ID C7LEQ4_BRUMC Unreviewed; 378 AA. AC C7LEQ4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 04-NOV-2026, entry version 92. DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684, ECO:0000256|HAMAP-Rule:MF_00110}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031, ECO:0000256|HAMAP-Rule:MF_00110}; GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110, GN ECO:0000313|EMBL:ACU48989.1}; GN OrderedLocusNames=BMI_I2049 {ECO:0000313|EMBL:ACU48989.1}; OS Brucella microti (strain BCCN 7-01 / CAPM 6434 / CCM 4915). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU48989.1, ECO:0000313|Proteomes:UP000002188}; RN [1] {ECO:0000313|EMBL:ACU48989.1, ECO:0000313|Proteomes:UP000002188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU48989.1, RC ECO:0000313|Proteomes:UP000002188}; RX PubMed=19653890; DOI=10.1186/1471-2164-10-352; RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.; RT "Brucella microti: the genome sequence of an emerging pathogen."; RL BMC Genomics 10:352-352(2009). CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate CC 7-phosphate (DAHP) to dehydroquinate (DHQ). CC {ECO:0000256|ARBA:ARBA00003485, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001393, ECO:0000256|HAMAP- CC Rule:MF_00110}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110}; CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+) CC or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|ARBA:ARBA00001911, ECO:0000256|HAMAP- CC Rule:MF_00110}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 2/7. {ECO:0000256|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412, CC ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001578; ACU48989.1; -; Genomic_DNA. DR RefSeq; WP_004684507.1; NC_013119.1. DR AlphaFoldDB; C7LEQ4; -. DR SMR; C7LEQ4; -. DR GeneID; 55591600; -. DR KEGG; bmr:BMI_I2049; -. DR HOGENOM; CLU_001201_0_2_5; -. DR OMA; AAACWMR; -. DR PhylomeDB; C7LEQ4; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000002188; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid biosynthetic process; IEA:InterPro. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd08195; DHQS; 1. DR FunFam; 3.40.50.1970:FF:000007; Pentafunctional AROM polypeptide; 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; IPR050071; Dehydroquinate_synthase. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030963; DHQ_synth_fam. DR InterPro; IPR030960; DHQS/DOIS_N. DR InterPro; IPR056179; DHQS_C. 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 Pfam; PF24621; DHQS_C; 1. DR PIRSF; PIRSF001455; DHQ_synth; 1. DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00110}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00110}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00110}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00110}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00110}; Reference proteome {ECO:0000313|Proteomes:UP000002188}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}. FT DOMAIN 77..189 FT /note="3-dehydroquinate synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 191..340 FT /note="3-dehydroquinate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF24621" FT BINDING 115..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 139..140 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 161 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 275 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" SQ SEQUENCE 378 AA; 39839 MW; 940948AD815BEB00 CRC64; MNAPTTVADS VTVPVSLGDR SYDILIGKGL VERAGEEVAK RLKGVRVAIV TDENVAAVHL ERLQASFARA GIDSTPVIVA PGEKSKSFAT LETVTNAILA AKLERGDAVV ALGGGVVGDL SGFVAGIVRR GMNFVQMPTS LLAQVDSSVG GKTGINTAHG KNLVGVFNQP QLVLADTQVL DTLSPREFRA GYAEVAKYGL IDRPDFFAWL EANWQEVFSG GAARTKAIAE SCRSKAAVVA RDERETGDRA LLNLGHTFGH ALESATGYDS SRLVHGEGVA IGMALAYRFS ARMNLAGIEA AERVEAHLKA VGLPVSLAEV PGGLPPAEKL MDYIAQDKKV TRGTLTFILT HGIGQSFIAK DVPPAAVLEF LKERLAIA //