ID A0A1H4CHV5_9FIRM Unreviewed; 343 AA.
AC A0A1H4CHV5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN02910384_01890 {ECO:0000313|EMBL:SEA59910.1};
OS Pseudobutyrivibrio sp. ACV-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520801 {ECO:0000313|EMBL:SEA59910.1, ECO:0000313|Proteomes:UP000199179};
RN [1] {ECO:0000313|Proteomes:UP000199179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
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; FNQZ01000007; SEA59910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4CHV5; -.
DR STRING; 1520801.SAMN02910384_01890; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000199179; 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; 38613 MW; A9461D275E8BAC13 CRC64;
MSFTYLKKLP TPEEIKEMLP VPEKVQQIKL QRDKEVADII TGKDDRFLCI IGPCSADNED
AVCEYISKLS RVAEDIKDKV LVVPRIYTNK PRTTGSGYKG IASQPDPNEA PDMVAGLIAM
RKMHIRAMTE SELTAADEML YPENWGYVDD LLSYVAIGAR SVEDQHHRLT VSGFDVASGM
KNPTSGDFSV MLNSVYAAQH PHHFTFSGYE VKTSGNPLAH TILRGAVSKH GNSTQNYHYE
DLIRLHNMYE QMDLVNPACI IDANHSNSNK QFKEQIRIVK EVMHNRNHSD AIKSLVKGVM
IESYLVEGCQ PISDHQTYGQ SITDPCLGWE DTRHLLYTIA ERN
//
