YDIB_ECO57
ID YDIB_ECO57 Reviewed; 288 AA.
AC Q8X5Y4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=Z2720, ECs2399;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56679.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35822.1; -; Genomic_DNA.
DR PIR; C85777; C85777.
DR PIR; G90928; G90928.
DR RefSeq; NP_310426.1; NC_002695.1.
DR RefSeq; WP_000383479.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; Q8X5Y4; -.
DR SMR; Q8X5Y4; -.
DR STRING; 155864.EDL933_2649; -.
DR EnsemblBacteria; AAG56679; AAG56679; Z2720.
DR EnsemblBacteria; BAB35822; BAB35822; ECs_2399.
DR GeneID; 912660; -.
DR KEGG; ece:Z2720; -.
DR KEGG; ecs:ECs_2399; -.
DR PATRIC; fig|386585.9.peg.2512; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_4_6; -.
DR OMA; SIFARND; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..288
FT /note="Quinate/shikimate dehydrogenase"
FT /id="PRO_0000136070"
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; 31226 MW; F5D4DAED958FB1E4 CRC64;
MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPFTYM AFEVDNDSFP GAIEGLKALK
MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF
DIKGKTMVLL GAGGASTAIG AQGAIEGLKE IKLFNRRDKF FDKALAFAQR VNENTDCVVT
VTDLADQQAF AEALASADIL TNGTKVGMKP LENKSLVNDI SLLHPGLLVT ECVYNPHMTK
LLQQAQQAGC KTIDGYGMLL WQGAEQFTLW TGKDFPLEYV KQVMGFGA
