ID Q8U0A9_PYRFU Unreviewed; 262 AA. AC Q8U0A9; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 126. DE SubName: Full=2-dehydro-3-deoxyphosphoheptonate aldolase {ECO:0000313|EMBL:AAL81814.1}; DE EC=2.5.1.54 {ECO:0000313|EMBL:AAL81814.1}; GN OrderedLocusNames=PF1690 {ECO:0000313|EMBL:AAL81814.1}; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497 {ECO:0000313|EMBL:AAL81814.1, ECO:0000313|Proteomes:UP000001013}; RN [1] {ECO:0000313|EMBL:AAL81814.1, ECO:0000313|Proteomes:UP000001013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 RC {ECO:0000313|Proteomes:UP000001013}; RX PubMed=10430560; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [2] {ECO:0007829|PDB:1ZCO} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=16142893; DOI=10.1021/bi050577z; RA Schofield L.R., Anderson B.F., Patchett M.L., Norris G.E., Jameson G.B., RA Parker E.J.; RT "Substrate ambiguity and crystal structure of Pyrococcus furiosus 3-deoxy- RT D-arabino-heptulosonate-7-phosphate synthase: an ancestral 3-deoxyald-2- RT ulosonate-phosphate synthase?"; RL Biochemistry 44:11950-11962(2005). RN [3] {ECO:0007829|PDB:4GRS} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-262. RX PubMed=23345433; DOI=10.1073/pnas.1217923110; RA Cross P.J., Allison T.M., Dobson R.C., Jameson G.B., Parker E.J.; RT "Engineering allosteric control to an unregulated enzyme by transfer of a RT regulatory domain."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2111-2116(2013). RN [4] {ECO:0007829|PDB:4C1K, ECO:0007829|PDB:4C1L} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=24239948; DOI=10.1016/j.jmb.2013.11.008; RA Nazmi A.R., Schofield L.R., Dobson R.C., Jameson G.B., Parker E.J.; RT "Destabilization of the homotetrameric assembly of 3-deoxy-D-arabino- RT heptulosonate-7-phosphate synthase from the hyperthermophile Pyrococcus RT furiosus enhances enzymatic activity."; RL J. Mol. Biol. 426:656-673(2014). 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; AE009950; AAL81814.1; -; Genomic_DNA. DR PDB; 1ZCO; X-ray; 2.25 A; A/B=1-262. DR PDB; 4C1K; X-ray; 2.15 A; A/B/C/D/E/F=1-262. DR PDB; 4C1L; X-ray; 1.80 A; A/B=1-262. DR PDB; 4GRS; X-ray; 3.00 A; A/B/C/D=33-262. DR PDBsum; 1ZCO; -. DR PDBsum; 4C1K; -. DR PDBsum; 4C1L; -. DR PDBsum; 4GRS; -. DR AlphaFoldDB; Q8U0A9; -. DR SMR; Q8U0A9; -. DR STRING; 186497.PF1690; -. DR PaxDb; 186497-PF1690; -. DR KEGG; pfu:PF1690; -. DR PATRIC; fig|186497.12.peg.1758; -. DR eggNOG; arCOG01049; Archaea. DR HOGENOM; CLU_062599_1_1_2; -. DR OrthoDB; 350424at2157; -. DR PhylomeDB; Q8U0A9; -. DR BRENDA; 2.5.1.54; 5243. DR EvolutionaryTrace; Q8U0A9; -. DR Proteomes; UP000001013; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. 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; PF00793; DAHP_synth_1; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K}; KW Metal-binding {ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1L}; KW Reference proteome {ECO:0000313|Proteomes:UP000001013}; KW Transferase {ECO:0000313|EMBL:AAL81814.1}. FT DOMAIN 13..255 FT /note="DAHP synthetase I/KDSA" FT /evidence="ECO:0000259|Pfam:PF00793" FT BINDING 31 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1L" FT BINDING 55 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 60 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 111 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 114 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 115 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 136 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 166 FT /ligand="phosphoenolpyruvate" FT /ligand_id="ChEBI:CHEBI:58702" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1K" FT BINDING 201 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1L" FT BINDING 227 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1L" FT BINDING 238 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0007829|PDB:1ZCO, ECO:0007829|PDB:4C1L" SQ SEQUENCE 262 AA; 29225 MW; ED84D28FD5DEADC2 CRC64; MKYSKEYKEK TVVKINDVKF GEGFTIIAGP CSIESRDQIM KVAEFLAEVG IKVLRGGAFK PRTSPYSFQG YGEKALRWMR EAADEYGLVT VTEVMDTRHV ELVAKYSDIL QIGARNSQNF ELLKEVGKVE NPVLLKRGMG NTIQELLYSA EYIMAQGNEN VILCERGIRT FETATRFTLD ISAVPVVKEL SHLPIIVDPS HPAGRRSLVI PLAKAAYAIG ADGIMVEVHP EPEKALSDSQ QQLTFDDFLQ LLKELEALGW KG //