ID AROB_SINMW Reviewed; 380 AA. AC A6UCL4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 98. 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=Smed_2564; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., RA Richardson P.; RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome."; RL Submitted (JUN-2007) 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: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=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00110}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC 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 -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|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: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 --------------------------------------------------------------------------- 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; CP000738; ABR61394.1; -; Genomic_DNA. DR AlphaFoldDB; A6UCL4; -. DR SMR; A6UCL4; -. DR STRING; 366394.Smed_2564; -. DR KEGG; smd:Smed_2564; -. DR PATRIC; fig|366394.8.peg.5756; -. DR eggNOG; COG0337; Bacteria. DR HOGENOM; CLU_001201_0_2_5; -. DR OrthoDB; 9806583at2; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000001108; 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: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; Aromatic amino acid biosynthesis; Cobalt; KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; KW Reference proteome; Zinc. FT CHAIN 1..380 FT /note="3-dehydroquinate synthase" FT /id="PRO_1000117499" FT BINDING 118..122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 142..143 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 164 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" FT BINDING 278 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110" SQ SEQUENCE 380 AA; 40577 MW; 23615227D79765CF CRC64; MKPMTSDVMP AAERKVRVDL AERSYDILIG PGLIAAAGGE IASRLKGRKM AVITDENVAP RYLEPLMASL AGSGMDPVSL ILPAGEKTKS FEHLIPVCEA VLGARIERND AVIALGGGVI GDLTGFAAGI VRRGSRFIQI PTSLLAQVDS SVGGKTGINS PHGKNLIGVF HQPDLVLADT AALDTLSPRE FRAGYAEVVK YGLIDKPDFF EWLEQNWQAV FAGGPARIEA IAVSCQAKAD VVAADERENG LRALLNLGHT FGHALEAATG YDSKRLVHGE GVAIGMVLAH EFSARMNIAS PDDARRVEMH LKTVGLPTRM ADIPGMLPPA DRLLEAIAQD KKVKGGKFTF ILTRGIGQSF IADDVPSSEV LSFLEERIPR //