ID AROF_STRLI Reviewed; 146 AA. AC P55911; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 02-SEP-2026, entry version 79. DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase; DE EC=2.5.1.54; DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase; DE AltName: Full=DAHP synthase; DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase; DE Flags: Fragment; OS Streptomyces lividans. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1916; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=TK64; RA Liaw L.L., Su M.H., Lee Y.H.W.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP IDENTIFICATION, AND CONCEPTUAL TRANSLATION. RX PubMed=8760910; DOI=10.1099/13500872-142-8-1973; RA Walker G.E., Dunbar B., Hunter I.S., Nimmo H.G., Coggins J.R.; RT "Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7- RT phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus RT and Neurospora crassa."; RL Microbiology 142:1973-1982(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7- CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 1/7. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L13767; Type=Frameshift; Evidence={ECO:0000305}; 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; L13767; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P55911; -. DR SMR; P55911; -. DR UniPathway; UPA00053; UER00084. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002480; DAHP_synth_2. DR PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1. DR PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1. DR Pfam; PF01474; DAHP_synth_2; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS52062; DAHPS_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Transferase. FT CHAIN <1..146 FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase" FT /id="PRO_0000140856" FT DOMAIN 1..146 FT /note="DAHPS class-II TIM-barrel" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01407" FT NON_TER 1 SQ SEQUENCE 146 AA; 16589 MW; 1A837D3371EDC546 CRC64; LQYIERLDPE REPGRLTFIV RMGADKIRDK LPELVERSPP PATVAWITDP MHGNTYEAAP VHKTRRFDDV LDEVKGFFEV HKSLGTHPGG IHVELTGDDV TECVGGGDEI FVDDLHQRYE TACDPRLNRS QSLDLAFLVA EMYRDQ //