ID AROE_BRUA2 Reviewed; 289 AA. AC Q2YR04; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 2. DT 27-MAR-2024, entry version 108. 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=BAB1_2070; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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 -!- SEQUENCE CAUTION: CC Sequence=CAJ12026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AM040264; CAJ12026.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_002967030.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YR04; -. DR SMR; Q2YR04; -. DR STRING; 359391.BAB1_2070; -. DR GeneID; 3788516; -. DR KEGG; bmf:BAB1_2070; -. DR HOGENOM; CLU_044063_2_0_5; -. DR PhylomeDB; Q2YR04; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000002719; Chromosome I. 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: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 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 InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. 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..289 FT /note="Shikimate dehydrogenase (NADP(+))" FT /id="PRO_0000325109" FT ACT_SITE 73 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 22..24 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 69 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 94 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 109 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 134..138 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 158..163 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 226 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 228 FT /ligand="shikimate" FT /ligand_id="ChEBI:CHEBI:36208" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" FT BINDING 249 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222" SQ SEQUENCE 289 AA; 30520 MW; B1B17A56EED18496 CRC64; MDDKSMARGR KAFVTGFPIR HSRSPLIHGF WLKELGIDGS YEAVEVKPED FSSFAASLAA NGFAGGNVTI PHKEAAYAAA ESLDEAARAI GAVNTLWLEN GRLCGGNTDA YGFAANLDAS APGWDKADRA LVLGAGGASR AVVHALLSRG VCHVSVVNRT LSRAEELAAH FGARVYAHSW DEAQALVSNA GLIVNTTALG MSGHGEGQDF PIDLTCAPKE AVATDIVYVP LRTAFLNKAE KAGLKTVDGL GMLLHQAVPG FERWFGQRPQ VTQALREHIL ADMAKAGAL //