ID AROB_ENTFO Reviewed; 358 AA.
AC F2MTI0; Q9ANY9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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}; OrderedLocusNames=OG1RF_11282;
OS Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=474186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=11722738; DOI=10.1046/j.1365-2958.2001.02638.x;
RA Huycke M.M., Moore D., Joyce W., Wise P., Shepard L., Kotake Y.,
RA Gilmore M.S.;
RT "Extracellular superoxide production by Enterococcus faecalis requires
RT demethylmenaquinone and is attenuated by functional terminal quinol
RT oxidases.";
RL Mol. Microbiol. 42:729-740(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110;
RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J.,
RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G.,
RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., Shang Y.,
RA Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., Chowdhury S.,
RA Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., Weinstock G.M.;
RT "Large scale variation in Enterococcus faecalis illustrated by the genome
RT analysis of strain OG1RF.";
RL Genome Biol. 9:R110.1-R110.16(2008).
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}.
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DR EMBL; AF318277; AAG53675.1; -; Genomic_DNA.
DR EMBL; CP002621; AEA93969.1; -; Genomic_DNA.
DR RefSeq; WP_002357583.1; NZ_JAJPFL010000002.1.
DR AlphaFoldDB; F2MTI0; -.
DR SMR; F2MTI0; -.
DR GeneID; 60893868; -.
DR KEGG; efi:OG1RF_11282; -.
DR HOGENOM; CLU_001201_0_1_9; -.
DR UniPathway; UPA00053; UER00085.
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: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; IEA:UniProtKB-UniPathway.
DR CDD; cd08195; DHQS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
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 NCBIfam; TIGR01357; aroB; 1.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc.
FT CHAIN 1..358
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000412116"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 129..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 169..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT CONFLICT 80
FT /note="T -> I (in Ref. 1; AAG53675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38938 MW; 31A85256B7CDA423 CRC64;
MKLTVTLPTH SYDLTIETGA LDKIGTWVRS LWQPQRVAII TDETVNKLYG AAVEKELQAA
GFETSLIAVA AGEQSKSLET AQLLYDFLAE QQLTRSDGLI ALGGGVVGDL AGFVASTYMR
GIHFLQVPTT LLAQVDSSIG GKTAVNTKKA KNLVGTFAQP DGVLIDPNTL KTLEPRRVRE
GIAEIVKSAA IADVELWHRL SSLENEQDLV AHAEEIITAC CKIKRDVVEE DELDLGLRLI
LNFGHTIGHA LENTAGYGVI AHGEGVSLGM IQITQVAEQQ GLSPLGTTQE LVTMLEKFHL
PVTTDRWSEE RLYQAITHDK KTRGGQIKII VLEKIGQAKI VSLPTEEIRA FLNREGGI
//
