ID A0A1D9GU21_9BURK Unreviewed; 359 AA.
AC A0A1D9GU21;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BKK79_04370 {ECO:0000313|EMBL:AOY91133.1};
OS Cupriavidus sp. USMAA2-4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY91133.1, ECO:0000313|Proteomes:UP000178101};
RN [1] {ECO:0000313|EMBL:AOY91133.1, ECO:0000313|Proteomes:UP000178101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY91133.1,
RC ECO:0000313|Proteomes:UP000178101};
RA Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT "Complete genome sequences of three Cupriavidus strains isolated from
RT various Malaysian environments.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017748; AOY91133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D9GU21; -.
DR STRING; 876364.BKK79_04370; -.
DR KEGG; cuu:BKK79_04370; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000178101; Chromosome 1.
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:UP000178101};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 45..341
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 359 AA; 38963 MW; 753DA4C687863773 CRC64;
MLKNTDDLRI RELKELLPPA HLIREFACSE KASDVIYGAR QAMHRILHGM DDRLIVIIGP
CSIHDTRAAL EYAKLLKEQR DRFAGELEVV MRVYFEKPRT TVGWKGLIND PHMDGSFKIN
DGLRTARELL LNISEMGLPA GTEYLDMISP QYIADLVSWG AIGARTTESQ VHRELASGLS
CPVGFKNGTD GNVKIAVDAI KAASQPHHFL SVTKGGHSAI VSTSGNEDCH IILRGGKAPN
YDAASVQEAC EAIAKAGLAA RLMIDASHAN SSKKHENQIP VCEDIGRQMA AGDERIVGVM
VESHLVGGRQ DHVQGTPVEN LTYGQSVTDA CIGWDDSVKV LETLANAVKA RRLAKGSGN
//