ID Q46TA0_CUPPJ Unreviewed; 377 AA.
AC Q46TA0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN OrderedLocusNames=Reut_B4281 {ECO:0000313|EMBL:AAZ63634.1};
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ63634.1};
RN [1] {ECO:0000313|EMBL:AAZ63634.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 {ECO:0000313|EMBL:AAZ63634.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL Submitted (AUG-2005) 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; CP000091; AAZ63634.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46TA0; -.
DR STRING; 264198.Reut_B4281; -.
DR KEGG; reu:Reut_B4281; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_4; -.
DR OMA; DLHIVHR; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
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 66..361
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 41037 MW; B4DD5F9FFBDA9523 CRC64;
MNTPQASTNS IGEGWPHPSD RTSGTDDARV DDIIPLPPPE HLIRFFPIAG TPIESLVTAT
RQSISRILHG QDDRLLVIMG PCSIHDPRAA LDYAQRLMAQ RVRYADTLEI VMRVYFEKPR
TTVGWKGLIN DPYLDESYRI DEGLRMARHL LLDINRLGLP AAGEFLDVIS PQYIGDLISW
GAIGARTTES QVHRELASGT SAPIGFKNGT DGNIKIAIDA IQAASRPHHF LGVHKNGQVA
TVHTRGNPDC HVILRGGKVP NYDADSVAAA CKDLDAAGLD RRLMVDCSHA NSSKQHLRQI
DVARDVARQV SGGSRSVFGV MVESHLIGGA QKFTPGQHNP SELTYGQSIT DACIGWDDSL
AVLDMLAEAV AARRQKA
//