ID AROE_ACIET Reviewed; 282 AA. AC B9MFP8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 04-NOV-2026, entry version 90. 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}; GN OrderedLocusNames=Dtpsy_2966; OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Comamonadaceae; Diaphorobacter. OX NCBI_TaxID=535289; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TPSY; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.; RT "Complete sequence of Diaphorobacter sp. TPSY."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. 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=shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+); 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; CP001392; ACM34399.1; -; Genomic_DNA. DR RefSeq; WP_015914251.1; NC_011992.1. DR AlphaFoldDB; B9MFP8; -. DR SMR; B9MFP8; -. DR KEGG; dia:Dtpsy_2966; -. DR eggNOG; COG0169; Bacteria. DR HOGENOM; CLU_044063_2_1_4; -. DR OMA; AAAYKIW; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000000450; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro. DR CDD; cd01065; NAD_bind_Shikimate_DH; 1. DR FunFam; 3.40.50.10860:FF:000006; Shikimate dehydrogenase (NADP(+)); 1. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. 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 NCBIfam; NF001310; aroE; 1. DR NCBIfam; TIGR00507; aroE; 1. DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1. DR Pfam; PF18317; SDH_C; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..282 FT /note="Shikimate dehydrogenase (NADP(+))" FT /id="PRO_1000124882" FT ACT_SITE 69 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 18..20 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 65 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 81 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 90 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 105 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 130..134 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 154..159 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 222 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 224 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 245 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" SQ SEQUENCE 282 AA; 29172 MW; F0C0C0973ABF4CB3 CRC64; MTAAADLYCV MGNPIAHSRS PWIHARFAQL TDQSLHYERR LVPLDGFAQA LQSFAAEGGR GCNITVPFKL EAAQLATTRS ERVQLAGAAN TLVFDGGSIH ADNTDGLGLV ADITQGAGVP LAGRDVLLVG AGGAAAGVLG PLLRQHPRRI AVVNRTPARA QALVDSHAAL AALQKTELLA LDMQAPGADF DVIINATASS LEGGPVPVPA SVLRPGSLAY DMMYGPAAQP FLDWASAHGA TARDGLGMLV EQAAEAFLLW RGVRPPSAPV LQELRAAIAA GA //