ID AROE_METBU Reviewed; 269 AA. AC Q12UJ9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 26-FEB-2020, entry version 92. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; OrderedLocusNames=Mbur_1998; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L., RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N., RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T., RA Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(2009). CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads CC to the biosynthesis of aromatic amino acids. Catalyzes the reversible CC NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate CC (SA). {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00222}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00222}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000300; ABE52877.1; -; Genomic_DNA. DR RefSeq; WP_011500018.1; NC_007955.1. DR EnsemblBacteria; ABE52877; ABE52877; Mbur_1998. DR GeneID; 3996950; -. DR KEGG; mbu:Mbur_1998; -. DR eggNOG; arCOG01033; Archaea. DR eggNOG; COG0169; LUCA. DR HOGENOM; CLU_044063_4_1_2; -. DR KO; K00014; -. DR OMA; FGNPIKH; -. DR OrthoDB; 98644at2157; -. DR BioCyc; MBUR259564:G1G6A-2092-MONOMER; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR041121; SDH_C. DR InterPro; IPR011342; Shikimate_DH. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF18317; SDH_C; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00507; aroE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..269 FT /note="Shikimate dehydrogenase (NADP(+))" FT /id="PRO_1000021302" FT NP_BIND 124..128 FT /note="NADP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT NP_BIND 147..152 FT /note="NADP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT REGION 15..17 FT /note="Shikimate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT ACT_SITE 66 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 62 FT /note="Shikimate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 86 FT /note="Shikimate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 100 FT /note="Shikimate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 211 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 213 FT /note="Shikimate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 234 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" SQ SEQUENCE 269 AA; 28790 MW; B5A787654C8B454A CRC64; MKKIFAVLGD PIEHSLSPIM HNSAFEALDM DCTYHAFRVE KNDLENALQG AKAMGFGGLN LTVPLKETAL KFVDADSLAA KIGAINTIDF KDGIKGYNTD GIGAKRTIED EGVDIKDKNV LILGAGGAAR AIAFTFAEAG ANVNIANRTP ERAMQLAAEI GDAKGYGLDI VDNGLEDIDI LINTTTVGLG NSNGTLVTAE QMHSDLAVFD IVYNPLMTKL LQEAETAGAR PITGIMMLVY QGAEAFRIWT GKEPPINVMK KTVMETLDI //