ID A0A093Q618_9PASS Unreviewed; 494 AA.
AC A0A093Q618;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=N-acetylgalactosamine-6-sulfatase {ECO:0000256|ARBA:ARBA00019527};
DE EC=3.1.6.4 {ECO:0000256|ARBA:ARBA00012117};
DE AltName: Full=Chondroitinsulfatase {ECO:0000256|ARBA:ARBA00033059};
DE AltName: Full=Galactose-6-sulfate sulfatase {ECO:0000256|ARBA:ARBA00030478};
DE AltName: Full=N-acetylgalactosamine-6-sulfate sulfatase {ECO:0000256|ARBA:ARBA00032952};
DE Flags: Fragment;
GN ORFNames=N305_04790 {ECO:0000313|EMBL:KFW84046.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW84046.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW84046.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW84046.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC galactosamine 6-sulfate units of chondroitin sulfate and of the D-
CC galactose 6-sulfate units of keratan sulfate.; EC=3.1.6.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000027};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR635626-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR635626-2};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779}.
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DR EMBL; KL672024; KFW84046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Q618; -.
DR STRING; 328815.ENSMVIP00005018760; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043890; F:N-acetylgalactosamine-6-sulfatase activity; IEA:UniProtKB-EC.
DR CDD; cd16157; GALNS; 1.
DR Gene3D; 3.30.1120.10; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035626; GALNS.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42693:SF50; N-ACETYLGALACTOSAMINE-6-SULFATASE; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR Pfam; PF14707; Sulfatase_C; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR635626-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR635626-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258}.
FT DOMAIN 12..326
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT ACT_SITE 50
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-1"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-2"
FT MOD_RES 50
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-4"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR635626-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW84046.1"
FT NON_TER 494
FT /evidence="ECO:0000313|EMBL:KFW84046.1"
SQ SEQUENCE 494 AA; 55315 MW; 8EB1AE101E1A6570 CRC64;
TLTSFGVLFL QMGWGDLGAF GEPSKETPNL DQMAAEGMLF LDFYTANPLC SPSRAALLTG
RLPVRNGFYT TNAHARNAYT PQDIVGGIQD SELLLPELLK KAGYINKIIG KWHLGHRPQF
HPLKHGFDEW FGSPNCHFGP YDNRELPNIP VYRDWEMIGR YYDDFKIDLK TGEANLTQLY
LQEALDFISK QQASQQPFFL YWAIDATHAP VYASKQFLGT SQRGLYGDAV REIDDSIGKI
LRHLQQLGIS ENTFVFFTSD NGAALISAPK QGGSNGPFLC GKQTTFEGGM REPAIAWWPG
HIPAGGVSHQ LGNVMDLFTT SLSLAGLQPP SDRQIDGIDL LPVMLQGKLI DRPIFYYRGN
EMMAVRVGLY KAHYWTWSNS WEEYGKGTDF CPGQSVSGVT THTQEEHTYL PLLFHLGRDP
GEKFPLSFAS EEYQRAMERI TGIVQQHKDT LIPGEPQLNV CDKAIMNWSP PGCEKLGKCL
KAPESDPKKC SWPH
//
