EzCatDB: D00859
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DB codeD00859
CATH domainDomain 1-.-.-.-
Domain 23.90.550.10 : Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain ACatalytic domain
E.C.2.4.1.-

CATH domainRelated DB codes (homologues)
3.90.550.10 : Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain AS00709,S00465,S00466,D00417,D00860,T00415

Enzyme Name
UniProtKBKEGG

P27809
Protein nameGlycolipid 2-alpha-mannosyltransferaseGlycolipid 2-alpha-mannosyltransferase
Guanosine diphosphomannose-oligosaccharide-lipid mannosyltransferase
GDP-mannose-oligosaccharide-lipid mannosyltransferase
Oligosaccharide-lipid mannosyltransferase
GDP-mannose:glycolipid 1,2-alpha-D-mannosyltransferase
SynonymsEC 2.4.1.-
Alpha-1,2-mannosyltransferase
RefSeqNP_010771.1 (Protein)
NM_001180791.1 (DNA/RNA sequence)
PfamPF01793 (Glyco_transf_15)
[Graphical view]
CAZyGT15 (Glycosyltransferase Family)


UniProtKB:Accession NumberP27809
Entry nameKRE2_YEAST
ActivityTransfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-1,2-D-mannosyl-D-mannose linkage.
Subunit
Subcellular locationGolgi apparatus membrane, Single-pass type II membrane protein.
CofactorManganese.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00034C00096L00058L00060C00035L00059L00061
CompoundManganeseGDP-mannoseMan2-Ser/Thr O-glycan(Man)n+9(GlcNAc)2-ASN N-glycanGDPMan3-Ser/Thr O-glycan(Man)2n+9(GlcNAc)2-ASN N-glycan
Typeheavy metalamide group,amine group,carbohydrate,nucleotidepeptide/protein,polysaccharideamide group,peptide/protein,polysaccharideamide group,amine group,nucleotidepeptide/protein,polysaccharideamide group,peptide/protein,polysaccharide
ChEBI18291
35154
15820


17552


PubChem23930
18396


8977


               
1s4nA00UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1s4nB00UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1s4oA00Bound:_MNUnboundUnboundUnboundBound:GDPUnboundUnbound
1s4oB00Bound:_MNUnboundUnboundUnboundBound:GDPUnboundUnbound
1s4pA00Bound:_MNUnboundAnalogue:MMAUnboundBound:GDPUnboundUnbound
1s4pB00Bound:_MNUnboundAnalogue:MMAUnboundBound:GDPUnboundUnbound

Active-site residues
resource
Literature [3]
pdbCatalytic residuesCofactor-binding residues
          
1s4nA00TYR 220
GLU 247;HIS 388(Manganese binding)
1s4nB00TYR 220
GLU 247;HIS 388(Manganese binding)
1s4oA00TYR 220
GLU 247;HIS 388(Manganese binding)
1s4oB00TYR 220
GLU 247;HIS 388(Manganese binding)
1s4pA00TYR 220
GLU 247;HIS 388(Manganese binding)
1s4pB00TYR 220
GLU 247;HIS 388(Manganese binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.5
[4]p.59-60
[5]Fig.10

references
[1]
PubMed ID9182588
JournalJ Biol Chem
Year1997
Volume272
Pages15527-31
AuthorsLussier M, Sdicu AM, Bussereau F, Jacquet M, Bussey H
TitleThe Ktr1p, Ktr3p, and Kre2p/Mnt1p mannosyltransferases participate in the elaboration of yeast O- and N-linked carbohydrate chains.
[2]
PubMed ID9878809
JournalBiochim Biophys Acta
Year1999
Volume1426
Pages323-34
AuthorsLussier M, Sdicu AM, Bussey H
TitleThe KTR and MNN1 mannosyltransferase families of Saccharomyces cerevisiae.
[3]
PubMed ID14752117
JournalJ Biol Chem
Year2004
Volume279
Pages17921-31
AuthorsLobsanov YD, Romero PA, Sleno B, Yu B, Yip P, Herscovics A, Howell PL
TitleStructure of Kre2p/Mnt1p: a yeast alpha1,2-mannosyltransferase involved in mannoprotein biosynthesis.
Related PDB1s4n,1s4o,1s4p
Related UniProtKBP27809
[4]
PubMed ID15653326
JournalTrends Biochem Sci
Year2005
Volume30
Pages53-62
AuthorsQasba PK, Ramakrishnan B, Boeggeman E
TitleSubstrate-induced conformational changes in glycosyltransferases.
[5]
PubMed ID18518825
JournalAnnu Rev Biochem
Year2008
Volume77
Pages521-55
AuthorsLairson LL, Henrissat B, Davies GJ, Withers SG
TitleGlycosyltransferases: structures, functions, and mechanisms.

comments
Previously, this enzyme was categorized in EC 2.4.1.131, but transferred to EC 2.4.1.-.
This enzyme belongs to glycosyltransferase family-15 (GT15 family), with a GT-A fold and a retaining mechanism (see [5]).
The structure of the N-terminal domain, which contains the N-terminal cytoplasmic region and a membrane-bound region, has not been determined yet.
According to the literature [3], [4] and [5], two possible reaction mechanisms have been proposed for this enzyme: A double displacement mechanism and a substitution nucleophilic internal (SNi)-like mechanism. To date, it has not been elucidated which mechanism is more appropriate.
In the double displacement mechanism, GDP-mannose is first transferred to a nucleophilic residue, Tyr220 in this enzyme, with an inversion of the configuration at C1 atom, and is then transferred to the acceptor mannose with the C1 atom reverting to its original configuration.
In the SNi-like mechanism, an oxocarbenium ion-like transition state/intermediate is formed from GDP-mannose, and the mannose group is attached on the same side by the acceptor mannose.

createdupdated
2010-08-182011-10-04


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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