ID   YDIB_SALTY              Reviewed;         288 AA.
AC   Q8ZPR4;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=STM1359;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RA   Minasov G., Light S.H., Halavaty A., Shuvalova L., Dubrovska I., Winsor J.,
RA   Papazisi L., Anderson W.F.;
RT   "1.95 angstrom crystal structure of shikimate 5-dehydrogenase (AroE) from
RT   Salmonella enterica subsp. enterica serovar Typhimurium in complex with
RT   NAD.";
RL   Submitted (JUL-2011) to the PDB data bank.
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; AE006468; AAL20284.1; -; Genomic_DNA.
DR   RefSeq; NP_460325.1; NC_003197.2.
DR   RefSeq; WP_000383490.1; NC_003197.2.
DR   PDB; 3T4E; X-ray; 1.95 A; A/B=1-288.
DR   PDBsum; 3T4E; -.
DR   AlphaFoldDB; Q8ZPR4; -.
DR   SMR; Q8ZPR4; -.
DR   STRING; 99287.STM1359; -.
DR   PaxDb; 99287-STM1359; -.
DR   GeneID; 1252877; -.
DR   KEGG; stm:STM1359; -.
DR   PATRIC; fig|99287.12.peg.1443; -.
DR   HOGENOM; CLU_044063_4_4_6; -.
DR   OMA; SIFARND; -.
DR   PhylomeDB; Q8ZPR4; -.
DR   BioCyc; SENT99287:STM1359-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Quinate/shikimate dehydrogenase"
FT                   /id="PRO_0000136072"
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                   ECO:0000269|Ref.2"
FT   BINDING         155..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT                   ECO:0000269|Ref.2"
FT   BINDING         205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT                   ECO:0000269|Ref.2"
FT   BINDING         232..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT                   ECO:0000269|Ref.2"
FT   BINDING         255
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT                   ECO:0000269|Ref.2"
FT   STRAND          8..15
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           71..74
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           83..88
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           106..117
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           134..145
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          149..155
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           160..174
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           187..196
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           240..247
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   STRAND          251..253
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           255..271
FT                   /evidence="ECO:0007829|PDB:3T4E"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:3T4E"
SQ   SEQUENCE   288 AA;  31337 MW;  42984154DE6BB962 CRC64;
     MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPYTYM AFEVDNTTFA SAIEGLKALK
     MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF
     DMRGKTMVLL GAGGAATAIG AQAAIEGIKE IKLFNRKDDF FEKAVAFAKR VNENTDCVVT
     VTDLADQHAF TEALASADIL TNGTKVGMKP LENESLIGDV SLLRPELLVT ECVYNPHMTK
     LLQQAQQAGC KTIDGYGMLL WQGAEQFELW TGKAFPLDYV KQVMGFTA
//