ID   AROE_CLOB6              Reviewed;         258 AA.
AC   C3L127;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=CLJ_B2770;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-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=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   ---------------------------------------------------------------------------
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; CP001083; ACQ52177.1; -; Genomic_DNA.
DR   RefSeq; WP_012720593.1; NC_012658.1.
DR   AlphaFoldDB; C3L127; -.
DR   SMR; C3L127; -.
DR   EnsemblBacteria; ACQ52177; ACQ52177; CLJ_B2770.
DR   KEGG; cbi:CLJ_B2770; -.
DR   HOGENOM; CLU_044063_4_1_9; -.
DR   OMA; FGNPIKH; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000002333; Chromosome.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   PANTHER; PTHR21089; PTHR21089; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..258
FT                   /note="Shikimate dehydrogenase (NADP(+))"
FT                   /id="PRO_1000204258"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         14..16
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         61
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         86
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         101
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         125..129
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         213
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         234
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   258 AA;  29725 MW;  D9B7CDD09D16F218 CRC64;
     MYTTGLIGKN INYSESPEIH NNYYKKNNIP FFYKIFNLKQ DQIDDFIKNL HKNNIKGFNV
     TIPYKETILQ YLNDIVYPAD KIGAVNTVAV QEDKLIGYNT DYIGFIKSLQ YYNIQVKNFK
     CLIIGSGGSA KCIYYALKEL NARDICIVSR NPEKARLKFE KKVKILNIKD ENKLDRYDLI
     VNCTPIGGPN FKEQKPIELK EIKKNCVVYD LNYTPKRSKL LKEAKENGAF IINGEKMLIF
     QAYSAIGLWC LNGIKGGR