Entry
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
ec00541 Biosynthesis of various nucleotide sugars
Orthology
K13016 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
K13020 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Genes
AVT : NCTC3438_01791(gfo_2)
PALI : A3K91_0139 A3K91_0719
PSYP : E5677_09790 E5677_12790
PVB : J5X90_03255 J5X90_03345
CATE : C2869_02600 C2869_15620
LWA : SAMEA4504053_1071(gfo)
LSS : NCTC12082_00067(gfo)
TLR : Thiosp_00142(wbpB_1) Thiosp_04203(wbpB_2)
TNI : TVNIR_0687(pht4_[H])
MFRA : D5125_03850 D5125_03960
HCAM : I4484_08290 I4484_11335
HAMC : HNO52_07875 HNO52_10795
HSX : HNO51_07700 HNO51_11040
HTX : EKK97_08735 EKK97_12330
NZO : SAMEA4504057_0083(iolG)
NANI : NCTC12227_01671(gfo)
NBA : CUN60_03460 CUN60_12660
CHAE : CH06BL_04730(wlbA) CH06BL_39690(wlbA)
LMIR : NCTC12852_00294(afr_1)
BTRM : SAMEA390648701342(bplA)
AXX : ERS451415_06023(gfo)
SMIO : CATMQ487_00180(wlbA)
MLIR : LPB04_23365 LPB04_23900
BRK : CWS35_31765 CWS35_31850
BSEP : HAP48_0047530 HAP48_0047655
BQB : J4P68_0000015 J4P68_0006710 J4P68_0006830
BAUT : QA635_15510 QA635_15625
BBRA : QA636_16015 QA636_16145
BPAH : QA639_29435 QA639_29555
BGEP : ACP2YO_15875 ACP2YO_33905
CAUB : AMEJIAPC_02971(wbpB)
HAD : CDV25_01305 CDV25_01335
HCL : NCTC13205_00267(ycjS)
HPUL : NCTC13154_00522(ycjS_1) NCTC13154_00530(ycjS_2)
GNT : KP003_11600 KP003_17840
PSYF : N1030_13690 N1030_13700
OBG : Verru16b_02254(afr_3)
OBT : OPIT5_15870 OPIT5_24765
MTAR : DF168_01365(iolG_19) DF168_01774(gfo_3)
RUL : UC8_06010(wbpB_1) UC8_10100(gfo_3) UC8_50390(wbpB_2)
RCF : Poly24_12390(pht4_1)
LCRE : Pla8534_38000(afr_6) Pla8534_69440(wbpB)
SNEP : Enr13x_24690(afr_2)
AMUC : Pan181_17760(afr_1)
AMOB : HG15A2_19280(pht4) HG15A2_31400(wbpB)
BMEI : Spa11_26770(ycjS_1)
PBS : Plabr_1624 Plabr_2773
GAZ : Pan241w_05910(afr_1)
PLON : Pla110_21360(afr_3)
CSPN : ACLV6H_18130 ACLV6H_24005
KNV : Pan216_34300(afr_1) Pan216_52050(afr_4)
PBAS : SMSP2_00900(ycjS_4) SMSP2_01883(wbpB)
LPRO : PQO03_07330 PQO03_15080
TPAV : HRQ91_00985 HRQ91_10790
SPER : EW093_13200 EW093_13430
SASS : MUG09_01420 MUG09_02095 MUG09_13360
LUB : TBR22_A19830 TBR22_A52970
PCRE : NCTC12858_00136(iolG)
BVIR : I6J59_09245 I6J59_14365
BACC : BRDCF_p620(ycjS) BRDCF_p621
DORI : FH5T_09010 FH5T_09100 FH5T_21445
MCOS : GM418_12515 GM418_23735
ANF : AQPE_0348 AQPE_0482 AQPE_3061 AQPE_4464
FGG : FSB75_02855 FSB75_06700 FSB75_11455
PGIN : FRZ67_02960 FRZ67_02965
FLV : KJS94_04580 KJS94_16535
AUP : AsAng_0054420 AsAng_0060370
PSN : Pedsa_1140 Pedsa_3258
CXI : ABWH99_15000 ABWH99_16430
ECHI : FKX85_14665 FKX85_20315
AHAO : OM944_05165 OM944_08425
FBT : D770_17580 D770_17610
ZGA : ZOBELLIA_1140 ZOBELLIA_1740(wbpB)
PLIT : K8354_09600 K8354_09870
PHG : KCTC32516_01449(wbpB)
AANR : KCTC52924_00162(iolG_5)
EMAR : D1013_01180 D1013_17800
GAA : HX109_12625 HX109_13045
ASAG : FGM00_13935 FGM00_16580
SPON : HME9304_01540(wbpB)
CGLE : NCTC11432_02321(ycjS)
CTAK : 4412677_01091(yvaA)
CSAL : NBC122_00346(iolW_1)
PTAN : CRYO30217_03202(iolG_2)
BBAU : AEM51_05415 AEM51_07995
BSON : S101395_01005(bvdR)
BHAM : ABN702_00935 ABN702_00940
CSOA : LIS82_06475 LIS82_24415
NOCE : V1499_05665 V1499_21450
MDG : K8L98_08590 K8L98_13025
MHRF : QLQ22_08615 QLQ22_13110
SEDD : ERJ70_04170 ERJ70_06670
MSUT : LC048_00250 LC048_00400
FEC : QNH15_21855 QNH15_23225
PNP : IJ22_38360 IJ22_49060
POW : IJ21_32520 IJ21_43900
PALB : EJC50_27535 EJC50_29195
PMAE : LMZ02_08485 LMZ02_17425
PAUN : MJA45_02230 MJA45_04980 MJA45_15150
PKP : SK3146_01713(afr_8) SK3146_05620(gfo_3)
PELG : ACJ7K1_02250 ACJ7K1_29185
PAJN : JNUCC32_18185 JNUCC32_19315
ATHE : K3F53_17225 K3F53_17345
CHEB : HH215_11990 HH215_20220
COHL : J4772_08780 J4772_18905 J4772_34885
FFE : LSG31_16560 LSG31_16605
LFB : C1X05_09310 C1X05_16015
PABS : JIR001_23250 JIR001_30150
CCOH : SAMEA4530647_1933(ycjS)
CTHD : CDO33_08210 CDO33_08265
AACX : DEACI_0262 DEACI_3301
BPRO : PMF13cell1_05065(iolX_4)
MAS : Mahau_0353 Mahau_1490
SSID : SPSIL_042160(iolG_2) SPSIL_051430(iolG_3)
SACV : SPACI_041580(iolG_2)
COB : COB47_1317 COB47_2107
CHD : Calhy_0192 Calhy_1486
COW : Calow_1030 Calow_2063
CKI : Calkr_1220 Calkr_2363
CLC : Calla_0086 Calla_0628
CKN : Calkro_0219 Calkro_1461
CCHA : ELD05_07305 ELD05_12070
CDIA : CaldiYA01_01930 CaldiYA01_12690
CNAG : OTJ99_000371 OTJ99_001498
CDAN : SOJ16_001196 SOJ16_002463
HRR : HZS55_01030 HZS55_22175
HPEL : HZS54_01075 HZS54_25835
» show all
Taxonomy
Reference
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
Sequence
Reference
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
Sequence
Reference
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
Sequence
Reference
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
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 1.1.1.335
LinkDB
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