ID YDIB_SALSV Reviewed; 288 AA.
AC B4TUS3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=SeSA_A1455;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
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; CP001127; ACF91472.1; -; Genomic_DNA.
DR RefSeq; WP_000383488.1; NC_011094.1.
DR AlphaFoldDB; B4TUS3; -.
DR SMR; B4TUS3; -.
DR KEGG; sew:SeSA_A1455; -.
DR HOGENOM; CLU_044063_4_4_6; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000001865; 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: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_1000147561"
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
//
