NAGAB_CHICK
ID NAGAB_CHICK Reviewed; 405 AA.
AC Q90744;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Alpha-galactosidase B;
GN Name=NAGA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8241271; DOI=10.1016/0167-4781(93)90158-a;
RA Davis M.O., Hata J., Smith D., Walker J.C.;
RT "Cloning and sequence of a chicken alpha-N-acetylgalactosamindase gene.";
RL Biochim. Biophys. Acta 1216:296-298(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH
RP N-ACETYLGALACTOSAMINE, GLYCOSYLATION AT ASN-161; ASN-185 AND ASN-369,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=12005440; DOI=10.1016/s0969-2126(02)00726-8;
RA Garman S.C., Hannick L., Zhu A., Garboczi D.N.;
RT "The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of
RT glycosidase deficiency diseases.";
RL Structure 10:425-434(2002).
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:0000269|PubMed:12005440}.
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; L18754; AAA16614.1; -; mRNA.
DR PIR; S45522; S45522.
DR PDB; 1KTB; X-ray; 1.90 A; A=1-405.
DR PDB; 1KTC; X-ray; 2.40 A; A=1-405.
DR PDBsum; 1KTB; -.
DR PDBsum; 1KTC; -.
DR AlphaFoldDB; Q90744; -.
DR SMR; Q90744; -.
DR STRING; 9031.ENSGALP00000019396; -.
DR ChEMBL; CHEMBL5655; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR iPTMnet; Q90744; -.
DR PaxDb; Q90744; -.
DR VEuPathDB; HostDB:geneid_396547; -.
DR eggNOG; KOG2366; Eukaryota.
DR InParanoid; Q90744; -.
DR PhylomeDB; Q90744; -.
DR EvolutionaryTrace; Q90744; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Lipid metabolism; Lysosome; Reference proteome.
FT CHAIN 1..405
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000001021"
FT ACT_SITE 140
FT /note="Nucleophile"
FT ACT_SITE 201
FT /note="Proton donor"
FT BINDING 61..62
FT /ligand="substrate"
FT BINDING 138
FT /ligand="substrate"
FT BINDING 172
FT /ligand="substrate"
FT BINDING 197
FT /ligand="substrate"
FT BINDING 201
FT /ligand="substrate"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12005440"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12005440"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12005440"
FT DISULFID 21..63
FT /evidence="ECO:0000269|PubMed:12005440"
FT DISULFID 25..32
FT /evidence="ECO:0000269|PubMed:12005440"
FT DISULFID 111..142
FT /evidence="ECO:0000269|PubMed:12005440"
FT DISULFID 171..193
FT /evidence="ECO:0000269|PubMed:12005440"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1KTB"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1KTB"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:1KTB"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:1KTB"
SQ SEQUENCE 405 AA; 45615 MW; E1EC0061739C305C CRC64;
LENGLARTPP MGWLAWERFR CNVNCREDPR QCISEMLFME MADRIAEDGW RELGYKYINI
DDCWAAKQRD AEGRLVPDPE RFPRGIKALA DYVHARGLKL DIYGDLGRLT CGGYPGTTLD
RVEQDAQTFA EWGVDMLKLD GCYSSGKEQA QGYPQMARAL NSTGRPIVYS CSWPAYQGGL
PPKVNYTLLG EICNLWRNYD DIQDSWDSVL SIVDWFFTNQ DVLQPFAGPG HWNDPDMLII
GNFGLSYEQS RSQMALWTIM AAPLLMSTDL RTISPSAKKI LQNRLMIQIN QDPLGIQGRR
IIKEGSHIEV FLRPLSQAAS ALVFFSRRTD MPFRYTTSLA KLGFPMGAAY EVQDVYSGKI
ISGLKTGDNF TVIINPSGVV MWYLCPKALL IQQQAPGGPS RLPLL
