GlycosylTransferase Family 15

Known Activitiesglycolipid 2-α-mannosyltransferase (EC 2.4.1.131); GDP-Man: α-1,2-mannosyltransferase (EC 2.4.1.-).
Mechanism Retaining
3D Structure StatusGT-A
External resourcesInterPro; PFAM;
Statistics GenBank accession (282); Uniprot accession (75); PDB accession (3); 3D entries (1); cryst (0)
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 α-1,2-mannosyltransferase (Mnt1;Kre2) 2.4.1.131 Candida albicans CAA67930.1 C4YPV8
Q00310
 
 α-1,2-mannosyltransferase (Mnt2) 2.4.1.131 Candida albicans CAA61538.1 P46592  
 GDP-Man: α-1,2-mannosyltransferase (Kre2;Mnt1;YDR483w;D8035.26) 2.4.1.- Saccharomyces cerevisiae S288c AAA34784.1
AAB64906.1
CAA44516.1
CAA82879.1
CAH59517.1
NP_010771.1
P27809.1 1S4N[A,B]
1S4O[A,B]
1S4P[A,B]
 α-1,2-mannosyltransferase (Ktr1;YOR099w;YOR3189w) 2.4.1.131 Saccharomyces cerevisiae S288c CAA44713.1
CAA64021.1
CAA99296.1
NP_014742.1
P27810.1  
 mannosyltransferase (Ktr2;YKR061w) 2.4.1.131 Saccharomyces cerevisiae S288c AAA16119.1
CAA82140.1
NP_012987.1
P33550.1  
 mannosyltransferase (Yur1;YJL139c;J0657) 2.4.1.131 Saccharomyces cerevisiae S288c CAA41111.1
CAA60816.1
CAA89434.1
NP_012396.1
P26725.1  

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