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CATH domain | Related DB codes (homologues) |
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2.60.40.1180 : Immunoglobulin-like | M00113,T00307,D00165,D00176,D00664,D00665,D00864,M00112,M00193,M00314,T00057,T00062,T00067 | 3.20.20.70 : TIM Barrel | S00215,S00217,S00218,S00219,S00532,S00198,S00220,S00745,S00537,S00538,S00539,S00826,S00841,S00235,S00239,S00240,S00243,S00244,S00199,S00200,S00201,S00221,S00222,S00847,S00224,S00225,S00226,D00014,D00029,M00141,T00015,T00239,D00664,D00665,D00804,T00089 |
Enzyme Name | UniProtKB | KEGG |
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| Q02402 |
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Protein name |
| Alpha-galactosidaseMelibiaseAlpha-D-galactosidaseAlpha-galactosidase AAlpha-galactoside galactohydrolase |
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Synonyms | Alpha-galactosidase |
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Pfam | PF02065 (Melibiase) [Graphical view]
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CAZy | GH27 (Glycoside Hydrolase Family)
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KEGG pathways | MAP code | Pathways |
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MAP00052 | Galactose metabolism | MAP00561 | Glycerolipid metabolism | MAP00600 | Sphingolipid metabolism | MAP00603 | Glycosphingolipid biosynthesis - globoseries |
UniProtKB:Accession Number | Q02402 |
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Entry name | Q02402_9FUNG |
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Activity |
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Subunit |
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Subcellular location |
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Cofactor |
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Active-site residues | resource |
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Literature [3], [4], [5], [6], [7], [8], [9] & Swiss-prot;P06280, Q9FXT4 | pdb | Catalytic residues |
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| | | | | | | | |
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3a5vA01 |  |  |  |  |  |  |  | ASP 51;TYR 93;ASP 129;ARG 185;ASP 189
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3a5vA02 |  |  |  |  |  |  |  |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[3] | Figure 4 |
| [6] | p.417-419 |
| [9] | FIGURE 1 |
| [10] | Fig.2, Fig.3, p.3627-3630 |
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references | [1] |
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PubMed ID | 10933800 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 9826-36 |
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Authors | Hart DO, He S, Chany CJ 2nd, Withers SG, Sims PF, Sinnott ML, Brumer H 3rd |
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Title | Identification of Asp-130 as the catalytic nucleophile in the main alpha-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase. |
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[2] |
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PubMed ID | 11128583 |
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Journal | Carbohydr Res |
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Year | 2000 |
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Volume | 329 |
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Pages | 539-47 |
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Authors | Ly HD, Howard S, Shum K, He S, Zhu A, Withers SG |
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Title | The synthesis, testing and use of 5-fluoro-alpha-D-galactosyl fluoride to trap an intermediate on green coffee bean alpha-galactosidase and identify the catalytic nucleophile. |
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[3] |
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PubMed ID | 12005440 |
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Journal | Structure |
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Year | 2002 |
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Volume | 10 |
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Pages | 425-34 |
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Authors | Garman SC, Hannick L, Zhu A, Garboczi DN |
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Title | The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 56-417 IN COMPLEX WITH D-GALACTOSE. |
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PubMed ID | 12657636 |
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Journal | J Biol Chem |
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Year | 2003 |
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Volume | 278 |
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Pages | 20313-8 |
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Authors | Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H |
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Title | Crystal structure of rice alpha-galactosidase complexed with D-galactose. |
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Related PDB | 1uas |
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Related UniProtKB | Q9FXT4 |
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[5] |
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Comments | X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, HOMODIMERIZATION, GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215. |
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PubMed ID | 15003450 |
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Journal | J Mol Biol |
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Year | 2004 |
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Volume | 337 |
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Pages | 319-35 |
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Authors | Garman SC, Garboczi DN |
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Title | The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. |
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Related PDB | 1r46,1r47 |
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Related UniProtKB | P06280 |
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[6] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 28-441. |
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PubMed ID | 15136043 |
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Journal | J Mol Biol |
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Year | 2004 |
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Volume | 339 |
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Pages | 413-22 |
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Authors | Golubev AM, Nagem RA, Brandao Neto JR, Neustroev KN, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Savel'ev AN, Polikarpov I |
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Title | Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism. |
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Related PDB | 1szn,1t0o |
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Related UniProtKB | Q92456 |
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[7] |
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Journal | Biocatal Biotransformation |
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Year | 2009 |
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Volume | 27 |
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Pages | 79-89 |
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Authors | Weignerova' L, Simerska' P, Kr(en V |
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Title | ¿-Galactosidases and their applications in biotransformations. |
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[8] |
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PubMed ID | 19374450 |
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Journal | Biochemistry |
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Year | 2009 |
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Volume | 48 |
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Pages | 4816-27 |
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Authors | Lieberman RL, D'aquino JA, Ringe D, Petsko GA |
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Title | Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability. |
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Related PDB | 3gxn,3gxp,3gxt |
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Related UniProtKB | P06280 |
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[9] |
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PubMed ID | 19809163 |
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Journal | Biosci Biotechnol Biochem |
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Year | 2009 |
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Volume | 73 |
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Pages | 2360-4 |
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Authors | Fujimoto Z, Kaneko S, Kim WD, Park GG, Momma M, Kobayashi H |
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Title | The tetramer structure of the glycoside hydrolase family 27 alpha-galactosidase I from Umbelopsis vinacea. |
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Related PDB | 3a5v |
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[10] |
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PubMed ID | 19940122 |
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Journal | J Biol Chem |
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Year | 2010 |
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Volume | 285 |
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Pages | 3625-32 |
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Authors | Guce AI, Clark NE, Salgado EN, Ivanen DR, Kulminskaya AA, Brumer H 3rd, Garman SC |
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Title | Catalytic mechanism of human alpha-galactosidase. |
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Related PDB | 3hg2,3hg3,3hg4,3hg5 |
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Related UniProtKB | P06280 |
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comments | This enzyme belongs to glycosidase family-27, with a retaining mechanism. Alpha-galactosidases can be classified into glycosidase family-4, 27, 36, 57, 97 and 110 (see [9]). Alpha-galactosidases from eukaryotes are generally classified into glycosidase family-27, whereas prokaryotic alpha-galactosidases are mostly classified into glycosidase family-36 (see [9]). This enzyme is homologous to Alpha-N-acetylgalactosaminidase (EC 3.2.1.49; D00665 in EzCatDB) and a counterpart enzyme from other organisms (EC 3.2.1.22; D00664), which shows different substrate specificities from this enzyme. This enzyme is specific only for galactomannan, whereas the counterpart enzyme is also active toward other alpha-galactosides (see [9]). However, considering the conservation of the active-site structure, this enzyme must catalyze the same reaction type as these homologous enzymes. Asp129 acts as a nucleophile, whereas Asp189 acts as catalytic acid-base.
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created | updated |
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2010-03-05 | 2012-02-01 |
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