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Information on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase
for references in articles please use BRENDA:EC1.1.1.336
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.336 UDP-N-acetyl-D-mannosamine dehydrogenase
IUBMB Comments
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.1.1.336
-
2-epimerase
- polysaccharide
-
pyrococcus
-
enterobacterial
- transposon
- udp-n-acetylglucosamine
-
uridylyltransferase
- horikoshii
- diagnostics
Reaction Schemes
showSynonyms
udp-n-acetyl-d-mannosamine dehydrogenase, mmp0706, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UDP-D-ManNAcDH
UDP-ManNAc 6-dehydrogenase
-
-
-
-
wbpA2
wbpA_2
wecC
wecC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
UDP-N-acetyl-alpha-D-mannosaminouronate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-mannosamine:NAD+ 6-oxidoreductase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
Substrates: enzyme is strictly specific for UDP-N-acetyl-mannosamine and NAD +
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
Substrates: -
Products: ratio of 1.95 NAD molecules consumed per UDP-N-acetyl-alpha-D-mannosaminuronate molecule produced, 4-electron oxidation
Products: ratio of 1.95 NAD molecules consumed per UDP-N-acetyl-alpha-D-mannosaminuronate molecule produced, 4-electron oxidation
?
additional information
?
-
Substrates: no substrate: UDP-glucose or N-acetyl-D-mannosamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: UDP-glucose or N-acetyl-D-mannosamine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
salts or divalent cations are not required
additional information
-
salts or divalent cations are not required
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-acetylglucosamine 1-phosphate
-
activation at low UDP-N-acetylmannosamine concentrations
tris-(2-carboxyethyl)phosphine hydrochloride
1 mM, about 25% increase in activity
additional information
-
the presence of SH compounds is required for activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
UDP-N-acetyl-alpha-D-mannosamine
-
pH 10.0, 37°C, presence of 150 mM KCl
0.22
UDP-N-acetyl-alpha-D-mannosamine
-
pH 10.0, 37°C, presence of 1 mM N-acetylglucosamine 1-phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
22 strains of Edwardsiella tarda, including 10 human isolates and 12 diseased fish isolates
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
pathogen cell culture in human Caco-2 cell monolyers
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
Edwardsiella tarda strains can be grouped into two types of human isolates and diseased fish isolates based on distribution of the wecC gene, type III and type VI secretion system genes, the groups are broadly clustered into two major subpopulations: EdwGI and EdwGII. Edwardsiella tarda EdwGI is composed of strains mainly isolated from fish, such as the turbot, striped bass, and Japanese eel, represents a genotype of fish pathogens, and possesses virulence-associated gene clusters such as T3SS and T6SS. Edwardsiella tarda EdwGII contains strains isolated from human feces, nonpathogenic strains to fish, and environmental strains, and lacks some important virulence-associated gene clusters including T3SS and T6SS
malfunction
-
motility activity, including swarming and swimming, of the wecC mutant is weaker than that f the wild-type strain
metabolism
physiological function
metabolism
-
the enzyme is important for the synthesis of amino sugars and uronic acid and involved in the biosynthesis pathway for the production of polysaccharide bioflocculant, overview
metabolism
-
the enzyme is important for the synthesis of amino sugars and uronic acid and involved in the biosynthesis pathway for the production of polysaccharide bioflocculant, overview
-
physiological function
gene wecC is important for survival of Yersinia pestis in murine macrophages
physiological function
specific knockout mutation in the UDP-D-Nacetylmannosamine dehydrogenase gene, wbpA, results in strains that no longer produce B-band lipopolysaccharide
physiological function
-
the enzyme is involved in synthesis of enterobacterial common antigen. The swarming and swimming abilities mediated by the wecC and fliF genes appears to be essential for penetration activity of Edwardsiella tarda through Caco-2 cell monolayers
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
51400
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
50000
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
dimer
-
monomers aggregate to dimeric form with major interactions from oligomerization domain residues
dimer
-
monomers aggregate to dimeric form with major interactions from oligomerization domain residues
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
gene is not able to complement a defect in the Escherichia coli homologue wecC
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 20 mM Tris-HCl, pH 7.9, 3 M KC1, 2 mM 2-mercaptoethanol, and 10% glycerol, storage without loss of activity for 2 weeks, presence of bovine serum albumin stabilizes
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene wbpA_2, genetic location at 2902611-2903891, DNA and amino acid sequence determination and analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
the wecC gene may represent a useful method for detecting the human type of Edwardsiella tarda, which may have the ability to cause human infection
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Namboori, S.C.; Graham, D.E.
Acetamido sugar biosynthesis in the Euryarchaea
J. Bacteriol.
190
2987-2996
2008
Methanococcus maripaludis (Q6LZC3), Methanococcus maripaludis
brenda
Lokanath, N.K.; Pampa, K.J.; Kamiya, T.; Kunishima, N.
Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. F
63
412-414
2007
Pyrococcus horikoshii (O59284), Pyrococcus horikoshii OT-3 (O59284)
brenda
Burrows, L.L.; Pigeon, K.E.; Lam, J.S.
Pseudomonas aeruginosa B-band lipopolysaccharide genes wbpA and wbpI and their Escherichia coli homologues wecC and wecB are not functionally interchangeable
FEMS Microbiol. Lett.
189
135-141
2000
Pseudomonas aeruginosa (G3XD94)
brenda
Klein, K.A.; Fukuto, H.S.; Pelletier, M.; Romanov, G.; Grabenstein, J.P.; Palmer, L.E.; Ernst, R.; Bliska, J.B.
A transposon site hybridization screen identifies galU and wecBC as important for survival of Yersinia pestis in murine macrophages
J. Bacteriol.
194
653-662
2012
Yersinia pestis (Q8ZAE4), Yersinia pestis
brenda
Kawamura, T.; Ishimoto, N.; Ito, E.
UDP-N-acetyl-D-mannosamine dehydrogenase from Escherichia coli
Methods Enzymol.
83
519-522
1982
Escherichia coli
brenda
Pampa, K.J.; Lokanath, N.K.; Girish, T.U.; Kunishima, N.; Rai, V.R.
Crystal structure of product-bound complex of UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3
Biochem. Biophys. Res. Commun.
453
662-667
2014
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Chen, Z.; Liu, P.; Li, Z.; Yu, W.; Wang, Z.; Yao, H.; Wang, Y.; Li, Q.; Deng, X.; He, N.
Identification of key genes involved in polysaccharide bioflocculant synthesis in Bacillus licheniformis
Biotechnol. Bioeng.
114
645-655
2017
Bacillus licheniformis, Bacillus licheniformis CGMCC 2876
brenda
Suezawa, C.; Yasuda, M.; Negayama, K.; Kameyama, T.; Hirauchi, M.; Nakai, T.; Okuda, J.
Identification of genes associated with the penetration activity of the human type of Edwardsiella tarda EdwGII through human colon epithelial cell monolayers
Microb. Pathog.
95
148-156
2016
Edwardsiella tarda
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.336)
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