ID A0A1G6ADQ5_9FIRM Unreviewed; 343 AA.
AC A0A1G6ADQ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN02910298_00186 {ECO:0000313|EMBL:SDB06564.1};
OS Pseudobutyrivibrio sp. YE44.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520802 {ECO:0000313|EMBL:SDB06564.1, ECO:0000313|Proteomes:UP000198713};
RN [1] {ECO:0000313|Proteomes:UP000198713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE44 {ECO:0000313|Proteomes:UP000198713};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FMXT01000001; SDB06564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6ADQ5; -.
DR STRING; 1520802.SAMN02910298_00186; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000198713; 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:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-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|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 34..335
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 343 AA; 38776 MW; 052F09A3D1FA785E CRC64;
MSFTYLKKMP TPEEIKEMLP VPEKVQELKK KRDQEVADII TGKDDRFLCI IGPCSADNED
AVCEYINKLS RVADDIKDKV LVVPRIYTNK PRTTGSGYKG IASQPDPNEA PDMLAGLIAM
RKMHIRAMEE SELTAADEML YPENWGYVDD LLSYVAIGAR SVEDQHHRLT VSGFDVASGM
KNPTSGDFSV MLNSVYAAQH PHHFTFSGYE VKTSGNPLAH TILRGAVSKH GNSTQNYHYE
DLIRLHNMYE EMDLVNPACI IDANHSNSNK QFKEQIRIVK EVMHNRKHSD DIKKLVKGVM
IESYLVEGCQ PISDHQTYGQ SITDACLGWE DTRHLLYTIA ERN
//
