ID E6WCL2_PANSA Unreviewed; 348 AA.
AC E6WCL2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=Pat9b_1658 {ECO:0000313|EMBL:ADU68974.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68974.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU68974.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU68974.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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 + 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|ARBA:ARBA00001370,
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|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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DR EMBL; CP002433; ADU68974.1; -; Genomic_DNA.
DR RefSeq; WP_013508832.1; NC_014837.1.
DR AlphaFoldDB; E6WCL2; -.
DR STRING; 592316.Pat9b_1658; -.
DR KEGG; pao:Pat9b_1658; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000001624; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
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; IPR006219; DAHP_synth_1.
DR NCBIfam; TIGR00034; aroFGH; 1.
DR PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF6; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TRP-SENSITIVE; 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|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:ADU68974.1}.
FT DOMAIN 40..336
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 348 AA; 38000 MW; B4E16B17880757F0 CRC64;
MNKTDELRTA RIGSLIMPAA LAQQHPISAD IAATVTAARQ RIARILTGED RRLLVIIGPC
SLHDPKAALE YAQRLNVLRE QYQDRLEIVM RAYFEKPRTV IGWKGLISDP DLDGSFDVNR
GIAIARQLLI DINAIGMPTA TEFLDMVIGQ FIADLISWGA IGARTTESQI HREMASALSC
PVGFKNGTDG NVQIAVDAIR ASRASHMFLS PDKNGQMTIY QTSGNPHGHV ILRGGRQPNY
HADDVAAAAA NLRDFNLPEQ LVIDFSHANC QKQHRRQRDV AEDVAAQIRA GSRAVAGVMI
ESFLQEGNQK VVSGEPLVYG QSITDPCLGW DDSADVLARL AAAVDSRF
//
