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Database: UniProt
Entry: A0A291Q3I3_9ACTN
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ID   A0A291Q3I3_9ACTN        Unreviewed;       372 AA.
AC   A0A291Q3I3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=KY5_1038 {ECO:0000313|EMBL:ATL26056.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL26056.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL26056.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL26056.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) 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; CP022685; ATL26056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291Q3I3; -.
DR   KEGG; sfk:KY5_1038; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000221011; 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: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:UP000221011};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          61..353
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   372 AA;  38955 MW;  F2E92BEAF6EA00FC CRC64;
     MQSLDMLAED RPDSVVALSP GDIGGQYRTH SAPTPHGLMS ELPLTEAAAR SVGEGRLMTR
     RVLSGTDDRL LAVVGPCSIH DVNAGLAYAK SLGELAADLA DDLAVVMRVY VEKPRTTVGW
     TGLLTDPALD GSLDVNHGLR TARTLMLEIA ELGLPIATEW LSPSAPVYLA DLISWGAIGA
     RTVESQVHRQ LASGLPMPVG MKNGSTGSVS VAVDAIRSAA APHAYLGVDR DGRAVTLRTS
     GNPDCHVVLR GGSGRPNYHP ENVREAARLL AAAALPTGVV IDASHGNSGK DHERQAVVAR
     EIGAQVAAGN TDIRGVMLEG FLIPGRQDLG PEEPVFGQSV TDACMGWDAT ADVLRDLAAA
     TRQRRAVTAS AR
//
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