ID AROE_CORGL Reviewed; 283 AA.
AC Q9X5C9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Quinate/shikimate dehydrogenase (NAD(+)) {ECO:0000303|PubMed:18566515};
DE Short=QSDH {ECO:0000303|PubMed:23929881};
DE EC=1.1.1.- {ECO:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881};
DE EC=1.1.1.24 {ECO:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222};
GN Synonyms=qsuD {ECO:0000303|PubMed:23929881};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Joy J., O'Donohue M., Dunican L.K.;
RT "The cloning and phylogenetic analysis of the 3-dehydroquinase gene from
RT Corynebacterium glutamicum.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4] {ECO:0007744|PDB:2NLO}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18566515; DOI=10.1107/s090744490801411x;
RA Schoepe J., Niefind K., Schomburg D.;
RT "1.6 Angstroms structure of an NAD(+)-dependent quinate dehydrogenase from
RT Corynebacterium glutamicum.";
RL Acta Crystallogr. D 64:803-809(2008).
RN [5] {ECO:0007744|PDB:3JYO, ECO:0007744|PDB:3JYP, ECO:0007744|PDB:3JYQ}
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS)IN COMPLEX WITH SHIKIMATE;
RP (-)-QUINATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=23929881; DOI=10.1515/hsz-2013-0170;
RA Hoppner A., Schomburg D., Niefind K.;
RT "Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from
RT Corynebacterium glutamicum enable new insights in substrate and cofactor
RT binding, specificity, and discrimination.";
RL Biol. Chem. 394:1505-1516(2013).
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:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881}.
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:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881};
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:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for NAD (with 16 mM quinate at pH 7.5)
CC {ECO:0000269|PubMed:23929881};
CC KM=0.28 mM for NAD (with 16 mM quinate at pH 9)
CC {ECO:0000269|PubMed:23929881};
CC KM=0.46 mM for NAD (with 60 mM shikimate at pH 9)
CC {ECO:0000269|PubMed:23929881};
CC KM=0.87 mM for NAD (with 60 mM shikimate at pH 7.5)
CC {ECO:0000269|PubMed:23929881};
CC KM=1.56 mM for quinate (at pH 7.5) {ECO:0000269|PubMed:23929881};
CC KM=2.37 mM for quinate (at pH 9) {ECO:0000269|PubMed:23929881};
CC KM=10.16 mM for shikimate(at pH 7.5) {ECO:0000269|PubMed:23929881};
CC KM=10.2 mM for quinate {ECO:0000269|PubMed:18566515};
CC KM=46.6 mM for shikimate {ECO:0000269|PubMed:18566515};
CC KM=53.8 mM for shikimate(at pH 10) {ECO:0000269|PubMed:23929881};
CC Note=The catalytic efficiency with quinate is 3.3-fold higher than
CC that with shikimate. With NADP(+) instead of NAD(+) as cosubstrate,
CC activity decreases by more than 300-fold with either shikimate or
CC quinate as a substrate. {ECO:0000269|PubMed:18566515,
CC ECO:0000269|PubMed:23929881};
CC pH dependence:
CC Optimum pH is 9-10. {ECO:0000269|PubMed:18566515,
CC ECO:0000269|PubMed:23929881};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000305}.
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route).
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222,
CC ECO:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881}.
CC -!- INDUCTION: By shikimate, quinate and QsuR.
CC {ECO:0000250|UniProtKB:A4QB65}.
CC -!- MISCELLANEOUS: Has a different substrate and cosubstrate specificities
CC relative to all other known bacterial shikimate/quinate dehydrogenases.
CC {ECO:0000269|PubMed:18566515, ECO:0000269|PubMed:23929881}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AF124518; AAD30993.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97817.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19140.1; -; Genomic_DNA.
DR RefSeq; NP_599671.1; NC_003450.3.
DR RefSeq; WP_011013640.1; NC_006958.1.
DR PDB; 2NLO; X-ray; 1.64 A; A=1-283.
DR PDB; 3JYO; X-ray; 1.00 A; A=1-283.
DR PDB; 3JYP; X-ray; 1.16 A; A=1-283.
DR PDB; 3JYQ; X-ray; 1.16 A; A=1-283.
DR PDBsum; 2NLO; -.
DR PDBsum; 3JYO; -.
DR PDBsum; 3JYP; -.
DR PDBsum; 3JYQ; -.
DR AlphaFoldDB; Q9X5C9; -.
DR SMR; Q9X5C9; -.
DR STRING; 196627.cg0504; -.
DR KEGG; cgb:cg0504; -.
DR KEGG; cgl:Cgl0424; -.
DR PATRIC; fig|196627.13.peg.423; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_3_11; -.
DR OrthoDB; 9776868at2; -.
DR BioCyc; CORYNE:G18NG-9981-MONOMER; -.
DR BioCyc; MetaCyc:MONOMER-15330; -.
DR BRENDA; 1.1.1.24; 960.
DR BRENDA; 1.1.1.25; 960.
DR BRENDA; 1.1.1.282; 960.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; Q9X5C9; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IDA: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: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; IDA:UniProtKB.
DR GO; GO:0019632; P:shikimate metabolic process; IDA:UniProtKB.
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 InterPro; IPR046346; Aminoacid_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; SHIKIMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21089:SF34; SHIKIMATE DEHYDROGENASE (NADP(+)); 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; Oxidoreductase; Reference proteome.
FT CHAIN 1..283
FT /note="Quinate/shikimate dehydrogenase (NAD(+))"
FT /id="PRO_0000136001"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:23929881"
FT BINDING 17..19
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 17
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 69
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 69
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 73
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 73
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 94
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 94
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 110
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 110
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 137..138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:23929881, ECO:0007744|PDB:3JYO,
FT ECO:0007744|PDB:3JYP, ECO:0007744|PDB:3JYQ"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYO, ECO:0007744|PDB:3JYP,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYO, ECO:0007744|PDB:3JYP,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 203..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYO, ECO:0007744|PDB:3JYP,
FT ECO:0007744|PDB:3JYQ"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP, ECO:0007744|PDB:3JYQ"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:23929881, ECO:0007744|PDB:3JYO,
FT ECO:0007744|PDB:3JYP, ECO:0007744|PDB:3JYQ"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:23929881, ECO:0007744|PDB:3JYO,
FT ECO:0007744|PDB:3JYP, ECO:0007744|PDB:3JYQ"
FT BINDING 258
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYP"
FT BINDING 258
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:23929881,
FT ECO:0007744|PDB:3JYQ"
FT CONFLICT 29
FT /note="A -> P (in Ref. 1; AAD30993)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..143
FT /note="AGGVGNAVA -> RRRRKRSR (in Ref. 1; AAD30993)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="Missing (in Ref. 1; AAD30993)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..273
FT /note="DV -> T (in Ref. 1; AAD30993)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3JYO"
FT TURN 44..48
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3JYO"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:3JYO"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2NLO"
FT HELIX 252..267
FT /evidence="ECO:0007829|PDB:3JYO"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:3JYO"
SQ SEQUENCE 283 AA; 29697 MW; 2DBCE25D186DAF74 CRC64;
MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD LKTLLDAALY
LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA TGHTTGHNTD VSGFGRGMEE
GLPNAKLDSV VQVGAGGVGN AVAYALVTHG VQKLQVADLD TSRAQALADV INNAVGREAV
VGVDARGIED VIAAADGVVN ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA
ARALGCETLD GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL
//
