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Database: UniProt
Entry: A9L4I1_SHEB9
LinkDB: A9L4I1_SHEB9
Original site: A9L4I1_SHEB9 
ID   A9L4I1_SHEB9            Unreviewed;       354 AA.
AC   A9L4I1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Sbal195_2603 {ECO:0000313|EMBL:ABX49771.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX49771.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX49771.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX49771.1,
RC   ECO:0000313|Proteomes:UP000000770};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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; CP000891; ABX49771.1; -; Genomic_DNA.
DR   RefSeq; WP_006086250.1; NC_009997.1.
DR   AlphaFoldDB; A9L4I1; -.
DR   GeneID; 11772698; -.
DR   KEGG; sbn:Sbal195_2603; -.
DR   HOGENOM; CLU_030903_0_1_6; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000000770; 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:ABX49771.1}.
FT   DOMAIN          45..337
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   354 AA;  39058 MW;  ABEC380C4CEC0863 CRC64;
     MTIKTDELRT SLLAKVISPA QLASEFPLTQ DAADYLVQQR REVEAIIMGE DQRLLVIIGP
     CSIHDTKAAL DYAQRLAALH QELKDDLCIL MRVYFEKPRT IVGWKGLISD PDLDGSFEPN
     KGLRIARELL QQITELKLPI ATEFLDMVNG QYIADLITWG AIGARTTESQ VHREMASALS
     CPVGFKNGTD GNINIAVDAV RAAQVPHIFY SPDKDGAMAV YRTHGNPFGH IILRGGKTPN
     YHAEDIEKAR QQLASVGVTQ RMVVDFSHGN SEKNHLKQLN VADEIMAQMR AGSTAIAGIM
     AESFLQEGNQ KVVADQPLCY GQSITDACLH WDDSEVLLRK LAAASRERKA LLAK
//
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