Entry
Name
quinate/shikimate dehydrogenase (NAD+);
quinate dehydrogenase (ambiguous);
quinic dehydrogenase (ambiguous);
quinate:NAD oxidoreductase;
quinate 5-dehydrogenase (ambiguous);
quinate:NAD+ 5-oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-quinate:NAD+ 3-oxidoreductase
Reaction(IUBMB)
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+ [RN:
R01872 ]
Reaction(KEGG)
Substrate
Product
Comment
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC
1.1.5.8 , quinate/shikimate dehydrogenase (quinone), EC
1.1.1.282 , quinate/shikimate dehydrogenase [NAD(P)+], and EC
1.1.1.25 , shikimate dehydrogenase (NADP+).
History
EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021
Pathway
ec00400 Phenylalanine, tyrosine and tryptophan biosynthesis
Orthology
K25901 quinate/shikimate dehydrogenase (NAD+)
Genes
NTE : NEUTE1DRAFT46730(NEUTE1DRAFT_46730)
SSCK : SPSK_00849 SPSK_06463
FGR : FGSG_03880 FGSG_05704 FGSG_12357
FPU : FPSE_06307 FPSE_06596 FPSE_06601
FPOA : FPOAC1_006297 FPOAC1_006302 FPOAC1_008652(QA3)
FVN : FVRRES_06901 FVRRES_06906 FVRRES_09249
FVR : FVEG_05965 FVEG_09879
FOX : FOXG_04621 FOXG_08708 FOXG_10944
NHE : NECHADRAFT_32803 NECHADRAFT_51161
FFC : NCS54_00213200 NCS54_01291000
FMU : J7337_000083 J7337_004802(QA3)
CFJ : CFIO01_01549 CFIO01_09601
CLUP : CLUP02_09230 CLUP02_14466
ELA : UCREL1_1141 UCREL1_7618
PFY : PFICI_03111 PFICI_14932 PFICI_15086
PSCO : LY89DRAFT_635429 LY89DRAFT_680000 LY89DRAFT_698602
AFM : AFUA_1G11590 AFUA_3G14800
AOR : AO090038000263 AO090103000428 AO090103000431
ANG : An03g03710 An04g08100
AFV : AFLA_008750 AFLA_013099 AFLA_013104
ALUC : AKAW2_30242S AKAW2_50769A
ACHE : ACHE_30247S ACHE_80025A
APUU : APUU_30054A APUU_31273S APUU_50617S
TMF : EYB26_001333 EYB26_002338
TRG : TRUGW13939_02954 TRUGW13939_04943
PNO : SNOG_10413 SNOG_11439
ZTR : MYCGRDRAFT_84424(qa-3)
CCAC : CcaHIS019_0606160(CcaverHIS019_0606160)
PAEB : NCGM1900_0235(aroE)
PCQ : PcP3B5_36090(aroE_2)
PPB : PPUBIRD1_3278(aroE_3)
PVD : CFBP1590__2183(aroE)
PPRC : PFLCHA0_c53540(aroE2)
PMUD : NCTC8068_04581(aroE2)
PFW : PF1751_v1c47820(aroE)
PPUU : PputUW4_04721(aroE2)
PSEC : CCOS191_3120(aroE2)
POJ : PtoMrB4_30530(aroE_2)
PTW : TUM18999_29460(aroE_3)
PTAE : NCTC10697_00709(aroE_2)
HTX : EKK97_10020 EKK97_21495
MARS : A8C75_03190 A8C75_03735
BPM : BURPS1710b_A1897(aroE)
BPL : BURPS1106A_A0483(aroE)
BPD : BURPS668_A0580(aroE)
BUE : BRPE67_ACDS07620(aroE)
PDIO : PDMSB3_2300.1(aroE)
PLG : NCTC10937_03700(aroE_2)
MESM : EJ066_01655 EJ066_30260
PHT : BLM14_17570 BLM14_19965
SMEL : SM2011_b20037(aroE2)
RHI : NGR_b00200 NGR_b06000
SFD : USDA257_c22240(aroE1) USDA257_c56320(aroE2)
SAME : SAMCFNEI73_pC0018(aroE)
SINO : SS05631_b49820 SS05631_b63110
ESJ : SJ05684_b47210 SJ05684_b53920
EAK : EKH55_1601 EKH55_4826
AVV : RvVAT039_38280(aroE)
AVF : RvVAR031_41320(aroE)
RET : RHE_CH02291(aroEch2) RHE_PC00214(aroEc)
REL : REMIM1_CH02301(aroE-2) REMIM1_PB00219(aroE-3)
REP : IE4803_CH01956(aroE-2) IE4803_PD00660(aroE-3)
REI : IE4771_CH02031(aroE-2) IE4771_PE00684(aroE-3)
RTR : RTCIAT899_PC05330 RTCIAT899_PC07925
RGA : RGR602_PC02220(aroE-2)
RHN : AMJ98_CH02346(aroE-2) AMJ98_PB00285(aroE-3)
RPHA : AMC79_CH03887(aroE-2) AMC79_PA00326(aroE-3)
RHX : AMK02_CH02362(aroE-2) AMK02_PB00300(aroE-3)
RHK : Kim5_CH02056(aroE-2) Kim5_PD00633(aroE-3)
REZ : AMJ99_CH02424(aroE-2) AMJ99_PA00285(aroE-3)
RBQ : J2J99_09965 J2J99_26870
RLN : J0663_20970 J0663_29630
SOJ : K6301_18725 K6301_20725 K6301_22005
SSUM : Q9314_19400 Q9314_21180 Q9314_26130
BJA : bll1059(aroE) bll6391(aroE)
BRO : BRAD285_1609(aroE) BRAD285_3019(aroE)
BGQ : X265_05330 X265_34730
BGZ : XH91_05355 XH91_33120
BVZ : BRAD3257_6024(aroE) BRAD3257_8666(aroE)
VGO : GJW-30_1_01140(aroE_2)
MAQU : Maq22A_c10215(aroE) Maq22A_c19135(aroE)
MEE : DA075_08870 DA075_24535
MTEA : DK419_05545 DK419_21185
MIND : mvi_02410(aroE_1) mvi_33050(aroE_3)
MOC : BB934_22135 BB934_24965
LAP : ACP90_08185 ACP90_08360
YPAC : CEW88_16985 CEW88_22640
SPSE : SULPSESMR1_00067(aroE)
PMAU : CP157_03022(aroE_2)
SBIN : SBA_ch2_1490(aroE_1) SBA_ch2_3400(aroE_2)
SPYG : YGS_C2P0952 YGS_C2P1151
MGAU : MGALJ_11380(aroE_2)
MMAT : MMAGJ_48380(aroE_1)
MSEI : MSEDJ_10090(aroE_1)
CCYC : SCMU_39920(aroE_2) SCMU_40300(aroE_3)
RHA : RHA1_ro01342(aroE1) RHA1_ro01853(aroE3)
REB : XU06_17790 XU06_22275
RQI : C1M55_18770 C1M55_23615
ROP : ROP_10580(aroE) ROP_15380(aroE) ROP_21990(aroE)
ROA : Pd630_LPD05461 Pd630_LPD06023
RPY : Y013_09920 Y013_14040
RAV : AAT18_10970 AAT18_25260
RRZ : CS378_00720 CS378_14840
RHOD : AOT96_03650 AOT96_29400
RRT : 4535765_03803(aroE_2)
RKO : JWS14_06905 JWS14_09520 JWS14_12960
RGO : KYT97_26160 KYT97_30380
ROZ : CBI38_11155 CBI38_24855
RPSK : JWS13_32905 JWS13_36315 JWS13_39525
SAMB : SAM23877_6314(aroE)
SLE : sle_11670(sle_11670)
SGM : GCM10017557_12750(aroE)
SPHV : F9278_40145 F9278_41605
STUI : GCM10017668_59870(aroE)
MHOS : CXR34_05715 CXR34_10865
AMAV : GCM10025877_22880(aroE_2)
LTN : KVY00_10585 KVY00_10615
ARL : AFL94_05075 AFL94_14405
ARY : ATC04_03530 ATC04_12810
ARTP : E5206_03525 E5206_14090
ACAO : NF551_08110 NF551_14275
PNV : JMY29_13025 JMY29_19420
GPR : JQN66_05515 JQN66_14430
SATK : SA2016_3914 SA2016_3943
NAQU : ENKNEFLB_00208(aroE_1)
PSEH : XF36_10740 XF36_13835
ASIC : Q0Z83_040480 Q0Z83_102990
» show all
Taxonomy
Reference
Authors
MITSUHASHI S, DAVIS BD.
Title
Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase.
Journal
Reference
2
Authors
Gamborg, O.L.
Title
Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures.
Journal
Biochim Biophys Acta 128:483-491 (1966)
Reference
Authors
Hawkins AR, Giles NH, Kinghorn JR.
Title
Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans.
Journal
Reference
Authors
Singh S, Stavrinides J, Christendat D, Guttman DS.
Title
A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass.
Journal
Reference
Authors
Teramoto H, Inui M, Yukawa H.
Title
Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum.
Journal
Sequence
Reference
Authors
Kubota T, Tanaka Y, Hiraga K, Inui M, Yukawa H.
Title
Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum.
Journal
Sequence
Reference
Authors
Peek J, Christendat D.
Title
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.24
ExPASy - ENZYME nomenclature database: 1.1.1.24