ID YDIB_ECOBW Reviewed; 288 AA. AC C4ZYF4; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Quinate/shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578}; DE EC=1.1.1.282 {ECO:0000255|HAMAP-Rule:MF_01578}; DE AltName: Full=NAD-dependent shikimate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578}; GN Name=ydiB {ECO:0000255|HAMAP-Rule:MF_01578}; GN OrderedLocusNames=BWG_1506; OS Escherichia coli (strain K12 / MC4100 / BW2952). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=595496; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MC4100 / BW2952; RX PubMed=19376874; DOI=10.1128/jb.00118-09; RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., RA Wang L.; RT "Genomic sequencing reveals regulatory mutations and recombinational events RT in the widely used MC4100 lineage of Escherichia coli K-12."; RL J. Bacteriol. 191:4025-4029(2009). CC -!- FUNCTION: The actual biological function of YdiB remains unclear, nor CC is it known whether 3-dehydroshikimate or quinate represents the CC natural substrate. Catalyzes the reversible NAD-dependent reduction of CC both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate CC (SA) and quinate, respectively. It can use both NAD or NADP for CC catalysis, however it has higher catalytic efficiency with NAD. CC {ECO:0000255|HAMAP-Rule:MF_01578}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; CC Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH; CC Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578}; 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; CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH; CC Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578}; 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_01578}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01578}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01578}. 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; CP001396; ACR65393.1; -; Genomic_DNA. DR RefSeq; WP_000383469.1; NC_012759.1. DR AlphaFoldDB; C4ZYF4; -. DR SMR; C4ZYF4; -. DR GeneID; 75171755; -. DR KEGG; ebw:BWG_1506; -. DR HOGENOM; CLU_044063_4_4_6; -. DR UniPathway; UPA00053; UER00087. DR GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0052733; F:quinate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0052734; F:shikimate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. 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 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 HAMAP; MF_01578; Shikimate_DH_YdiB; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR022872; Quinate/Shikimate_DH. DR InterPro; IPR041121; SDH_C. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. 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; NAD; NADP; KW Oxidoreductase. FT CHAIN 1..288 FT /note="Quinate/shikimate dehydrogenase" FT /id="PRO_1000215614" FT BINDING 71 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 132..135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 155..158 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 205 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 232..235 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" FT BINDING 255 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578" SQ SEQUENCE 288 AA; 31228 MW; C3D1415E03820A5A CRC64; MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPFTYM AFEVDNDSFP GAIEGLKALK MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF DIKGKTMVLL GAGGASTAIG AQGAIEGLKE IKLFNRRDEF FDKALAFAQR VNENTDCVVT VTDLADQQAF AEALASADIL TNGTKVGMKP LENESLVNDI SLLHPGLLVT ECVYNPHMTK LLQQAQQAGC KTIDGYGMLL WQGAEQFTLW TGKDFPLEYV KQVMGFGA //