ID C0ZCD9_BREBN Unreviewed; 366 AA. AC C0ZCD9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 02-SEP-2026, entry version 98. 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:BAH43448.1}; GN OrderedLocusNames=BBR47_24710 {ECO:0000313|EMBL:BAH43448.1}; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43448.1, ECO:0000313|Proteomes:UP000001877}; RN [1] {ECO:0000313|EMBL:BAH43448.1, ECO:0000313|Proteomes:UP000001877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599 RC {ECO:0000313|Proteomes:UP000001877}; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H., RA Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|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: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 -!- 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; AP008955; BAH43448.1; -; Genomic_DNA. DR RefSeq; WP_012686155.1; NC_012491.1. DR AlphaFoldDB; C0ZCD9; -. DR STRING; 358681.BBR47_24710; -. DR KEGG; bbe:BBR47_24710; -. DR eggNOG; COG0337; Bacteria. DR HOGENOM; CLU_001201_0_2_9; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000001877; 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:0009073; P:aromatic amino acid family 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:000001; 3-dehydroquinate synthase; 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:UP000001877}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}. FT DOMAIN 73..183 FT /note="3-dehydroquinate synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01761" FT DOMAIN 185..329 FT /note="3-dehydroquinate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF24621" FT BINDING 110..114 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 134..135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 146 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 155 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" FT BINDING 268 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110" SQ SEQUENCE 366 AA; 39212 MW; D767D5EC0567B3D3 CRC64; MSVEKLTVEL GERSYEIVIG EGLLDQAAAL LVEAGIASTS KLMIVTDENV AVHYLEPLLG VLRQHGYQAH SAVIAAGEQS KSLAVYERLM TEAIDAGLDR KSAVLALGGG VVGDLAGFVA ATYMRGIDFV QMPTTLLAHD SSVGGKVAIN HPLGKNLIGA FHQPKVVIYD TIALHSLPKR EVAAGFAEVV KHGLIADAAF VDWLEDNADR LWQLDSELLG KAIEKGCAVK AAIVSQDETE QGQRALLNLG HTFGHAFEAL SAYSTLNHGE AISIGMCLAA KVAERIGFAE TGVYHRTKRM LELFHLPTAW PGNLSPEAVL EAMKRDKKTV GGKLALVLPR AIGQVEVVKN IEEELILGVM REEVEG //