ID   AROE_COREF              Reviewed;         284 AA.
AC   Q8FSF0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Quinate/shikimate dehydrogenase;
DE            EC=1.1.1.24;
DE            EC=1.1.1.-;
DE   AltName: Full=NAD(+)-dependent quinate dehydrogenase;
DE            Short=QDH;
GN   Name=aroE; OrderedLocusNames=CE0443;
OS   Corynebacterium efficiens.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=152794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of both quinate
CC       and shikimate to 3-dehydroquinate and 3-dehydroshikimate,
CC       respectively. Seems to play a key role in the quinate degradation
CC       pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: Quinate + NAD(+) = 3-dehydroquinate + NADH.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NAD(+) = 3-dehydroshikimate +
CC       NADH.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 4/7.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
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DR   EMBL; BA000035; BAC17253.1; -; Genomic_DNA.
DR   RefSeq; NP_737053.1; -.
DR   HSSP; Q58484; 1NVT.
DR   SMR; Q8FSF0; 4-284.
DR   GeneID; 1034899; -.
DR   GenomeReviews; BA000035_GR; CE0443.
DR   KEGG; cef:CE0443; -.
DR   NMPDR; fig|196164.1.peg.443; -.
DR   HOGENOM; Q8FSF0; -.
DR   OMA; Q8FSF0; VKAFELF.
DR   BioCyc; CEFF196164:CE0443-MON; -.
DR   BRENDA; 1.1.1.25; 277326.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030266; F:quinate 5-dehydrogenase activity; IEA:EC.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic pro...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00222; atypical; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005097; Saccharopine_DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03435; Saccharop_dh; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    284       Quinate/shikimate dehydrogenase.
FT                                /FTId=PRO_0000325114.
FT   NP_BIND     135    139       NAD (By similarity).
FT   NP_BIND     252    256       NAD (By similarity).
FT   ACT_SITE     74     74       Proton acceptor (Potential).
FT   BINDING     111    111       Substrate (By similarity).
FT   BINDING     159    159       NAD (By similarity).
SQ   SEQUENCE   284 AA;  29938 MW;  7179FA02CF0DE537 CRC64;
     MNHDSILLGL IGEDISLSRT PAMHEAEGLA QGAATVYRRI DTLTDRARGR SLQELLDAAR
     STGFNGLNIT HPYKQAVLPL LDEVSEQAAQ LGAVNTVVIG EDGRTSGHNT DVTGFARGLE
     EGLPDATMTT VVQVGAGGVG NAVAYSLVTH GVEQLQVADL DPARAQALAD AINSAIGREA
     VHGIDARGVE EAIAAADGVV NATPMGMLAH PGTAFDTSCL TPHHWVGDVV YMPIETQLLK
     DARALGCRTL DGTRMAIHQA VDAFRLFTGL EPDVERMRAT FLSL
//