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Information on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59284

for references in articles please use BRENDA:EC1.1.1.336
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IUBMB Comments
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
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Pyrococcus horikoshii
UNIPROT: O59284
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
udp-n-acetyl-d-mannosamine dehydrogenase, mmp0706, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-D-ManNAcDH
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UDP-ManNAc 6-dehydrogenase
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wecC
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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+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46100
2 * 46100, calculated
92000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 46100, calculated
dimer
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monomers aggregate to dimeric form with major interactions from oligomerization domain residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution, space group P21
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team