ID C9P4V2_VIBME Unreviewed; 352 AA.
AC C9P4V2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN ORFNames=VIB_001320 {ECO:0000313|EMBL:EEX37206.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX37206.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX37206.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX37206.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) 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; ACZO01000006; EEX37206.1; -; Genomic_DNA.
DR RefSeq; WP_004395306.1; NZ_ACZO01000006.1.
DR AlphaFoldDB; C9P4V2; -.
DR STRING; 675813.VIB_001320; -.
DR GeneID; 79887737; -.
DR eggNOG; COG0722; Bacteria.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000005604; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000005604};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:EEX37206.1}.
FT DOMAIN 42..338
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 352 AA; 38933 MW; ED86267E6195B28A CRC64;
MPLKTDELRT QALGPMPTPA ELSLAHPVTH EVAERIAHSR QQIEQILSGQ DDRLLVIVGP
CSVHDTHAAL EYARRLSEIQ DQYRDQLFIV MRTYFEKPRT VVGWKGLITD PNLDGSYALE
AGLNKARQLL LDINKLGLAT ATEFLDMITG QYIADLISWG AIGARTTESQ IHREMASALS
CPVGFKNGTN GNVKIAIDAI RAAHASHYFY SPDKNGRMTV YRTSGNPYGH VILRGGESGP
NFDVDSINSA CAQLAEFNLP ERLVVDFSHA NCQKQHRKQL EVAEEIGRQI ESGSHKVAGI
MAESFLIEGN QSMCNLNNLT YGQSITDPCL SWDDTATMLT RLAQAINTRR TQ
//
