ID A0A838NGN9_9ARCH Unreviewed; 261 AA. AC A0A838NGN9; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 13-SEP-2023, entry version 9. DE RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000256|HAMAP-Rule:MF_00960}; DE Short=ADH synthase {ECO:0000256|HAMAP-Rule:MF_00960}; DE Short=ADHS {ECO:0000256|HAMAP-Rule:MF_00960}; DE Short=ADTH synthase {ECO:0000256|HAMAP-Rule:MF_00960}; DE EC=2.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00960}; GN Name=aroA' {ECO:0000256|HAMAP-Rule:MF_00960}; GN ORFNames=H0U27_14720 {ECO:0000313|EMBL:MBA3286295.1}; OS Nitrosopumilus sp. OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales; OC Nitrosopumilaceae; Nitrosopumilus. OX NCBI_TaxID=2024843 {ECO:0000313|EMBL:MBA3286295.1}; RN [1] {ECO:0000313|EMBL:MBA3286295.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MGR_bin105 {ECO:0000313|EMBL:MBA3286295.1}; RA Leung P.M., Ortiz M., Shelley G., Cowan D.A., Greening C.; RT "Metagenome from Mackay Glaciers Regions."; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5- CC ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with CC an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- CC dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an CC alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), CC which is involved in the canonical pathway for the biosynthesis of CC aromatic amino acids. {ECO:0000256|HAMAP-Rule:MF_00960}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate + L-aspartate 4- CC semialdehyde = 2,3-dioxopropyl phosphate + 2-amino-2,3,7-trideoxy-D- CC lyxo-hept-6-ulosonate; Xref=Rhea:RHEA:25952, ChEBI:CHEBI:58859, CC ChEBI:CHEBI:58860, ChEBI:CHEBI:58861, ChEBI:CHEBI:537519; CC EC=2.2.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_00960}; CC -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_00960}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00960}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBA3286295.1}. 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; JACCUR010000943; MBA3286295.1; -; Genomic_DNA. DR AlphaFoldDB; A0A838NGN9; -. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro. DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro. DR GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00958; DhnA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00960; ADH_synthase; 1. DR InterPro; IPR010210; ADH_synthase. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase. DR InterPro; IPR041720; FbaB-like. DR NCBIfam; TIGR01949; ADH_synth; 1. DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1. DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF038992; Aldolase_Ia; 1. DR SMART; SM01133; DeoC; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00960}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00960}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00960}; Transferase {ECO:0000256|HAMAP-Rule:MF_00960}. FT ACT_SITE 24 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" FT ACT_SITE 142 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960, FT ECO:0000256|PIRSR:PIRSR038992-1" FT ACT_SITE 173 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000256|PIRSR:PIRSR038992-1" FT ACT_SITE 173 FT /note="Schiff-base intermediate with substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" FT BINDING 24..28 FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58861" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" FT BINDING 142..144 FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58861" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" FT BINDING 198..199 FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58861" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" FT BINDING 226..227 FT /ligand="1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58861" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00960" SQ SEQUENCE 261 AA; 28367 MW; 84A194FD91C47213 CRC64; MVLGKDVRLS RILNNGKMIC IPMDHGISSG PLDGIKDIHR FIYDTENSGL SCILINKGII KTLPRPLKIG IIAHMSASTS LGPDPNKKVI LGSVKESIRL GADAVSLHIN IGSSEEPMML YTLGLIADEC NEWNMPLIAM MYPRGENIKN PNDATAIAHA SRIGAEAGAD IVKTVYTGNI DTFKDIVKSC PVPIVIAGGP KSKTNRDTLE MCHGAIQAGA IGVTFGRNIF QNSDPNKTIK ALYQIIIENK KLEEVLYKFE R //