NAGAB_BOVIN
ID NAGAB_BOVIN Reviewed; 411 AA.
AC Q58DH9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Alpha-galactosidase B;
DE Flags: Precursor;
GN Name=NAGA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from
CC glycolipids and glycopeptides. Required for the breakdown of
CC glycolipids. {ECO:0000250|UniProtKB:P17050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine
CC residues from human blood group A and AB mucin glycoproteins,
CC Forssman hapten and blood group A lacto series glycolipids.;
CC EC=3.2.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + H2O = a neolactoside IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:48212, ChEBI:CHEBI:15377, ChEBI:CHEBI:28471,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:40356;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48213;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:0) + H2O = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0)
CC + N-acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:49304,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:91118,
CC ChEBI:CHEBI:91119; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49305;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside IV3GalNAc-Gb4Cer + H2O = globoside Gb4Cer + N-
CC acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:48412,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:88167,
CC ChEBI:CHEBI:90400; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48413;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P17050}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P17050}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR EMBL; BT021618; AAX46465.1; -; mRNA.
DR RefSeq; NP_001039814.1; NM_001046349.1.
DR AlphaFoldDB; Q58DH9; -.
DR SMR; Q58DH9; -.
DR STRING; 9913.ENSBTAP00000012508; -.
DR ChEMBL; CHEMBL5079; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PaxDb; Q58DH9; -.
DR PRIDE; Q58DH9; -.
DR GeneID; 533357; -.
DR KEGG; bta:533357; -.
DR CTD; 4668; -.
DR eggNOG; KOG2366; Eukaryota.
DR InParanoid; Q58DH9; -.
DR OrthoDB; 964130at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; ISS:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR GO; GO:0019377; P:glycolipid catabolic process; ISS:UniProtKB.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035373; Melibiase/NAGA_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17450; Melibiase_2_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Lysosome; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..411
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000001017"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..80
FT /evidence="ECO:0000250"
FT DISULFID 42..49
FT /evidence="ECO:0000250"
FT DISULFID 127..158
FT /evidence="ECO:0000250"
FT DISULFID 187..209
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 46533 MW; 69039FB69B869144 CRC64;
MLLKTVLLLA LASQVLVLEN GLLRKPPMGW LAWERFRCNI DCSEDPKNCI SEQLFMEMAD
RLAQDGWRDL GYVYLNIDDC WIGGRDAKGN LVPDRKRFPH GIAFLADYAH SLGLKLGIYE
DLGNFTCMGY PGTTLDKVVQ DAQTFAEWKV DMLKLDGCYS TPQERAEGYP KMAAALNATG
RPIAFSCSWP AYEGGLPPKV NYTLLADICN LWRNFDDIQD SWRSVLSVLD WFVTHQDVLQ
PIAGPGHWND PDMLLIGNFG LSFEQAQAQM ALWTVLAAPL FMSTDLRTIS AQNMDILQNP
LMIKINQDPL GIQGRRILKE KSHIEVYLRP LASEASAIVF FSRRMDMPYH YHSSLARLNF
SSSVVYEAQD VYTGDIISGL QDKTNFTVII NPSGVVMWYL YPIRKLEIPQ Q
