KEGG   ENZYME: 1.1.1.305Help
Entry
EC 1.1.1.305                Enzyme                                 

Name
UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating);
UDP-GlcUA decarboxylase;
ArnADH;
UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
UDP-alpha-D-glucuronate:NAD+ oxidoreductase (decarboxylating)
Reaction(IUBMB)
UDP-alpha-D-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+ [RN:R07658]
Reaction(KEGG)
Substrate
UDP-alpha-D-glucuronate [CPD:C00167];
NAD+ [CPD:C00003]
Product
UDP-beta-L-threo-pentapyranos-4-ulose [CPD:C16155];
CO2 [CPD:C00011];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).
History
EC 1.1.1.305 created 2010
Pathway
ec00520  Amino sugar and nucleotide sugar metabolism
Orthology
K10011  UDP-4-amino-4-deoxy-L-arabinose formyltransferase / UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
Genes
ECO: b2255(arnA)
ECJ: JW2249(yfbG)
ECD: ECDH10B_2415(arnA)
EBW: BWG_2028(arnA)
ECOK: ECMDS42_1825(yfbG)
ECE: Z3513
ECS: ECs3143
ECF: ECH74115_3396(arnA)
ETW: ECSP_3132(arnA)
ELX: CDCO157_2906
EOJ: ECO26_3245(arnA)
EOH: ECO103_2721(arnA)
ECG: E2348C_2399(arnA)
EOK: G2583_2795(arnA)
ECC: c2797(yfbG)
ECP: ECP_2298
ECI: UTI89_C2537(yfbG)
ECV: APECO1_4306(yfbG)
ECX: EcHS_A2400(arnA)
ECW: EcE24377A_2550(arnA)
ECM: EcSMS35_2409(arnA)
ECY: ECSE_2514
ECR: ECIAI1_2331(yfbG)
ECQ: ECED1_2721(yfbG)
ECK: EC55989_2501(yfbG)
ECT: ECIAI39_2402(yfbG)
EOC: CE10_2638(arnA)
EUM: ECUMN_2596(yfbG)
ECZ: ECS88_2404(yfbG)
ELO: EC042_2498(arnA)
ELH: ETEC_2389
ESE: ECSF_2135
ESO: O3O_17420
ESM: O3M_08165
ESL: O3K_08215
EBR: ECB_02181(yfbG)
EBD: ECBD_1404
EKF: KO11_11410(arnA)
EAB: ECABU_c25890(arnA)
EDJ: ECDH1ME8569_2191(arnA)
EIH: ECOK1_2491(arnA)
ENA: ECNA114_2348(yfbG)
ELW: ECW_m2446(arnA)
ELL: WFL_11970(arnA)
ELC: i14_2596(yfbG)
ELD: i02_2596(yfbG)
ELP: P12B_c2349(arnA)
EBL: ECD_02181(arnA)
EBE: B21_02140(arnA)
ELF: LF82_0136(arnA)
ECOI: ECOPMV1_02416(arnA)
ECOJ: P423_12625
ECOS: EC958_2593(yfbG)
EFE: EFER_0914(yfbG)
EAL: EAKF1_ch3724c(arnA)
STY: STY2529
STT: t0564
STM: STM2299(yfbG)
SEO: STM14_2837(yfbG)
SEY: SL1344_2268(yfbG)
SEJ: STMUK_2329(yfbG)
SEB: STM474_2395(yfbG)
SENI: CY43_12320
SPT: SPA0564(yfbG)
SEK: SSPA0528
SEI: SPC_1412(yfbG)
SHB: SU5_02894
SENS: Q786_11335
SED: SeD_A2643
SEG: SG2328(yfbG)
SEL: SPUL_0591(yfbG)
SEGA: SPUCDC_0591(yfbG)
SET: SEN2281(yfbG)
SENO: AU37_11540
SENV: AU39_11540
SENQ: AU40_12920
SENL: IY59_11855
SEEP: I137_02725
SENE: IA1_11450
SBG: SBG_2088
SBZ: A464_2413
SFX: S2467(ybfG)
SFV: SFV_2325
SFE: SFxv_2577(arnA)
SFN: SFy_3321
SFS: SFyv_3396
SFT: NCTC1_02567(arnA)
SSN: SSON_2316
SBO: SBO_2292
SBC: SbBS512_E2631(arnA)
ENC: ECL_04861
ECLO: ENC_26920
EEC: EcWSU1_04282(arnA)
ECLY: LI62_23410
KPN: KPN_03845(yfbG)
KPU: KP1_5182
KPP: A79E_0271
KPT: VK055_3625(arnA)
KPE: KPK_0268(arnA)
KPR: KPR_5072(arnA)
KPJ: N559_0309
KPX: PMK1_01347(arnA)
KPNU: LI86_01380
KPNK: BN49_0272(arnA)
KVA: Kvar_0256
KOX: KOX_05070
KOE: A225_5481
EAE: EAE_05690
EAR: CCG32860
CAMA: F384_12075
HDE: HDEF_0857(arnA)
SECT: A359_07480
SEHC: A35E_00191
EBT: EBL_c14160(arnA)
EBF: D782_1295
YPE: YPO2420
YPK: y1919
YPA: YPA_1764
YPN: YPN_1874
YPM: YP_2207(wcaG9)
YPG: YpAngola_A2610(arnA)
YPZ: YPZ3_1467
YPD: YPD4_1432
YPX: YPD8_1513
YPH: YPC_2055
YPW: CH59_4254
YPJ: CH55_496
YPV: BZ15_1105
YPL: CH46_2685
YPS: YPTB2328(pmrI)
YPO: BZ17_126
YPI: YpsIP31758_1727(arnA)
YPY: YPK_1833
YPB: YPTS_2403
YPQ: DJ40_4257
YPU: BZ21_1616
YPR: BZ20_3915
YPC: BZ23_1902
YPF: BZ19_1693
YEN: YE2190
YEY: Y11_08001
YEW: CH47_1625
YET: CH48_3631
YAL: AT01_262
YFR: AW19_1396
YIN: CH53_4133
YKR: CH54_266
YRO: CH64_735
YRU: BD65_479
SPE: Spro_2156
SRL: SOD_c19700(arnA)
SPLY: Q5A_010900(arnA)
SMAF: D781_1987
SMW: SMWW4_v1c21850(arnA)
SMAR: SM39_1617(arnA)
SMAC: SMDB11_1430(arnA)
SERF: L085_17840
RAA: Q7S_14230
ECA: ECA3144
PATR: EV46_15565
PATO: GZ59_31540
PCT: PC1_2926
PEC: W5S_1258
SGL: SG1843
SOD: Sant_1032(arnA)
PES: SOPEG_3209(arnA)
DDD: Dda3937_01078(yfbG)
DDQ: DDI_4291
ETA: ETA_23810(arnA)
EPY: EpC_25160(arnA)
EPR: EPYR_02726(yfbG)
EAM: EAMY_1085(yfbG)
EAY: EAM_1092(arnA)
EBI: EbC_12130(arnA)
ERJ: EJP617_22110(arnA)
EGE: EM595_p0068(arnA)
WBR: b2255
WGL: WIGMOR_0622(arnA)
PAM: PANA_4004(arnA)
PLF: PANA5342_0585(arnA) PANA5342_p10122(arnA)
PAJ: PAJ_p0005(arnA)
PAQ: PAGR_p093
PVA: Pvag_pPag10070(yfbG)
PLU: plu2658(pbgP3)
PAY: PAU_01877(arnA)
PMR: PMI1045(arnA)
PMIB: BB2000_1082(arnA)
XBO: XBJ1_2534(arnA)
XBV: XBW1_3010(pbgP)
XNE: XNC1_1837(pbgP3)
XNM: XNC2_1782(pbgP)
XDO: XDD1_1781(pbgP)
XPO: XPG1_1548(pbgP)
PSI: S70_19365
PSX: DR96_2785
PRG: RB151_019250(arnA)
MMK: MU9_2436
ETR: ETAE_1293
ETD: ETAF_1205
ETE: ETEE_3268(arnA)
PAE: PA3554(arnA)
PAEV: N297_3677
PAEI: N296_3677
PAU: PA14_18350(fmt)
PNC: NCGM2_4680(fmt)
PAEB: NCGM1900_2729(fmt)
PAEP: PA1S_07650
PAEM: U769_07125
PAEL: T223_07365
PAEG: AI22_26255
PAEC: M802_3674
PAEO: M801_3542
PCQ: PcP3B5_10970(arnA)
PSB: Psyr_2691
PSYR: N018_13795
PSP: PSPPH_2804(arnA)
PFL: PFL_3045(arnA)
PPRC: PFLCHA0_c30730(arnA)
PPRO: PPC_3073
PFS: PFLU_3041
PFC: PflA506_2684(arnA)
PFW: PF1751_v1c26890(arnA)
PFB: VO64_0275
PMAN: OU5_0511(arnA)
PKC: PKB_4721(arnA)
PSEM: TO66_15070
PSOS: POS17_3049
PANR: A7J50_2964
SSE: Ssed_0924
AHA: AHA_0990
ASA: ASA_3309(arnA)
ASR: WL1483_257(arnA)
SLIM: SCL_0154
BBH: BN112_3283(wbmQ) BN112_3284(wbmR)
BBX: BBS798_0127(wbmQ)
CFU: CFU_3305(yfbG)
MAGQ: MGMAQ_1148
WIN: WPG_2358
SALI: L593_11355
 » show all
Taxonomy
Reference
1  [PMID:15695810]
  Authors
Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR.
  Title
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose.
  Journal
J Biol Chem 280:14154-67 (2005)
DOI:10.1074/jbc.M414265200
  Sequence
[eco:b2255]
Reference
2  [PMID:15491143]
  Authors
Gatzeva-Topalova PZ, May AP, Sousa MC
  Title
Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance.
  Journal
Biochemistry 43:13370-9 (2004)
DOI:10.1021/bi048551f
  Sequence
[eco:b2255]
Reference
3  [PMID:15809294]
  Authors
Williams GJ, Breazeale SD, Raetz CR, Naismith JH.
  Title
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.
  Journal
J Biol Chem 280:23000-8 (2005)
DOI:10.1074/jbc.M501534200
  Sequence
[eco:b2255]
Reference
4  [PMID:15939024]
  Authors
Gatzeva-Topalova PZ, May AP, Sousa MC
  Title
Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.
  Journal
Structure 13:929-42 (2005)
DOI:10.1016/j.str.2005.03.018
  Sequence
[eco:b2255]
Reference
5  [PMID:17928292]
  Authors
Yan A, Guan Z, Raetz CR
  Title
An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.
  Journal
J Biol Chem 282:36077-89 (2007)
DOI:10.1074/jbc.M706172200
  Sequence
[eco:b2255]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.305
IUBMB Enzyme Nomenclature: 1.1.1.305
ExPASy - ENZYME nomenclature database: 1.1.1.305
BRENDA, the Enzyme Database: 1.1.1.305

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