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
ec00520  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)
PLUM: A4R40_23860
PAY: PAU_04312(wblB)
PTT: VY86_07520
XBO: XBJ1_4314
XNE: XNC1_0112
XNM: XNC2_0114
MSU: MS1500(mviM)
ASU: Asuc_0110
AAZ: ADJ80_05775
PAE: PA3158(wbpB)
PAEV: N297_3269(wbpB)
PAEI: N296_3269(wbpB)
PAEM: U769_09132
PAEC: M802_3267(wbpB)
PAEO: M801_3134(wbpB)
PMY: Pmen_1858
PPUH: B479_06900
PSES: PSCI_2866
PSOS: POS17_4987
PSET: THL1_1977
ACB: A1S_0053
SAZ: Sama_2259
SSE: Ssed_2972
PSEO: OM33_04950
AAUS: EP12_05245
SDE: Sde_0872
LFA: LFA_0788
LOK: Loa_02107
TNI: TVNIR_0687(pht4_[H])
HCO: LOKO_02148(wbpB)
ADI: B5T_01708(wbpB)
CVI: CV_4127
LHK: LHK_02805(wblB)
PSE: NH8B_0413
REH: H16_B0033(wbpB)
PPNO: DA70_17270
BPE: BP0093(bplA)
BPC: BPTD_0089(bplA)
BPER: BN118_0162(wlbA)
BPET: B1917_0096(bplA)
BPEU: Q425_2060(bplA)
BPA: BPP0155(bplA)
BPAR: BN117_0153(wlbA)
BBR: BB0155(bplA)
BBM: BN115_0144(wlbA)
BBH: BN112_3256(wlbA)
BBX: BBS798_0154(bplA)
BPT: Bpet4814(wlbA)
BAV: BAV0098(wlbA)
BHO: D560_1328
BHM: D558_1317
BHZ: ACR54_00110(gfo)
BTRM: SAMEA390648701342(bplA)
AXX: ERS451415_06023(gfo)
TEA: KUI_0407
TEG: KUK_0147
ODI: ODI_R2826
PNA: Pnap_3129
AAV: Aave_0950
AJS: Ajs_3015
CTES: O987_08010
HYB: Q5W_21470
LCH: Lcho_0289
RGE: RGE_41570(bplA)
HPJ: jhp_0620
HPG: HPG27_637
HPP: HPP12_0690(wbpB)
HPL: HPB8_881(wbpB)
HPI: hp908_0688(wbpB)
HPQ: hp2017_0665(wbpB)
HPW: hp2018_0666(wbpB)
HEF: HPF16_0688(wbpB)
HPF: HPF30_0654(wbpB)
HEQ: HPF32_0643(wbpB)
HEX: HPF57_0700(wbpB)
HPZ: HPKB_0669
HPD: KHP_0646(wbpB)
HEY: MWE_0830(wbpB)
HPYO: HPOK113_0689(wbpB)
HPYL: HPOK310_0668(wbpB)
HPYR: K747_07485
HPYI: K750_05685
HPYU: K751_03995
HPYM: K749_02110
HEB: U063_0983
HEZ: U064_0987
HHE: HH_1662(wbpB)
HAC: Hac_0861(wbpB)
HMS: HMU06630
HCE: HCW_05405
HCM: HCD_05220
HCP: HCN_0856(wbpB)
HCB: HCBAA847_1124(wbpB)
WSU: WS2188(WBPB)
ABU: Abu_0662
SUN: SUN_0093
GLO: Glov_1510
GEB: GM18_1433
LIP: LIC097
LIR: LAW_30095
DBA: Dbac_3255
DOL: Dole_1819
BBAT: Bdt_1672
BBAC: EP01_04555
AMT: Amet_3444
SWO: Swol_0706
TTH: TT_C0287(wbpB)
MRB: Mrub_0358
PBAS: SMSP2_01883(wbpB)
TLI: Tlie_1823
GAU: GAU_1966
GBA: J421_2473
BACC: BRDCF_p620(ycjS) BRDCF_p621
PGI: PG_2119
PGN: PGN_0168(wbpB)
BLQ: L21SP5_01622(wbpB)
RMR: Rmar_1674
ZGA: ZOBELLIA_1740(wbpB)
TJE: TJEJU_1135(wbpB)
TMAR: MARIT_2536(wbpB)
SPON: HME9304_01540(wbpB)
IAL: IALB_2460(wbpB)
MRO: MROS_2688
CACI: CLOAM1565(mviM)
CABY: Cabys_972
 » 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 284:11854-62 (2009)
DOI:10.1074/jbc.M808583200
  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 48:5446-55 (2009)
DOI:10.1021/bi900186u
  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 49:7939-48 (2010)
DOI:10.1021/bi101103s
  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 50:1483-91 (2011)
DOI:10.1021/bi101871f
  Sequence
[bpe:BP0093] [cvi:CV_4127]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.335
IUBMB Enzyme Nomenclature: 1.1.1.335
ExPASy - ENZYME nomenclature database: 1.1.1.335
BRENDA, the Enzyme Database: 1.1.1.335

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