ID AROE_CHLTE Reviewed; 295 AA. AC Q8KBH8; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Shikimate dehydrogenase; DE EC=1.1.1.25; GN Name=aroE; OrderedLocusNames=CT1809; OS Chlorobium tepidum. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=1097; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / TLS; RX MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). 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; AE006470; AAM73030.1; -; Genomic_DNA. DR RefSeq; NP_662688.1; -. DR HSSP; Q58484; 1NVT. DR GeneID; 1008183; -. DR GenomeReviews; AE006470_GR; CT1809. DR KEGG; cte:CT1809; -. DR NMPDR; fig|194439.1.peg.1782; -. DR TIGR; CT1809; -. DR HOGENOM; Q8KBH8; -. DR OMA; Q8KBH8; VYTIFNI. DR BioCyc; CTEP194439:CT_1809-MON; -. DR BRENDA; 1.1.1.25; 189605. 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 1 295 Shikimate dehydrogenase. FT /FTId=PRO_0000135999. FT NP_BIND 132 136 NADP (By similarity). FT ACT_SITE 72 72 Proton acceptor (Potential). SQ SEQUENCE 295 AA; 31734 MW; B0A86744C10FAEA1 CRC64; MSNSQSKKIF GLIGKHVDYS WSPLIHNTGF EALGLPCVYT IFNIPSPEMI GDALKGSRAL GIAGFSVTIP YKKTVVPFLD ELSPEALSIG AVNTIVNDNG RLLGYNTDID GFAAPLLPMA ESIRNRPVCI FGNGGAALAA VEAFRLRFNP SSVLLVVRDT QKAEDMLEEY AYRDLVTIHA GREIDQPACS KLIRDCRVLV NATPVGTAGR NDHIHSILPT GHGLLHDGQI VYDMVYNPPE TPLLAEARAA GATVIAGIEM LIAQAARAFS IWTGQELPVD LVRKTVLAAI EKSEG //