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YDIB_SALHS
ID   YDIB_SALHS              Reviewed;         288 AA.
AC   B4TGJ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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}; OrderedLocusNames=SeHA_C1490;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
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DR   EMBL; CP001120; ACF69023.1; -; Genomic_DNA.
DR   RefSeq; WP_000383488.1; NC_011083.1.
DR   AlphaFoldDB; B4TGJ7; -.
DR   SMR; B4TGJ7; -.
DR   KEGG; seh:SeHA_C1490; -.
DR   HOGENOM; CLU_044063_4_4_6; -.
DR   OMA; SIFARND; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001866; Chromosome.
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: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   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   HAMAP; MF_01578; Shikimate_DH_YdiB; 1.
DR   InterPro; IPR046346; Aminiacid_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; PTHR21089; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 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_1000147559"
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;  31319 MW;  0E389500DB2EAEDF CRC64;
     MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPYTYM AFEVDNTTFA SAIEGLKALK
     MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF
     DIRGKTMVLL GAGGAATAIG AQAAIEGIKE IKLFNRKDDF FEKAVAFAKR VNENTDCVVT
     VTDLADQHAF TEALASADIL TNGTKVGMKP LENESLIGDV SLLRPELLVT ECVYNPHMTK
     LLQQAQQAGC KTIDGYGMLL WQGAEQFELW TGKAFPLDYV KQVMGFTA
 
 
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