ID AROF_THEMA Reviewed; 338 AA. AC Q9WYH8; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 143. 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; GN Name=aroF; OrderedLocusNames=TM_0343; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=12743122; DOI=10.1074/jbc.m304631200; RA Wu J., Howe D.L., Woodard R.W.; RT "Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) RT synthase: the ancestral eubacterial DAHP synthase?"; RL J. Biol. Chem. 278:27525-27531(2003). CC -!- FUNCTION: Catalyzes the condensation of phosphoenolpyruvate (PEP) and CC D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- CC heptulosonate-7-phosphate (DAHP). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 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 -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Note=Divalent metal ions.; CC -!- ACTIVITY REGULATION: Inhibited by L-phenylalanine and L-tyrosine. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.3 at 60 degrees Celsius.; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Extremely thermostable.; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 1/7. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {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; AE000512; AAD35429.1; -; Genomic_DNA. DR PIR; E72388; E72388. DR RefSeq; NP_228154.1; NC_000853.1. DR RefSeq; WP_004083125.1; NZ_CP011107.1. DR PDB; 1RZM; X-ray; 2.20 A; A/B=1-338. DR PDB; 1VR6; X-ray; 1.92 A; A/B/C/D=1-338. DR PDB; 3PG8; X-ray; 2.00 A; A/B=71-338. DR PDB; 3PG9; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-338. DR PDB; 4GRS; X-ray; 3.00 A; A/B/C/D=1-103. DR PDBsum; 1RZM; -. DR PDBsum; 1VR6; -. DR PDBsum; 3PG8; -. DR PDBsum; 3PG9; -. DR PDBsum; 4GRS; -. DR AlphaFoldDB; Q9WYH8; -. DR SMR; Q9WYH8; -. DR STRING; 243274.TM_0343; -. DR DrugBank; DB03937; D-erythrose 4-phosphate. DR DrugBank; DB01819; Phosphoenolpyruvate. DR PaxDb; 243274-THEMA_03000; -. DR EnsemblBacteria; AAD35429; AAD35429; TM_0343. DR KEGG; tma:TM0343; -. DR eggNOG; COG2876; Bacteria. DR InParanoid; Q9WYH8; -. DR OrthoDB; 9780456at2; -. DR BRENDA; 2.5.1.54; 6331. DR UniPathway; UPA00053; UER00084. DR EvolutionaryTrace; Q9WYH8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro. 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-KW. 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; IPR006218; DAHP1/KDSA. DR InterPro; IPR041071; DAHP_snth_FXD. DR InterPro; IPR006268; DAHP_syn_2. DR NCBIfam; TIGR01361; DAHP_synth_Bsub; 1. DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1. DR PANTHER; PTHR43018:SF2; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1. DR Pfam; PF18152; DAHP_snth_FXD; 1. DR Pfam; PF00793; DAHP_synth_1; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..338 FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase" FT /id="PRO_0000140847" FT STRAND 1..5 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 11..23 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 26..32 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 37..47 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:1VR6" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:3PG8" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 107..119 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1RZM" FT HELIX 144..157 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 171..177 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 191..198 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 214..226 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 254..261 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 270..274 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 280..290 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 293..299 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:1VR6" FT HELIX 316..333 FT /evidence="ECO:0007829|PDB:1VR6" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1VR6" SQ SEQUENCE 338 AA; 37378 MW; E9634B6704D3DF4D CRC64; MIVVLKPGST EEDIRKVVKL AESYNLKCHI SKGQERTVIG IIGDDRYVVA DKFESLDCVE SVVRVLKPYK LVSREFHPED TVIDLGDVKI GNGYFTIIAG PCSVEGREML METAHFLSEL GVKVLRGGAY KPRTSPYSFQ GLGEKGLEYL REAADKYGMY VVTEALGEDD LPKVAEYADI IQIGARNAQN FRLLSKAGSY NKPVLLKRGF MNTIEEFLLS AEYIANSGNT KIILCERGIR TFEKATRNTL DISAVPIIRK ESHLPILVDP SHSGGRRDLV IPLSRAAIAV GAHGIIVEVH PEPEKALSDG KQSLDFELFK ELVQEMKKLA DALGVKVN //