ID A0A3E2N7J0_9CLOT Unreviewed; 342 AA.
AC A0A3E2N7J0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DS742_20820 {ECO:0000313|EMBL:RFZ76922.1};
OS Clostridium indicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=759821 {ECO:0000313|EMBL:RFZ76922.1, ECO:0000313|Proteomes:UP000260680};
RN [1] {ECO:0000313|EMBL:RFZ76922.1, ECO:0000313|Proteomes:UP000260680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PI-S10-A1B {ECO:0000313|EMBL:RFZ76922.1,
RC ECO:0000313|Proteomes:UP000260680};
RA Krishna G., Summeta K., Shikha S., Prabhu P.B., Suresh K.;
RT "New species, Clostridium PI-S10-A1B.";
RL Submitted (JUL-2018) 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}.
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:RFZ76922.1}.
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DR EMBL; QOHO01000071; RFZ76922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2N7J0; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000260680; 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 Reference proteome {ECO:0000313|Proteomes:UP000260680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 38..334
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 38894 MW; DF4DFF18D0C1B5A2 CRC64;
MSFKPLHDMP SPEQLREEYP VSSRLAARKL ERDRELAAVI QNQTNKFLVI VGPCSASSED
AVCDYVSRLS KVNRKLNKKL FIIPRIYTAK PRTNGNGYKG ILHYPVGKGH SDLVKGLRAA
RNLHLRVVEE SGLTTADELL YPEAYAYFQD IISYLAIGAR SVEDQQHRFV SSGVDCPVGM
KNPTNGNPDT LFYSIFAAQH GHKFIYRDRE VKSSGNPLAH AIIRGYENLK GEYVPNYQYE
QLLKIGERYR KQRLKNPFII CDVNHANSGK DYSREPMIIY DVLESRSKSE EIRMMVRGVM
IESFIEAGRQ EISGNVYGKS VTDGCLGWNE TEELLHYIAE HV
//
