ID A0A1C7LIB9_9BURK Unreviewed; 372 AA. AC A0A1C7LIB9; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 16-JAN-2019, entry version 11. DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210916}; DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110}; DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210941}; GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110}; GN ORFNames=ACM14_05305 {ECO:0000313|EMBL:OBY86562.1}; OS Delftia sp. JD2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=469553 {ECO:0000313|EMBL:OBY86562.1, ECO:0000313|Proteomes:UP000093107}; RN [1] {ECO:0000313|EMBL:OBY86562.1, ECO:0000313|Proteomes:UP000093107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JD2 {ECO:0000313|EMBL:OBY86562.1, RC ECO:0000313|Proteomes:UP000093107}; RA Morel M.A., Iriarte A., Jara E., Musto H., Castro-Sowinski S.; RT "Revealing the biotechnological potential of Delftia sp. JD2 by a RT genomic approach."; RL AIMS Bioeng 3:156-175(2016). CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino- CC heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). CC {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00858858}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3- CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, CC ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; CC EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS01116881}; 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 CC Co(2+) or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00110, ECO:0000256|SAAS:SAAS00336779}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|SAAS:SAAS00607009}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00210851}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00210934}. CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110, CC ECO:0000256|SAAS:SAAS00858850}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OBY86562.1}. 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; LFJT01000006; OBY86562.1; -; Genomic_DNA. DR RefSeq; WP_065345555.1; NZ_LFJT01000006.1. DR EnsemblBacteria; OBY86562; OBY86562; ACM14_05305. DR PATRIC; fig|469553.3.peg.3615; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000093107; Unassembled WGS sequence. 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00210890}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00210867}; KW Cobalt {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00210864}; KW Complete proteome {ECO:0000313|Proteomes:UP000093107}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00210856}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00958949}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS01080055}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210880}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00110, KW ECO:0000256|SAAS:SAAS00858852}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00210870}. FT DOMAIN 76 337 DHQ_synthase. {ECO:0000259|Pfam:PF01761}. FT NP_BIND 80 85 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT NP_BIND 114 118 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT NP_BIND 138 139 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. FT METAL 193 193 Cobalt or zinc. {ECO:0000256|HAMAP-Rule: FT MF_00110}. FT METAL 256 256 Cobalt or zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT METAL 273 273 Cobalt or zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT BINDING 151 151 NAD; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00110}. FT BINDING 160 160 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}. SQ SEQUENCE 372 AA; 39679 MW; 091F88601643F253 CRC64; MPTASSLPAA QVVTIDLGDR SYPITIGTGL LDQAATYAAL PSAAQAVIVS NDVVAPLYEP ALRRVLEQRY RSVRTVVLPD GEAHKDWQTL NLIFDDLLSG GCDRKTVLFA LGGGVIGDMT GFAAASYMRG VPFVQVPTTL LSQVDSSVGG KTAINHPLGK NMIGAFYQPQ LVVCDLASLD TLPVRELSAG LAEVIKYGPI ADMDFLAWLE ENMDALLARD RTALAHAIKR SVEIKAWVVG QDEKEAGLRA ILNFGHTFGH AIEAGMGYGN WLHGEGVGAG MVMAAELSQR LGLVDAAFVQ RLRVLIARAG LPVRGAVLDE ADNAGRYLEL MRVDKKSEAG EIRFVLIDGP GKAIMRSAPD ALVREVINAC CA //