KEGG   ENZYME: 1.1.1.335Help
Entry
EC 1.1.1.335                Enzyme                                 

Name
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase;
WlbA;
WbpB
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase
Reaction(IUBMB)
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH + H+ [RN:R10140]
Reaction(KEGG)
Substrate
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate [CPD:C04573];
NAD+ [CPD:C00003]
Product
UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate [CPD:C20395];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
History
EC 1.1.1.335 created 2012
Pathway
Amino sugar and nucleotide sugar metabolism
Orthology
K13016  
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
K13020  
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Genes
PLU: 
plu4797(wblB)
PAY: 
PAU_04312(wblB)
PTT: 
XBO: 
XNE: 
XNM: 
MSU: 
MS1500(mviM)
ASU: 
AAZ: 
DJI: 
DJA: 
VTU: 
PAE: 
PA3158(wbpB)
PAEV: 
N297_3269(wbpB)
PAEI: 
N296_3269(wbpB)
PAEM: 
PAEC: 
M802_3267(wbpB)
PAEO: 
M801_3134(wbpB)
PMY: 
PPUH: 
PBA: 
PDR: 
PSES: 
PSOS: 
PCR: 
PRW: 
PALI: 
ACB: 
ABK: 
ABW: 
ACC: 
ACD: 
SAZ: 
SSE: 
PSEO: 
PLZ: 
MSR: 
MARI: 
AAUS: 
LAL: 
SDE: 
LFA: 
LOK: 
TMB: 
TNI: 
TVNIR_0687(pht4_[H])
TTI: 
HCO: 
ADI: 
B5T_01708(wbpB)
MMW: 
TOR: 
SDF: 
SEDS: 
NEL: 
CVI: 
CVC: 
LHK: 
LHK_02805(wblB)
PSE: 
RPJ: 
REH: 
H16_B0033(wbpB)
PPNO: 
BPE: 
BP0093(bplA)
BPC: 
BPTD_0089(bplA)
BPER: 
BPET: 
BPEU: 
Q425_2060(bplA)
BPA: 
BPP0155(bplA)
BPAR: 
BBR: 
BB0155(bplA)
BBM: 
BBH: 
BBX: 
BPT: 
Bpet4814(wlbA)
BAV: 
BAV0098(wlbA)
BHO: 
BHM: 
BHZ: 
BTRM: 
AXY: 
AXN: 
AXS: 
AXX: 
TEQ: 
TEA: 
TEG: 
PNA: 
AAV: 
AJS: 
ACK: 
VAP: 
VPE: 
VPD: 
CTES: 
HYB: 
HYL: 
HSE: 
HSZ: 
MASW: 
LCH: 
RGE: 
RGE_41570(bplA)
RBN: 
RDP: 
PKT: 
MIU: 
APP: 
HEO: 
HPJ: 
HPA: 
HPS: 
HHP: 
HHQ: 
HHR: 
HPG: 
HPP: 
HPB: 
HPL: 
HPB8_881(wbpB)
HPC: 
HCA: 
HPM: 
HPE: 
HPO: 
HPI: 
HPQ: 
HPW: 
HPU: 
HEF: 
HPF: 
HEQ: 
HEX: 
HPT: 
HPZ: 
HPV: 
HPX: 
HEN: 
HPH: 
HEG: 
HPN: 
HEP: 
HEU: 
HES: 
HPYS: 
HCN: 
HPD: 
KHP_0646(wbpB)
HEY: 
MWE_0830(wbpB)
HER: 
HEI: 
HPYA: 
HPYK: 
HPYO: 
HPYL: 
HPYB: 
HPYC: 
HPYD: 
HPYE: 
HPYF: 
HPYG: 
HPYH: 
HPYJ: 
HPYR: 
HPYI: 
HPYU: 
HPYM: 
HEM: 
HEB: 
HEZ: 
HHE: 
HH_1662(wbpB)
HAC: 
Hac_0861(wbpB)
HMS: 
HFE: 
HBI: 
HCE: 
HCM: 
HCP: 
HCN_0856(wbpB)
HCB: 
HHM: 
WSU: 
WS2188(WBPB)
TDN: 
CCO: 
ABU: 
ANT: 
SUN: 
GLO: 
GEB: 
GSB: 
LIP: 
LIR: 
DBA: 
BBAT: 
BBAC: 
DOL: 
AGC: 
HNI: 
AMT: 
SWO: 
PMI: 
PMB: 
DSW: 
TTH: 
TT_C0287(wbpB)
MRB: 
MRE: 
PBS: 
TPX: 
ABA: 
GAU: 
GPH: 
GBA: 
ACO: 
TLI: 
CPOR: 
BACC: 
PGI: 
PGN: 
PGN_0168(wbpB)
PGT: 
OSP: 
DOI: 
RMR: 
RMG: 
HHY: 
FBT: 
FBR: 
ZGA: 
POM: 
POB: 
TDI: 
TEN: 
LUT: 
WFU: 
IAL: 
IALB_2460(wbpB)
MRO: 
SAF: 
CNI: 
CABY: 
BLQ: 
 » show all
Taxonomy
Reference
1  [PMID:19282284]
  Authors
Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS
  Title
Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the  biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas  aeruginosa.
  Journal
J. Biol. Chem. 284 (2009) 11854-62.
  Sequence
[pae:PA3158]
Reference
2  [PMID:19348502]
  Authors
Larkin A, Imperiali B
  Title
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1.
  Journal
Biochemistry. 48 (2009) 5446-55.
  Sequence
[pae:PA3158]
Reference
3  [PMID:20690587]
  Authors
Thoden JB, Holden HM
  Title
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid .
  Journal
Biochemistry. 49 (2010) 7939-48.
  Sequence
[pae:PA3158]
Reference
4  [PMID:21241053]
  Authors
Thoden JB, Holden HM
  Title
Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid.
  Journal
Biochemistry. 50 (2011) 1483-91.
  Sequence
[bpe:BP0093] [cvi:CV_4127]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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