Sequence of WBDD_ECOLX
EC Number:2.1.1.294
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase
J7I4B7
Escherichia coli
708
81732
Reaction
S-adenosyl-L-methionine + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = S-adenosyl-L-homocysteine + 3-O-methylphospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other sequences found for EC No. 2.1.1.294
EC Number:2.7.1.181
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
J7I4B7
Escherichia coli
708
81732
Reaction
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other sequences found for EC No. 2.7.1.181
General information:
Sequence
0 MTKDLNTLVS ELPEIYQTIF GHPEWDGDAA RDCNQRLDLI TEQYDNLSRA LGRPLNVLDL
60 GCAQGFFSLS LASKGATIVG IDFQQENINV CRALAEENPD FAAEFRVGRI EEVIAALEEG
120 EFDLAIGLSV FHHIVHLHGI DEVKRLLSRL ADVTQAVILE LAVKEEPFYW GVSQPDDPRE
180 LIEQCAFYRL IGEFDTHLSP VPRPMYLVSN HRVLINDFNQ PFQHWQNQPY AGAGLAHKRS
240 RRYFFGEDYV CKFFYYDMPH GILTAEESQR NKYELHNEIK FLTQPPAGFD APAVLAHGEN
300 AQSGWLVMEK LPGRLLSDML AAGEEIDREK ILGSLLRSLA ALEKQGFWHD DVRPWNVMVD
360 ARQHARLIDF GSIVTTPQDC SWPTNLVQSF FVFVNELFAE NKSWNGFWRS APVHPFNLPQ
420 PWSNWLYAVW QEPVERWNFV LLLALFEKKA KLPSAEQQRG ATEQWIIAQE TVLLELQSRV
480 RNESAGSEAL RGQIHTLEQQ MAQLQSAQDA FVEKAQQQVE VSHELTWLGE NMEQLAALLQ
540 TAQAHAQADV QPELPPETAE LLQRLEAANR EIHHLSNENQ QLRQEIEKIH RSRSWRMTKG
600 YRYLGLQIHL LRQYGFVQRC KHFIKRVLRF VFSFMRKHPQ VKHTAVNGLH KLGLYQPAYR
660 LYRRMNPLPH SQYQADAQIL SQTELQVMHP ELLPPEVYEI YLKLTKNK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
250469
Clarke B.R.,Cuthbertson L.,Whitfield C.
Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter.
J. Biol. Chem.
279
35709-35718
2004
250470
Clarke B.R.,Greenfield L.K.,Bouwman C.,Whitfield C.
Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway.
J. Biol. Chem.
284
30662-30672
2009
250471
Clarke B.R.,Richards M.R.,Greenfield L.K.,Hou D.,Lowary T.L.,Whitfield C.
In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan.
J. Biol. Chem.
286
41391-41401
2011
250472
Hagelueken G.,Huang H.,Harlos K.,Clarke B.R.,Whitfield C.,Naismith J.H.
Crystallization, dehydration and experimental phasing of WbdD, a bifunctional kinase and methyltransferase from Escherichia coli O9a.
Acta Crystallogr. D
68
1371-1379
2012
250473
Hagelueken G.,Huang H.,Clarke B.R.,Lebl T.,Whitfield C.,Naismith J.H.
Structure of WbdD: a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a.
Mol. Microbiol.
86
730-742
2012
