ID AROE_PELPB Reviewed; 283 AA. AC B4SD14; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 02-SEP-2026, entry version 96. 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=Ppha_2066; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales; OC Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J., RA Bryant D.A., Richardson P.; RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."; RL Submitted (JUN-2008) 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; CP001110; ACF44273.1; -; Genomic_DNA. DR RefSeq; WP_012508752.1; NC_011060.1. DR AlphaFoldDB; B4SD14; -. DR SMR; B4SD14; -. DR STRING; 324925.Ppha_2066; -. DR KEGG; pph:Ppha_2066; -. DR eggNOG; COG0169; Bacteria. DR HOGENOM; CLU_044063_4_1_10; -. DR OrthoDB; 9792692at2; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000002724; 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 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 NCBIfam; TIGR00507; aroE; 1. DR NCBIfam; NF001319; PRK00258.3-3; 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; 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..283 FT /note="Shikimate dehydrogenase (NADP(+))" FT /id="PRO_1000100128" FT ACT_SITE 70 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 66 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 91 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 106 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 225 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 227 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 248 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" SQ SEQUENCE 283 AA; 30466 MW; 9E1B7DA5EA2A3CF0 CRC64; MTKSTKILGL IGRAVDYSYS PLIHNTACRL LGLSYHYTVF NIADPSMIPD ALRGAKALGI AGFNVTIPYK KSVVPFLDAL SAEAASIQAV NTIVNEGGKL TGHNTDIAGF AAPLLPYRES IRGKTLSIFG AGGAALAAIE AFIRFFSPKE ILLFVRNPEK ASLLLEESGH DKSAPVRILC SDNPEIIREC RVIVNATPIG TRGNNDSPLP LDRELLHPGQ IVYDMVYNPL DTPLLLAAQK AGAATISGIE MLIGQAEHSF TLWTGMQMPV KAVKESLLQE IQQ //