AROE_CORGB
ID AROE_CORGB Reviewed; 283 AA.
AC A4QB65;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Quinate/shikimate dehydrogenase (NAD(+)) {ECO:0000303|PubMed:19376919};
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=cgR_0495;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RC STRAIN=R;
RX PubMed=19376919; DOI=10.1128/aem.00163-09;
RA Teramoto H., Inui M., Yukawa H.;
RT "Regulation of expression of genes involved in quinate and shikimate
RT utilization in Corynebacterium glutamicum.";
RL Appl. Environ. Microbiol. 75:3461-3468(2009).
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. {ECO:0000269|PubMed:19376919}.
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:0000303|PubMed:19376919}.
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route).
CC {ECO:0000303|PubMed:19376919}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9X5C9}.
CC -!- INDUCTION: By shikimate, quinate and QsuR.
CC {ECO:0000269|PubMed:19376919}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow with
CC quinate and shikimate as substrate but do not affect growth with
CC glucose. {ECO:0000269|PubMed:19376919}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AP009044; BAF53462.1; -; Genomic_DNA.
DR RefSeq; WP_003860437.1; NC_009342.1.
DR AlphaFoldDB; A4QB65; -.
DR SMR; A4QB65; -.
DR EnsemblBacteria; BAF53462; BAF53462; cgR_0495.
DR KEGG; cgt:cgR_0495; -.
DR HOGENOM; CLU_044063_4_3_11; -.
DR OMA; HEHEGDA; -.
DR PhylomeDB; A4QB65; -.
DR BRENDA; 1.1.1.25; 960.
DR BRENDA; 1.1.1.282; 960.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000006698; 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; IMP:UniProtKB.
DR GO; GO:0019632; P:shikimate metabolic process; IMP: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; 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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW Oxidoreductase.
FT CHAIN 1..283
FT /note="Quinate/shikimate dehydrogenase (NAD(+))"
FT /id="PRO_0000351451"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 17..19
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 17
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 69
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 69
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 73
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 73
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 94
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 94
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 110
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 110
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 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 163
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 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 258
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
FT BINDING 258
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000250|UniProtKB:Q9X5C9"
SQ SEQUENCE 283 AA; 29710 MW; 82490DA71877A4A2 CRC64;
MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD LKTLLDAALY
LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA NGHTTGHNTD VSGFGRGMEE
GLPNAKLDSV VQVGAGGVGN AVAYALVTHG VQKLQVADLD TSRAQALADV INNAVGREAV
VGVDARGIED VIAAADGVVN ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA
ARALGCETLD GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL
