ID AROE_MARN8 Reviewed; 275 AA. AC A1TWN6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 04-NOV-2026, entry version 111. 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=Maqu_0048; OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter OS aquaeolei). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Marinobacteraceae; Marinobacter. OX NCBI_TaxID=351348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8; RX PubMed=21335390; DOI=10.1128/aem.01866-10; RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A., RA Edwards K.J.; RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical RT 'opportunitroph'."; RL Appl. Environ. Microbiol. 77:2763-2771(2011). 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; CP000514; ABM17155.1; -; Genomic_DNA. DR RefSeq; WP_011783628.1; NC_008740.1. DR AlphaFoldDB; A1TWN6; -. DR SMR; A1TWN6; -. DR STRING; 351348.Maqu_0048; -. DR KEGG; maq:Maqu_0048; -. DR eggNOG; COG0169; Bacteria. DR HOGENOM; CLU_044063_2_1_6; -. DR OMA; AAAYKIW; -. DR OrthoDB; 9776868at2; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000000998; 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; 3.40.50.720:FF:000104; 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..275 FT /note="Shikimate dehydrogenase (NADP(+))" FT /id="PRO_1000021297" FT ACT_SITE 67 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 16..18 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 63 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 88 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 104 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 129..133 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 153..158 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 219 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 221 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 243 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" SQ SEQUENCE 275 AA; 29658 MW; 2A4EC9E294A8ED94 CRC64; MTNDLYAVVG NPISHSKSPR IHSLFAQQTG EAVEYTAIQA PLEDFAGTVH HFFDHGGKGL NITVPFKEQA WTLAEHRTHR AELAGAANTL YLDQEDQLVA DNTDGVGIVR DLRDNHGVPL KGARVLVLGA GGAVRGVLGP LLDEQPASVV VANRTVARAE ALARLFGREH SGIELSACGF EQVEGPFDLV INGTSASLKG DLPAITADVI RADTVVYDMM YSLQTTTFNQ WALDHGAVRV FDGLGMLVEQ AAEAFFVWRG VRPETSAVTE ELRTD //