3

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 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.