ID Q081C0_SHEFN Unreviewed; 354 AA.
AC Q081C0;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Sfri_2299 {ECO:0000313|EMBL:ABI72145.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72145.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI72145.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72145.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000447; ABI72145.1; -; Genomic_DNA.
DR RefSeq; WP_011637754.1; NC_008345.1.
DR AlphaFoldDB; Q081C0; -.
DR STRING; 318167.Sfri_2299; -.
DR KEGG; sfr:Sfri_2299; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_6; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000000684; 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 Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:ABI72145.1}.
FT DOMAIN 45..338
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 354 AA; 38992 MW; 7B52DB456F4C419F CRC64;
MTIKTDELRT TLLSKVISPA QLASEYPLTQ NAADYLVAQR REVEAIIAGE DQRLLVIIGP
CSIHDTKAAL EYAERLSALH HELKDDLCIL MRVYFEKPRT IVGWKGLISD PDLDGSFSPN
KGLRMARQLL QQITELKLPI ATEFLDMVNG QYIADLITWG AIGARTTESQ IHREMASALS
CPVGFKNGTD GNINIAVDAV RAAQAPHIFY SPDKDGAMAV YRTHGNPFGH IILRGGKTPN
YSAEDIEVAR AQLENVGVTQ RMVVDFSHGN SEKQHRNQLN VANSIMAQLR SGSTAIAGIM
AESFMIEGNQ KVVKDEPLVY GQSITDACLH WADSEKLLRD LAQASKERKA LLAQ
//
