AROB_ECOLI
ID AROB_ECOLI Reviewed; 362 AA.
AC P07639; Q2M754;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000305};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000305};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110};
GN OrderedLocusNames=b3389, JW3352;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3009224; DOI=10.1016/0014-5793(86)80501-4;
RA Millar G., Coggins J.R.;
RT "The complete amino acid sequence of 3-dehydroquinate synthase of
RT Escherichia coli K12.";
RL FEBS Lett. 200:11-17(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-362.
RC STRAIN=K12;
RX PubMed=2549371; DOI=10.1007/bf00330946;
RA Jonczyk P., Hines R., Smith D.W.;
RT "The Escherichia coli dam gene is expressed as a distal gene of a new
RT operon.";
RL Mol. Gen. Genet. 217:85-96(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, KINETIC PARAMETERS, AND SUBUNIT.
RX PubMed=2514789; DOI=10.1021/bi00445a009;
RA Bender S.L., Mehdi S., Knowles J.R.;
RT "Dehydroquinate synthase: the role of divalent metal cations and of
RT nicotinamide adenine dinucleotide in catalysis.";
RL Biochemistry 28:7555-7560(1989).
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, ECO:0000269|PubMed:2514789}.
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 ECO:0000269|PubMed:2514789};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000269|PubMed:2514789};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000269|PubMed:2514789};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000269|PubMed:2514789};
CC Note=Binds 1 divalent metal cation per subunit. Displays higher
CC activity with Co(2+), however, Zn(2+) may be the physiological metal
CC cofactor. {ECO:0000269|PubMed:2514789};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH
CC 6.5) {ECO:0000269|PubMed:2514789};
CC KM=5.5 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH
CC 8.5) {ECO:0000269|PubMed:2514789};
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2514789}.
CC -!- INTERACTION:
CC P07639; P68646: fixX; NbExp=2; IntAct=EBI-550843, EBI-1113234;
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; X03867; CAA27495.1; -; Genomic_DNA.
DR EMBL; Z19601; CAA79666.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58186.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76414.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77902.1; -; Genomic_DNA.
DR EMBL; X15162; CAA33252.1; -; Genomic_DNA.
DR PIR; A24863; SYECQ.
DR RefSeq; NP_417848.1; NC_000913.3.
DR RefSeq; WP_000439848.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P07639; -.
DR SMR; P07639; -.
DR BioGRID; 4259296; 55.
DR BioGRID; 852236; 5.
DR DIP; DIP-9150N; -.
DR IntAct; P07639; 9.
DR STRING; 511145.b3389; -.
DR BindingDB; P07639; -.
DR ChEMBL; CHEMBL3554; -.
DR jPOST; P07639; -.
DR PaxDb; P07639; -.
DR PRIDE; P07639; -.
DR EnsemblBacteria; AAC76414; AAC76414; b3389.
DR EnsemblBacteria; BAE77902; BAE77902; BAE77902.
DR GeneID; 947927; -.
DR KEGG; ecj:JW3352; -.
DR KEGG; eco:b3389; -.
DR PATRIC; fig|1411691.4.peg.3341; -.
DR EchoBASE; EB0072; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_2_6; -.
DR InParanoid; P07639; -.
DR OMA; YGVIWDA; -.
DR PhylomeDB; P07639; -.
DR BioCyc; EcoCyc:AROB-MON; -.
DR BioCyc; MetaCyc:AROB-MON; -.
DR BRENDA; 4.2.3.4; 2026.
DR SABIO-RK; P07639; -.
DR UniPathway; UPA00053; UER00085.
DR PRO; PR:P07639; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IDA:EcoCyc.
DR GO; GO:0070403; F:NAD+ binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140737"
FT BINDING 71..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
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 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ SEQUENCE 362 AA; 38881 MW; F67496010D5C9182 CRC64;
MERIVVTLGE RSYPITIASG LFNEPASFLP LKSGEQVMLV TNETLAPLYL DKVRGVLEQA
GVNVDSVILP DGEQYKSLAV LDTVFTALLQ KPHGRDTTLV ALGGGVVGDL TGFAAASYQR
GVRFIQVPTT LLSQVDSSVG GKTAVNHPLG KNMIGAFYQP ASVVVDLDCL KTLPPRELAS
GLAEVIKYGI ILDGAFFNWL EENLDALLRL DGPAMAYCIR RCCELKAEVV AADERETGLR
ALLNLGHTFG HAIEAEMGYG NWLHGEAVAA GMVMAARTSE RLGQFSSAET QRIITLLKRA
GLPVNGPREM SAQAYLPHML RDKKVLAGEM RLILPLAIGK SEVRSGVSHE LVLNAIADCQ
SA
