ID   B9JAW3_RHIR8            Unreviewed;       354 AA.
AC   B9JAW3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 85.
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=Arad_1335 {ECO:0000313|EMBL:ACM25796.1};
OS   Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Martinezella.
OX   NCBI_TaxID=311403 {ECO:0000313|EMBL:ACM25796.1, ECO:0000313|Proteomes:UP000001600};
RN   [1] {ECO:0000313|EMBL:ACM25796.1, ECO:0000313|Proteomes:UP000001600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600};
RX   PubMed=19251847; DOI=10.1128/JB.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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|ARBA:ARBA00003726,
CC       ECO:0000256|PIRNR:PIRNR001361}.
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         Evidence={ECO:0000256|ARBA:ARBA00047508,
CC         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|ARBA:ARBA00004688, 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; CP000628; ACM25796.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9JAW3; -.
DR   STRING; 311403.Arad_1335; -.
DR   KEGG; ara:Arad_1335; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_5; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000001600; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA.
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   FunFam; 3.20.20.70:FF:000005; Phospho-2-dehydro-3-deoxyheptonate aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   NCBIfam; NF009395; PRK12755.1; 1.
DR   NCBIfam; NF009396; PRK12756.1; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYROSINE-INHIBITED; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|PIRNR:PIRNR001361}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001600};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          45..337
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   354 AA;  38212 MW;  615B54FAE6ACDB8A CRC64;
     MLNSTDDLRI IEITALTPPA RIIDEIPRDA AVTSAVTGAR SAVHNILHND DDRLIVVIGP
     CSIHDPIAAR DYAARLMEQR GRFADDLEII MRVYFEKPRT TVGWKGLIND PHLDGSYRIE
     EGLRLARQLL VDVNEIGLPA GCEFLDTITP QYIADLVSWG AIGARTTESQ VHRELASGLS
     CPIGFKNGTN GDTRIALDAI MAASQPHHFP AVTKDGLAAI ASTRGNDDGH IILRGGKQPN
     YDAASVQAVS ELASKLGLDP QIIIDASHAN SNKNPENQPA VVSAVAAQVS AGDHRIKGMM
     MESNIVGGRQ DLVPGKALVY GQSITDGCID WPTSVRTLEE LARAAQARRR MSRQ
//