| IED ID | IndEnz0002014380 |
| Enzyme Type ID | protease014380 |
| Protein Name |
Arylsulfatase A ASA EC 3.1.6.8 Cerebroside-sulfatase Cleaved into: Arylsulfatase A component B; Arylsulfatase A component C |
| Gene Name | ARSA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA |
| Enzyme Length | 507 |
| Uniprot Accession Number | P15289 |
| Absorption | |
| Active Site | ACT_SITE 69; /note=Nucleophile; /evidence=ECO:0000269|PubMed:7628016; ACT_SITE 125; /evidence=ECO:0000269|PubMed:12888274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by phosphate. The phosphate forms a covalent bond with the active site 3-oxoalanine. {ECO:0000269|PubMed:12888274}. |
| Binding Site | BINDING 123; /note=Substrate; /evidence=ECO:0000269|PubMed:11124905; BINDING 150; /note=Substrate; /evidence=ECO:0000269|PubMed:11124905; BINDING 229; /note=Substrate; /evidence=ECO:0000269|PubMed:11124905; BINDING 302; /note=Substrate; /evidence=ECO:0000269|PubMed:11124905 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate; Xref=Rhea:RHEA:21300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:18390, ChEBI:CHEBI:75956; EC=3.1.6.8; Evidence={ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:24294900};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21301; Evidence={ECO:0000269|PubMed:24294900}; |
| DNA Binding | |
| EC Number | 3.1.6.8 |
| Enzyme Function | FUNCTION: Hydrolyzes cerebroside sulfate. {ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:24294900}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:24294900}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Beta strand (21); Binding site (4); Chain (3); Disulfide bond (6); Erroneous initiation (2); Glycosylation (3); Helix (21); Metal binding (5); Modified residue (1); Mutagenesis (3); Natural variant (108); Sequence conflict (1); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Direct protein sequencing;Disease variant;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Ichthyosis;Leukodystrophy;Lipid metabolism;Lysosome;Metachromatic leukodystrophy;Metal-binding;Reference proteome;Signal |
| Interact With | P50995; Q6P5X5; Q13554-3; O60826; Q96D98; Q9H0I2; Q12951-2; Q16512; P28069; O75360; Q9BQY4; Q15645; O95231 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:9342345}. Lysosome {ECO:0000305|PubMed:2562955}. |
| Modified Residue | MOD_RES 69; /note="3-oxoalanine (Cys)"; /evidence="ECO:0000269|PubMed:7628016, ECO:0000269|PubMed:9342345" |
| Post Translational Modification | PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD). {ECO:0000269|PubMed:7628016, ECO:0000269|PubMed:9342345}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:1352993 |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 1AUK; 1E1Z; 1E2S; 1E33; 1E3C; 1N2K; 1N2L; 2AIJ; 2AIK; 2HI8; |
| Mapped Pubmed ID | 11333871; 11777924; 11857580; 12459318; 12473917; 12757705; 12757706; 14563551; 15375602; 15657036; 15772092; 16110195; 16140556; 16311251; 16678723; 17329011; 17452787; 17560502; 17660863; 17845130; 18248830; 18624398; 18768108; 19021637; 19054018; 20711500; 21167507; 21454621; 21516116; 21648305; 21695197; 21966540; 21988832; 23192358; 23209833; 23247813; 23689179; 24001781; 24835590; 24989669; 25297594; 25416956; 26462614; 26577183; 27374302; 28799099; 30083785; 30362153; 30674982; 30834272; 31312839; 31694723; 31922587; 32431092; 32470555; 32617873; 32632536; 32792226; 33385934; 33498624; 8681943; 8692836; 9699462; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,588 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.099 mM for galactosyl-3-sulfate ceramide {ECO:0000269|PubMed:24294900}; Note=kcat is 0,087 sec(-1) with galactosyl-3-sulfate ceramide as substrate. {ECO:0000269|PubMed:24294900}; |
| Metal Binding | METAL 29; /note="Calcium"; /evidence="ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K"; METAL 30; /note="Calcium"; /evidence="ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K"; METAL 69; /note="Calcium; via 3-oxoalanine"; /evidence="ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K"; METAL 281; /note="Calcium"; /evidence="ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K"; METAL 282; /note="Calcium"; /evidence="ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K" |
| Rhea ID | RHEA:21300; RHEA:21301 |
| Cross Reference Brenda |