Glycoside Hydrolase Family 39

Known Activitiesα-L-iduronidase (EC 3.2.1.76); β-xylosidase (EC 3.2.1.37).
Mechanism Retaining
ClanGH-A
3D Structure Status( β / α ) 8
Catalytic Nucleophile/BaseGlu (experimental)
Catalytic Proton DonorGlu (experimental)
External resourcesCAZypedia; InterPro; PFAM; PRINTS; PROSITE;
Commercial Enzyme Provider(s)PROZOMIX;
Statistics GenBank accession (391); Uniprot accession (252); PDB accession (5); 3D entries (3); cryst (1)
All (344) Archaea (3) Bacteria (324) Eukaryota (17) Structure (3 - 1 cryst) Characterized (12)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 β-1,4-xylosidase (XysA) 3.2.1.37 Aeromonas caviae ME-1 BAA95685.1 Q9LBF2  
 β-xylosidase (XylBH39;Bxyl;BH1068) 3.2.1.37 Bacillus halodurans C-125 BAB04787.1
NP_241934.1
Q9KDZ3  
 β-xylosidase B (XynB;Orf5) 3.2.1.37 Caldicellulosiruptor saccharolyticus AAA23063.1
AAB87376.1
P23552.1  
 β-xylosidase D (XynD) 3.2.1.37 Caldicellulosiruptor saccharolyticus AAB87373.1 O30428  
 β-xylosidase (XynD;Csac_2409) 3.2.1.37 Caldicellulosiruptor saccharolyticus DSM 8903 ABP67986.1
ABP67986.2
A4XM51  
 β-xylosidase A (BxlA) (Bxl39A) 3.2.1.37 Clostridium stercorarium NCIMB 11745 CAD48308.1 Q8GJ43  
 β-xylosidase (XynB;XynB1) 3.2.1.37 Geobacillus stearothermophilus T-6 NCIMB 40222 AAC98129.1
ABI49941.1
Q9ZFM2 1W91[A,B,C,D,E,F,G,H]
2BFG[A,B,C,D,E,F,G,H]
2BS9[A,B,C,D,E,F,G,H]
 β-xylosidase (XynB) 3.2.1.37 Thermoanaerobacterium saccharolyticum B6A-RI AAA27369.1 P36906.1 1PX8[A,B]
1UHV[A,B,C,D]
 β-xylosidase (XylB) 3.2.1.37 Thermoanaerobacterium sp. 'JW/SL YS485' AAB68820.1 O30360.1  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 α-L-iduronidase (IduA) 3.2.1.76 Canis lupus familiaris AAA51455.1 Q01634  
 α-L-iduronidase (IduA) 3.2.1.76 Homo sapiens AAA51698.1
AAA81589.1
AAE53576.1
AAE72581.1
AAH29959.1
AAN25812.1
AAQ32908.1
AAQ46779.1
AAT18792.1
AAY01759.1
ABH73761.1
ABL21590.1
ACG93377.1
ACH14961.1
ACK10791.1
BAD92138.1
BAF84505.1
BAG54168.1
NP_000194.1
XP_042678.2
P35475.2 cryst
 α-L-iduronidase (IduA) 3.2.1.76 Mus musculus AAC42044.1
AAH57935.1
BAC27393.1
BAC32313.1
BAE33353.1
BAE41504.1
NP_032351.1
P48441
Q8BLF6
Q8BMG0
 

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.





Last update: 2012-01-31 © Copyright 1998-2012
AFMB - CNRS - Universités Aix-Marseille I & II