KEGG   ENZYME: 1.1.1.282
Entry
EC 1.1.1.282                Enzyme                                 

Name
quinate/shikimate dehydrogenase;
YdiB
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-quinate:NAD(P)+ 3-oxidoreductase
Reaction(IUBMB)
(1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ [RN:R01872 R06846];
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ [RN:R02413 R06847]
Reaction(KEGG)
Substrate
L-quinate [CPD:C00296];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
shikimate [CPD:C00493]
Product
3-dehydroquinate [CPD:C00944];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
3-dehydroshikimate [CPD:C02637]
Comment
This is the second shikimate dehydrogenase enzyme found in Escherichia coli and differs from EC 1.1.1.25, shikimate dehydrogenase, in that it can use both quinate and shikimate as substrate and either NAD+ or NADP+ as acceptor.
History
EC 1.1.1.282 created 2004
Pathway
ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K05887  quinate/shikimate dehydrogenase
Genes
ECO: b1692(ydiB)
ECJ: JW1682(ydiB)
ECD: ECDH10B_1828(ydiB)
EBW: BWG_1506(ydiB)
ECOK: ECMDS42_1365(ydiB)
ECE: Z2720(ydiB)
ECS: ECs2399(aroE)
ECF: ECH74115_2408
ETW: ECSP_2259(ydiB)
ELX: CDCO157_2233(aroE)
EOI: ECO111_2161(ydiB)
EOJ: ECO26_2420(ydiB)
EOH: ECO103_1835(ydiB)
ECOO: ECRM13514_2187(aroE)
ECOH: ECRM13516_2092(aroE)
ESL: O3K_11775
ESO: O3O_13860
ESM: O3M_11740
ECK: EC55989_1859(ydiB)
ECG: E2348C_1777(ydiB)
EOK: G2583_2089(ydiB)
ELH: ETEC_1725
ECP: ECP_1639
ENA: ECNA114_1739(ydiB)
ECOS: EC958_1912(ydiB)
ECV: APECO1_768(ydiB)
ECY: ECSE_1815
ECR: ECIAI1_1745(ydiB)
ECQ: ECED1_1891(ydiB)
EUM: ECUMN_1981(ydiB)
ECT: ECIAI39_1366(ydiB)
EOC: CE10_1966(ydiB)
EBR: ECB_01661(ydiB)
EBL: ECD_01661(ydiB)
EBE: B21_01650(ydiB)
EBD: ECBD_1954
ECI: UTI89_C1884(ydiB)
ECZ: ECS88_1742(ydiB)
ECC: c2087(ydiB)
ESE: ECSF_1552
EKF: KO11_14285(ydiB)
EAB: ECABU_c19460(ydiB)
EDJ: ECDH1ME8569_1636(ydiB)
ELW: ECW_m1861(ydiB)
ELL: WFL_09110(ydiB)
ELC: i14_1909(aroE)
ELD: i02_1909(aroE)
ELP: P12B_c1391(aroE)
ELF: LF82_2870(ydiB)
ECOI: ECOPMV1_01791(ydiB)
ECOJ: P423_09035
EFE: EFER_0091
ESZ: FEM44_23400(ydiB)
STM: STM1359(ydiB)
SEO: STM14_1650(aroE_1)
SEY: SL1344_1293(aroE)
SEJ: STMUK_1326(aroE)
SEB: STM474_1364(aroE)
SEF: UMN798_1416(aroE)
SENR: STMDT2_12921(aroE)
SEND: DT104_13371(aroE)
SENI: CY43_06920
SEI: SPC_2371(aroE)
SEC: SCH_1378(ydiB)
SHB: SU5_01977
SENS: Q786_08455
SED: SeD_A1984
SEG: SG1757(ydiB)
SEL: SPUL_1177(ydiB)
SEGA: SPUCDC_1177(ydiB)
SET: SEN1685(ydiB)
SENA: AU38_08725
SENO: AU37_08730
SENV: AU39_08735
SENQ: AU40_09735
SENL: IY59_08920
SEEP: I137_05420
SENE: IA1_06705
SFL: SF1722(aroE)
SFX: S1854(ydiB)
SFV: SFV_1718(ydiB)
SFE: SFxv_1929(ydiB)
SFN: SFy_2467
SFS: SFyv_2522
SFT: NCTC1_01868(ydiB)
SSN: SSON_1462(ydiB)
SDY: SDY_1475(ydiB)
ENF: AKI40_1900(ydiB)
KPU: KP1_0890(aroE)
KPP: A79E_4226
KPT: VK055_2498(ydiB)
KPO: KPN2242_02810(aroE)
KPR: KPR_0998
KPJ: N559_4356
KPX: PMK1_02383(aroE_2)
KPNU: LI86_22370
KPNK: BN49_4265
KVA: Kvar_4308
KPE: KPK_4667
KOX: KOX_10830(aroE)
KOE: A225_0875
KOY: J415_26885(aroE)
EAE: EAE_11160(aroE)
EAR: CCG31755
CPOT: FOB25_01110(ydiB)
CAMA: F384_06180
METY: MRY16398_47470(aroE)
SUTK: FG381_00155(ydiB)
BAQ: BACAU_0778(aroE1)
BYA: BANAU_0723(aroE1)
BAMP: B938_03870
BAMA: RBAU_0782(ydiB)
BAMN: BASU_0758(ydiB)
BAMB: BAPNAU_0734(aroE1)
BAMT: AJ82_04495
BAMY: V529_07450
BMP: NG74_00799(aroE_1)
BAO: BAMF_0755(RBAM_008070)
BQL: LL3_00809
BQY: MUS_0802(aroE)
BAMI: KSO_015775
BAMC: U471_07900
BAMF: U722_04025
BMQ: BMQ_0974(aroD)
BMD: BMD_0975(aroD) BMD_3610
BMEG: BG04_3263(aroE) BG04_523
BACI: B1NLA3E_05085(aroE) B1NLA3E_05110(aroE)
BACP: SB24_05875
BACB: OY17_06660
LMOE: BN418_0563
LMOB: BN419_0569
LIV: LIV_2223
PPY: PPE_00893
PPM: PPSC2_04635(ydiB1)
PPO: PPM_0869(ydiB1)
PPOL: X809_04280
PPQ: PPSQR21_009250(aroE)
PPOY: RE92_07330
LPJ: JDM1_2789(aroD3) JDM1_2790(aroD4)
LPT: zj316_0126(aroD3) zj316_0127(aroD4)
LCA: LSEI_0476
LCS: LCBD_0541(aroDE)
LCE: LC2W_0542(aroDE)
LPAP: LBPC_0442
LCW: BN194_05480(aroE_2)
ECAS: ECBG_02583
EDU: LIU_07945
EGA: AL523_01565(aroE)
JAR: G7057_00650(aroE)
CKL: CKL_1014(aroE3)
CKR: CKR_0918
CSB: CLSA_c07000(aroE2) CLSA_c07040(aroE3)
CSQ: CSCA_1647
RUM: CK1_34250
BFI: CIY_16020
RIX: RO1_38400
RIM: ROI_16940
CCT: CC1_23550
BLAB: EYS05_11210(aroE)
CSCI: HDCHBGLK_02860(aroE)
EHL: EHLA_0534
RTO: RTO_32440
ERT: EUR_24270
ERA: ERE_09960
PDC: CDIF630_02965(aroE2)
CDC: CD196_2549(ydiB)
CDL: CDR20291_2596(ydiB)
PDF: CD630DERM_27080(aroE2)
ELM: ELI_0966
OVA: OBV_35430(aroE)
BPRS: CK3_17120
EBM: SG0102_23460(aroE)
TPYO: X956_05370
ELE: Elen_2551
XII: AMD24_00667(ydiB)
 » show all
Reference
1  [PMID:12637497]
  Authors
Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ.
  Title
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
  Journal
J Biol Chem 278:19463-72 (2003)
DOI:10.1074/jbc.M300794200
  Sequence
[eco:b1692]
Reference
2  [PMID:12624088]
  Authors
Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF.
  Title
The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
  Journal
J Biol Chem 278:19176-82 (2003)
DOI:10.1074/jbc.M301348200
  Sequence
[eco:b1692]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.282
IUBMB Enzyme Nomenclature: 1.1.1.282
ExPASy - ENZYME nomenclature database: 1.1.1.282
BRENDA, the Enzyme Database: 1.1.1.282
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