ID AROE_BACAH Reviewed; 277 AA. AC A0RIV1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Shikimate dehydrogenase; DE EC=1.1.1.25; GN Name=aroE; OrderedLocusNames=BALH_3922; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17337577; DOI=10.1128/JB.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., RA Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000485; ABK87144.1; -; Genomic_DNA. DR RefSeq; YP_896651.1; -. DR GeneID; 4545071; -. DR GenomeReviews; CP000485_GR; BALH_3922. DR KEGG; btl:BALH_3922; -. DR NMPDR; fig|412694.5.peg.3776; -. DR OMA; A0RIV1; IVSDIIY. 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 1 277 Shikimate dehydrogenase. FT /FTId=PRO_1000021258. FT NP_BIND 127 131 NADP (By similarity). FT ACT_SITE 66 66 Proton acceptor (Potential). SQ SEQUENCE 277 AA; 30122 MW; D73883CD2D1BA542 CRC64; MKQLYGVIGN PIGHSLSPVM HNDAFEHLNM DAHYHAFLVK EEVLGEAVRG LKALGISGFN VTTPHKVAIM DYLDEIDPLA KQIGAVNTVV HKNGKLIGYN TDGIGFVRAL QSISSEPLQE KRILLLGAGG ASRAIYFSLA DAGVKEIDVA NRTVDKAKEL IAACTATVHS VALSLEKATK EQGSYDIIIQ TTTIGMHPRV EHTPLQISSL KKGTIVSDII YNPFETKILC EAKEQGAIIQ NGIDMFVYQG ALAFEMWTGC VPNIERMKQL VIRKLGG //