ID A0A094ABQ5_9PEZI Unreviewed; 379 AA.
AC A0A094ABQ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=V490_03881 {ECO:0000313|EMBL:KFX95411.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX95411.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX95411.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX95411.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KFX95411.1}.
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DR EMBL; JPJS01001035; KFX95411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094ABQ5; -.
DR STRING; 1437433.A0A094ABQ5; -.
DR HOGENOM; CLU_030903_0_1_1; -.
DR Proteomes; UP000029320; 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 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:SF18; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHENYLALANINE-INHIBITED; 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|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|PIRNR:PIRNR001361};
KW Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 58..356
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 379 AA; 40935 MW; FA53B752BE85C81E CRC64;
MSSSFFIENK DVGNRAGTED WRIRGYNPLT PPGLLQHEIP QTPESKETVI TGRDESVAIV
SGTDDKHRLL VVIGPCSIHD PAAALEYCDK LLALKEKYKD DLLIVMRSYL EKPRTTVGWK
GLINDPEIDN SFQINKGLRI SRQLFVDLTS KGMPLASEML DTISPQFFSD LLSVGAVGAR
TTESQLHREL ASGLSFPVGF KNGTDGSLGV AIDAIGAVRH PHHFLSVTKP GVVAIVGTVG
NEDCFVILRG GTKGTNFDAK SIAEAKAALQ KSGVRERLMV DCSHGNSQKD HRNQPKVAAV
LAEQIAQGET AIMGVMIESN INEGNQKVPK EGKAGLKYGV SITDACIGWD DTESVLETLA
AACKKRRDIL NKSKANGSN
//
