ID H1LT13_9FIRM Unreviewed; 101 AA.
AC H1LT13;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase {ECO:0000256|ARBA:ARBA00032193};
DE AltName: Full=DAHP synthase {ECO:0000256|ARBA:ARBA00031349};
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase {ECO:0000256|ARBA:ARBA00031111};
GN ORFNames=HMPREF9099_00591 {ECO:0000313|EMBL:EHO53920.1};
OS Lachnospiraceae bacterium oral taxon 082 str. F0431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=861454 {ECO:0000313|EMBL:EHO53920.1, ECO:0000313|Proteomes:UP000003005};
RN [1] {ECO:0000313|EMBL:EHO53920.1, ECO:0000313|Proteomes:UP000003005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0431 {ECO:0000313|EMBL:EHO53920.1,
RC ECO:0000313|Proteomes:UP000003005};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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 -!- 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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000256|ARBA:ARBA00004688}.
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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:EHO53920.1}.
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DR EMBL; AGRL01000029; EHO53920.1; -; Genomic_DNA.
DR AlphaFoldDB; H1LT13; -.
DR PATRIC; fig|861454.3.peg.569; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_2287833_0_0_9; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000003005; 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:InterPro.
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 PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..93
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 101 AA; 11825 MW; A3821C7062E46DB4 CRC64;
MKLLHDLYLE RDIVNPAVIV DANHSNSNKK YKEQVRIVKE VLHSMRYSDE IRNFVKGVMI
ESYIEEGNQK IEEHIYGKSI TDPCLSFEDS KKLLLEMAEI L
//
