| Activities in Family | α-L-fucosidase (EC 3.2.1.51); α-1,2-L-fucosidase (EC 3.2.1.63); α-L-galactosidase (EC 3.2.1.-) |
|---|---|
| Mechanism | Inverting |
| 3D Structure Status | ( α / α ) 6 |
| Catalytic Nucleophile/Base | Asn activated by Asp |
| Catalytic Proton Donor | Glu |
| Note | Created based on a paper by Katayama, Sakuma, Kimura, Makimura, Hiratake, Sakata, Yamanoi, Kumagai, and Yamamoto (J. Bacteriol. 2004 Aug;186(15):4885-4893) |
| External resources | CAZypedia; |
| Commercial Enzyme Provider(s) | MEGAZYME; |
| Statistics | GenBank accession (2003); Uniprot accession (226); PDB accession (6); 3D entries (3); cryst (0) |
| Bacteria | ||||||
| Protein Name | EC# | Organism | GenBank | Uniprot | PDB/3D | |
| α-L-galactosidase (BACOVA_03438) | 3.2.1.- | Bacteroides ovatus ATCC 8483 | EDO10805.1 | 4UFC[A,B] | ||
| α-L-galactosidase (cleaves L-Galp-α-1,2-D-GlcpA; BT1010) | 3.2.1.- | Bacteroides thetaiotaomicron VPI-5482 | AAO76117.1 NP_809923.1 |
Q8A907 | ||
| α-1,2-L-fucosidase (AfcA;AfuA;BbAfcA) | 3.2.1.63 | Bifidobacterium bifidum JCM 1254 | AAQ72464.1 | 2EAB[A,B] 2EAC[A,B] 2EAD[A,B] 2EAE[A] |
||
| α-1,2-L-fucosidase (Blon_2335) | 3.2.1.63 | Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088 | ACJ53393.1 | B7GNN7 | ||
| α-L-fucosidase 95A (CjAfc95A;CJA_2710) (Afc95A) | 3.2.1.63 | Cellvibrio japonicus Ueda107 | ACE83895.1 | B3PBE3 | ||
| α-1,2-L-fucosidase (Afc3;CPF_2129) | 3.2.1.63 | Clostridium perfringens ATCC 13124 | ABG82552.1 | Q0TP83 | ||
| Eukaryota | ||||||
| Protein Name | EC# | Organism | GenBank | Uniprot | PDB/3D | |
| α-1,2-L-fucosidase (Axy8;AXY8;At4g34260) (Fuc95A) | 3.2.1.63 | Arabidopsis thaliana | CAB36703.1 AAM78086.1 AAO11638.1 AEE86349.1 CAB80143.1 NP_195152.2 |
Q8L7W8 | ||
| α-1,2-L-fucosidase (AN8149.2) | 3.2.1.63 | Aspergillus nidulans FGSC A4 | EAA59171.1 ABF50892.1 |
C8V6V7 Q5AU81 |
||
| α-1,2-L-fucosidase (EBM II;LlFuc) | 3.2.1.63 | Lilium longiflorum | BAF85832.1 | A8J657 | ||
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