AROE_COREF
ID AROE_COREF Reviewed; 284 AA.
AC Q8FSF0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Quinate/shikimate dehydrogenase (NAD(+)) {ECO:0000250|UniProtKB:Q9X5C9};
DE Short=QSDH {ECO:0000250|UniProtKB:Q9X5C9};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q9X5C9};
DE EC=1.1.1.24 {ECO:0000250|UniProtKB:Q9X5C9};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; OrderedLocusNames=CE0443;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC to the biosynthesis of aromatic amino acids, and plays a key role in
CC the quinate degradation pathway. Catalyzes the NAD(+)-dependent
CC oxidation of both quinate and shikimate to 3-dehydroquinate and 3-
CC dehydroshikimate, respectively. It can only use NAD.
CC {ECO:0000250|UniProtKB:Q9X5C9}.
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; EC=1.1.1.24;
CC Evidence={ECO:0000250|UniProtKB:Q9X5C9};
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 Evidence={ECO:0000250|UniProtKB:Q9X5C9};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000250|UniProtKB:Q9X5C9, ECO:0000255|HAMAP-Rule:MF_00222}.
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route).
CC {ECO:0000250|UniProtKB:Q9X5C9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9X5C9, ECO:0000255|HAMAP-
CC Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000250|UniProtKB:Q9X5C9, ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; BA000035; BAC17253.1; -; Genomic_DNA.
DR RefSeq; WP_006770320.1; NZ_GG700690.1.
DR AlphaFoldDB; Q8FSF0; -.
DR SMR; Q8FSF0; -.
DR STRING; 196164.23492279; -.
DR EnsemblBacteria; BAC17253; BAC17253; BAC17253.
DR KEGG; cef:CE0443; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_3_11; -.
DR OMA; HEHEGDA; -.
DR OrthoDB; 1054867at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000001409; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0052734; F:shikimate 3-dehydrogenase (NAD+) activity; IEA:RHEA.
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; ISS:UniProtKB.
DR GO; GO:0019632; P:shikimate metabolic process; ISS:UniProtKB.
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; IPR005097; Sacchrp_dh_NADP.
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; PF03435; Sacchrp_dh_NADP; 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;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..284
FT /note="Quinate/shikimate dehydrogenase (NAD(+))"
FT /id="PRO_0000325114"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 18..20
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 18
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 70
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 70
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 74
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 74
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 95
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 95
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 111
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 111
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 137..138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 203..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 259
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 259
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
SQ SEQUENCE 284 AA; 29938 MW; 7179FA02CF0DE537 CRC64;
MNHDSILLGL IGEDISLSRT PAMHEAEGLA QGAATVYRRI DTLTDRARGR SLQELLDAAR
STGFNGLNIT HPYKQAVLPL LDEVSEQAAQ LGAVNTVVIG EDGRTSGHNT DVTGFARGLE
EGLPDATMTT VVQVGAGGVG NAVAYSLVTH GVEQLQVADL DPARAQALAD AINSAIGREA
VHGIDARGVE EAIAAADGVV NATPMGMLAH PGTAFDTSCL TPHHWVGDVV YMPIETQLLK
DARALGCRTL DGTRMAIHQA VDAFRLFTGL EPDVERMRAT FLSL
