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Database: UniProt
Entry: Q9KRX6_VIBCH
LinkDB: Q9KRX6_VIBCH
Original site: Q9KRX6_VIBCH 
ID   Q9KRX6_VIBCH            Unreviewed;       395 AA.
AC   Q9KRX6;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=VC_1507 {ECO:0000313|EMBL:AAF94662.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF94662.1, ECO:0000313|Proteomes:UP000000584};
RN   [1] {ECO:0000313|EMBL:AAF94662.1, ECO:0000313|Proteomes:UP000000584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961
RC   {ECO:0000313|Proteomes:UP000000584};
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA   Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA   Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF94662.1; -; Genomic_DNA.
DR   PIR; C82191; C82191.
DR   AlphaFoldDB; Q9KRX6; -.
DR   STRING; 243277.VC_1507; -.
DR   DNASU; 2614013; -.
DR   EnsemblBacteria; AAF94662; AAF94662; VC_1507.
DR   KEGG; vch:VC_1507; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_6; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000000584; Chromosome 1.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; 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:UP000000584};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          87..380
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   395 AA;  43671 MW;  BB5007E0055FEFC3 CRC64;
     MVKCSVFTSI YTPFRSCFRR NGLFSLTNSL SLALRNKRTG APMPLKTDEL RTQALGPMPT
     PAELSHAHPI TDEVALRIAQ SRRQIESILT GEDDRLLVIV GPCSVHDTDA ALDYARRLAA
     LQENYTDELF VVMRTYFEKP RTVVGWKGLI TDPNLDGSYA LETGLNKARK LLLDVNKLGL
     ATATEFLDMI TGQYIADLIT WGAIGARTTE SQIHREMASA LSCPVGFKNG TNGNVKIAID
     AIRAAKASHY FYSPDKNGRM TVYRTSGNPF GHIILRGGDS GPNFDAASIN EACQQLAQFN
     LPERLVVDFS HANCQKQHRK QVDVARDICQ QIEAGSHKIA GIMAESFLVE GNQPMHDLNN
     LTYGLSITDP CLGWKDTATM LDMLAQSIKV RRSRH
//
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