ID   AROE_CLOPS              Reviewed;         271 AA.
AC   Q0SV31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Shikimate dehydrogenase;
DE            EC=1.1.1.25;
GN   Name=aroE; OrderedLocusNames=CPR_0693;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 4/7.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
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DR   EMBL; CP000312; ABG85376.1; -; Genomic_DNA.
DR   RefSeq; YP_698019.1; -.
DR   GeneID; 4204010; -.
DR   GenomeReviews; CP000312_GR; CPR_0693.
DR   KEGG; cpr:CPR_0693; -.
DR   TIGR; CPR_0693; -.
DR   HOGENOM; Q0SV31; -.
DR   OMA; Q0SV31; LHGYWLK.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
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; -; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR011342; Quinate/shikimate_5-DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    271       Shikimate dehydrogenase.
FT                                /FTId=PRO_1000021278.
FT   NP_BIND     125    129       NADP (By similarity).
FT   ACT_SITE     65     65       Proton acceptor (Potential).
SQ   SEQUENCE   271 AA;  30555 MW;  940043DF69B7C38B CRC64;
     MKLFGLIGEK LGHSLSPEIH NKVFKDNNID GLYNLFSVKK DFENNIVESL KCLGVRGANV
     TIPYKEKVMN QLDIISHEAK AIGAVNTILI KDGKSYGYNT DYYGFGKMLE RAKVDIEGNS
     FFVLGAGGAA RSILKYLEDS KAKKIVLVSR DKEKVFKKFK DFNINFMSYG ELEEIHEEFA
     LINTTPCGMY PNTNSVAVSE KVIKKFKVAL DIVYNPLETK FLKMAKDNGL KTVDGLFMLV
     GQGVKAEEIW NGIKVDKSTE ENIYEELKCR F
//