ID A0A1M5Y790_9VIBR Unreviewed; 355 AA.
AC A0A1M5Y790;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN Name=aroF {ECO:0000313|EMBL:SHI07927.1};
GN ORFNames=VA7868_01524 {ECO:0000313|EMBL:SHI07927.1};
OS Vibrio aerogenes CECT 7868.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI07927.1, ECO:0000313|Proteomes:UP000184608};
RN [1] {ECO:0000313|EMBL:SHI07927.1, ECO:0000313|Proteomes:UP000184608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI07927.1,
RC ECO:0000313|Proteomes:UP000184608};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXZ01000015; SHI07927.1; -; Genomic_DNA.
DR RefSeq; WP_073603271.1; NZ_FQXZ01000015.1.
DR AlphaFoldDB; A0A1M5Y790; -.
DR STRING; 1216006.VA7868_01524; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000184608; 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:SF10; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYR-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:UP000184608};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:SHI07927.1}.
FT DOMAIN 41..337
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 355 AA; 39349 MW; A28EBF957D814B8D CRC64;
MSELNDVNII EQQVLITPEQ LKAKLPLSSD AQAFIHHSRQ AISDIIHKRD HRLLVVCGPC
SIHDLDAAKD YARRFKALAE EVSDQLLLVM RVYFEKPRTT VGWKGLINDP YLNGTFDIEH
GLHVGRQLLV ELAEMGIPLA TEALDPISPQ YLSDTFSWAA IGARTTESQT HREMASGLSM
PIGFKNGTDG SLMTAINAMQ AASSSHRFMG INAKGQVALL TTQGNPNGHV ILRGGKQTNY
DSVSVAECEE EMRQSNLEPS LMIDCSHANS RKDFRRQPLV AEDAFRQIRE GNRSIVGLMI
ESHINEGNQS ADLPLDQMEY GVSITDACIS WETTEVLLRK ACDALSPVLE KRLKD
//
