AROB_CORGL
ID AROB_CORGL Reviewed; 365 AA.
AC Q9X5D2; O87382; Q8NQ31;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110};
GN OrderedLocusNames=Cgl1621, cg1827;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Burke K.G., Joy J., O'Donohue M.R., Dunican L.K.;
RT "Genetic aspects of the prechorismate pathway in Corynebacterium
RT glutamicum.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=10907426; DOI=10.1139/w99-076;
RA Han M.A., Lee H.S., Cheon C.I., Min K.H., Lee M.-S.;
RT "Cloning and analysis of the aroB gene encoding dehydroquinate synthase
RT from Corynebacterium glutamicum.";
RL Can. J. Microbiol. 45:885-890(1999).
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=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 [4]
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).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-
CC Rule:MF_00110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000305}.
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DR EMBL; AF124600; AAD27840.1; -; Genomic_DNA.
DR EMBL; AF053071; AAC35272.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99014.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21630.1; -; Genomic_DNA.
DR RefSeq; NP_600835.1; NC_003450.3.
DR RefSeq; WP_011014486.1; NC_006958.1.
DR AlphaFoldDB; Q9X5D2; -.
DR SMR; Q9X5D2; -.
DR STRING; 196627.cg1827; -.
DR KEGG; cgb:cg1827; -.
DR KEGG; cgl:Cgl1621; -.
DR PATRIC; fig|196627.13.peg.1583; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_3_11; -.
DR OMA; YGVIWDA; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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_00110; DHQ_synthase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..365
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140734"
FT BINDING 75..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 109..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 133..134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT CONFLICT 35
FT /note="A -> Q (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..40
FT /note="ESGAE -> NQAR (in Ref. 1; AAD27840 and 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> R (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> S (in Ref. 1; AAD27840)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> R (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..91
FT /note="CWDE -> V (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="R -> G (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="A -> R (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..246
FT /note="LKESSLR -> SKNLAC (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..275
FT /note="AVAV -> VCS (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="Missing (in Ref. 2; AAC35272)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..365
FT /note="AISH -> QSATKC (in Ref. 1; AAD27840 and 2;
FT AAC35272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 38858 MW; 72CBB0DE3BBDDE18 CRC64;
MSAVQIFNTV HVNGSSPYDV HIGSGLNELI VQRAAESGAE QVAILHQPSM DDIASELDAA
LVAAGLKVLH LNVPDAENGK SLEVAGQCWD ELGGAAFGRR DIVIGLGGGA ATDLAGFVAA
AWMRGVRVIQ VPTTLLAMVD AAVGGKTGIN TAAGKNLVGA FHEPDAVFID TDRLATLPDA
EIIAGSAEII KTGFIADPEI LRLYETDPAA CLKKEVEGSH LPELIWRSVT VKGSVVGQDL
KESSLREILN YGHTFAHAVE LRENFRWRHG NAVAVGMMFI ANLSHKLGLI DAPLLERHRS
ILAAIGLPTS YEGGAFDELY DGMTRDKKNR DGNIRFVALT AVGEVTRIEG PSKQDLQSAY
EAISH
