GlycosylTransferase Family 39

Known ActivitiesDol-P-Man: protein α-mannosyltransferase (EC 2.4.1.109)
Mechanism Inverting
3D Structure StatusGT-C
NoteThese enzymes use dolichol-P-mannose (b-linked) as the sugar donor.
External resourcesCFG(O-linked); InterPro; PFAM;
Statistics GenBank accession (353); Uniprot accession (105);
All (237) Bacteria (114) Eukaryota (123) Characterized (23)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 protein O-mannosyltransferase (Pmt;cg1014) 2.4.1.109 Corynebacterium glutamicum ATCC 13032 ACC04358.1
BAB98283.1
CAF19596.1
NP_600117.1
   
 protein O-mannosyltransferase (Rv1002c) 2.4.1.109 Mycobacterium tuberculosis H37Rv CAB08157.1    
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 protein O-mannosyltransferase A (PmtA) 2.4.1.109 Aspergillus awamori AAK77607.1 Q96VV1  
 Dol-P-Man: protein O-mannosyltransferase 1 (Pmt1;AFUA_3G06450;Afu3g06450) 2.4.1.109 Aspergillus fumigatus Af293 EAL92923.1    
 protein mannosyltransferase (Pmt6) 2.4.1.109 Candida albicans AAF16867.1 Q9UVB5  
 Dolichyl-phosphate-mannose-protein mannosyltransferase 1 (Pmt1) 2.4.1.109 Candida albicans CAF3-1 AAC31119.1
BAE44795.1
O74189.1  
 protein O-mannosyltransferase (Pmt4) 2.4.1.109 Cryptococcus neoformans var. grubii ABG57096.1 A3E242  
 protein O-mannosyltransferase 2 (POMT2) 2.4.1.109 Homo sapiens AAF14118.1
AAF62558.1
AAF63184.1
AAH31651.1
AAM12046.1
BAD92351.1
CAB89256.1
CAD62348.1
CAE91890.1
CAH10531.1
NP_037514.2
Q9UKY4.2  
 protein O-mannosyl-transferase 1 (POMT1) 2.4.1.109 Homo sapiens AAD41245.1
AAD41246.1
AAH22877.2
AAH22877.3
AAH65268.1
BAA91135.1
BAA91190.1
BAC11269.1
BAD92667.1
BAG52022.1
BAG57011.1
BAG58392.1
BAG58462.1
BAG61567.1
BAG62126.1
BAG62223.1
BAG63000.1
BAG64337.1
CAF86083.1
CAF86827.1
CAI40219.1
CAI40220.1
CAI40221.1
CAI40222.1
CAI40223.1
CAI40224.1
CAI40225.1
CAI40226.1
CAI40227.1
NP_009102.2
Q9Y6A1.2  
 protein O-mannosyltransferase (Pomt1;Pmt1) 2.4.1.109 Hypocrea jecorina RUTC-30 AAP05785.1
AAR99494.1
Q870E9  
 protein O-mannosyltransferase 2 (POMT2) 2.4.1.109 Mus musculus AAH52045.1
AAH62965.1
AAK30026.1
AAL85627.1
AAM09080.1
AAM09081.1
AAM12047.1
AAM12048.1
BAC34458.1
NP_700464.1
Q8BGQ4.1  
 protein O-mannosyltransferase 2 (Pomt2) 2.4.1.109 Rattus norvegicus BAE97674.1 Q14U74  
 protein O-mannosyltransferase 1 (Pomt1) 2.4.1.109 Rattus norvegicus AAG53461.1
AAH70912.1
NP_445858.1
Q99PR0  
 Dol-P-Man: protein mannosyltransferase 6 (Pmt6;YGR199w;G7722) 2.4.1.109 Saccharomyces cerevisiae S288C CAA88992.1
CAA97226.1
NP_011715.1
P42934  
 Dol-P-Man: protein mannosyltransferase 2 (Pmt2;YAL023c;FUN25) 2.4.1.109 Saccharomyces cerevisiae S288C AAA70392.1
AAC04934.2
NP_009379.2
P31382.2  
 Dol-P-Man: protein mannosyltransferase 3 (Pmt3;YOR321w;O6148) 2.4.1.109 Saccharomyces cerevisiae S288C CAA58728.1
CAA62176.1
CAA99641.1
NP_014966.1
P47190  
 Dol-P-Man: protein mannosyltransferase 1 (Pmt1;YDL095W;D2390) 2.4.1.109 Saccharomyces cerevisiae S288C AAA02928.1
CAA02295.1
CAA64917.1
CAA98663.1
NP_010188.1
P33775.1  
 Dol-P-Man: protein mannosyltransferase 4 (Pmt4;YJR143c;J2176) 2.4.1.109 Saccharomyces cerevisiae S288C CAA58729.1
CAA89676.1
NP_012677.1
P46971  
 Dol-P-Man: protein mannosyltransferase 5 (Pmt5;YDL093w;D2399) 2.4.1.109 Saccharomyces cerevisiae S288C CAA63414.1
CAA64918.1
CAA98661.1
NP_010190.1
P52867.1  
 Dol-P-Man: protein mannosyltransferase 7 (Pmt7;D9740.4;YDR307w) 2.4.1.109 Saccharomyces cerevisiae S288C AAB64743.1
NP_010593.1
Q06644  
 protein O-mannosyltransferase (Ogm2;Oma2;SPAPB1E7.09) 2.4.1.109 Schizosaccharomyces pombe 972h- CAC36926.1
NP_594135.1
Q9C100  
 protein O-mannosyltransferase (Ogm4;Oma4;SPBC16C6.09) 2.4.1.109 Schizosaccharomyces pombe 972h- CAA16916.1
NP_596807.1
O42933.1  
 protein O-mannosyltransferase (Ogm1;Oma1;SPAC22A12.07C) 2.4.1.109 Schizosaccharomyces pombe 972h- CAB16577.1
NP_593237.1
O13898.1  

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.