ID A0A2N0WTL9_9GAMM Unreviewed; 358 AA.
AC A0A2N0WTL9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CW748_03690 {ECO:0000313|EMBL:PKF58554.1};
OS Alteromonadales bacterium alter-6D02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=2058087 {ECO:0000313|EMBL:PKF58554.1, ECO:0000313|Proteomes:UP000233605};
RN [1] {ECO:0000313|EMBL:PKF58554.1, ECO:0000313|Proteomes:UP000233605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alter-6D02 {ECO:0000313|Proteomes:UP000233605};
RX PubMed=27311813; DOI=.1038/ncomms11965;
RA Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT "Microbial interactions lead to rapid micro-scale successions on model
RT marine particles.";
RL Nat. Commun. 7:11965-11965(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKF58554.1}.
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DR EMBL; PIZK01000005; PKF58554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0WTL9; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000233605; 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:UP000233605};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 43..339
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 358 AA; 39585 MW; 12BA1D2F61FD6E53 CRC64;
MNSGKIDNKH ISSEKVLITP AQLKELMPLN EGAQSYISQA RETIANIIHG KDKRLLVVTG
PCSIHDIESA KEYALKLKKL HEELKDDMYL VMRIYFEKPR TTVGWKGLLN DPDMDGSFEV
EKGLKQGREL LLWLAELELP VATEALDPIS PQYLSELFSW AAIGARTTES QTHREMASGL
SMPVGFKNGT DGKLNVAINA LESAAHSHRF MGINPQGQVA LMQTQGNPDG HIILRGGKSP
NYQSDLITEI ESQIQGEGLV PKLVVDCSHG NSNKDHRRQP LVADDIFDQI NQGNSSIMGI
MLESHLEEGN QSSSLPKEQL RYGVSVTDAC INWADTEQLL IHGAEKVRSA LKKRTIST
//
