GenomeNet

Database: UniProt
Entry: A0A1D7YF31_9ACTN
LinkDB: A0A1D7YF31_9ACTN
Original site: A0A1D7YF31_9ACTN 
ID   A0A1D7YF31_9ACTN        Unreviewed;       125 AA.
AC   A0A1D7YF31;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE            EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase {ECO:0000256|ARBA:ARBA00032193};
DE   AltName: Full=DAHP synthase {ECO:0000256|ARBA:ARBA00031349};
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase {ECO:0000256|ARBA:ARBA00031111};
GN   ORFNames=BFF78_27070 {ECO:0000313|EMBL:AOR34228.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34228.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-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   -!- 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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985}.
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; CP017248; AOR34228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D7YF31; -.
DR   KEGG; spun:BFF78_27070; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000094960; Chromosome.
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:InterPro.
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   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   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..107
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   125 AA;  13375 MW;  8CCF94DF7DCCE0B5 CRC64;
     MVLRGAPGKP NYHAEHVREA ARLLSAAALP TGLVIDASHG NSGKDHERQA VVAREIGAQI
     AHGDTDIRGV MLESFLIAGR QELGSCDLEF GLSVTDACMG WDATVDVLHD LASAARRRRA
     VRVRP
//
DBGET integrated database retrieval system