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Database: UniProt
Entry: Q9RTE8_DEIRA
LinkDB: Q9RTE8_DEIRA
Original site: Q9RTE8_DEIRA 
ID   Q9RTE8_DEIRA            Unreviewed;       361 AA.
AC   Q9RTE8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 109.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   OrderedLocusNames=DR_1817 {ECO:0000313|EMBL:AAF11369.1};
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11369.1, ECO:0000313|Proteomes:UP000002524};
RN   [1] {ECO:0000313|EMBL:AAF11369.1, ECO:0000313|Proteomes:UP000002524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {ECO:0000256|PIRNR:PIRNR001361}.
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         Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; AE000513; AAF11369.1; -; Genomic_DNA.
DR   PIR; A75350; A75350.
DR   RefSeq; NP_295540.1; NC_001263.1.
DR   RefSeq; WP_010888452.1; NZ_CP015081.1.
DR   STRING; 243230.DR_1817; -.
DR   EnsemblBacteria; AAF11369; AAF11369; DR_1817.
DR   GeneID; 1798966; -.
DR   KEGG; dra:DR_1817; -.
DR   PATRIC; fig|243230.17.peg.2029; -.
DR   eggNOG; ENOG4105E99; Bacteria.
DR   eggNOG; COG0722; LUCA.
DR   HOGENOM; HOG000220501; -.
DR   InParanoid; Q9RTE8; -.
DR   KO; K01626; -.
DR   OMA; YDINTGL; -.
DR   OrthoDB; 853329at2; -.
DR   BioCyc; DRAD243230:GH46-1848-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156}.
SQ   SEQUENCE   361 AA;  38728 MW;  90AB5C772928EE6A CRC64;
     MTQPPAPSTT ENLNVTGFTP LMTPRELKAE VPLTDAAERT VLAGRRAAQA ILSGEDDRLL
     VVVGPCSIHD QAQALEYAGR LAALRERVKD RLEVQMRVYV DKPRTTVGWR GYLLDPDMDG
     SNDMGKGVRR TRELMVAVSE LGLPVATELL DPFAPQYLFD AVAWACLGAR TAESQTHRVM
     ASAVSAPMGF KNGTGGGIKL AVDAVVAASH PHAFFTIDED GRAAIVHTKG NAHGHVILRG
     GRAGPNYAPQ FVQEAADLLR AAGREEAVMV DCSHANSGSD WTRQRLVWRD VLGQRLAGQR
     AIRGAMLESN LQAGKQSLPA DLTQLKPGVS VTDACVGWDE TEALLLEAHE QLSGRAALAT
     C
//
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