ID A0A2T0FJU6_9ASCO Unreviewed; 363 AA.
AC A0A2T0FJU6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=B9G98_02881 {ECO:0000313|EMBL:PRT55261.1};
OS Wickerhamiella sorbophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT55261.1, ECO:0000313|Proteomes:UP000238350};
RN [1] {ECO:0000313|EMBL:PRT55261.1, ECO:0000313|Proteomes:UP000238350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS02 {ECO:0000313|EMBL:PRT55261.1,
RC ECO:0000313|Proteomes:UP000238350};
RA Ahn J.O.;
RT "Genome sequencing of [Candida] sorbophila.";
RL Submitted (APR-2017) 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:PRT55261.1}.
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DR EMBL; NDIQ01000021; PRT55261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0FJU6; -.
DR STRING; 45607.A0A2T0FJU6; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000238350; 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:UP000238350};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 54..349
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 363 AA; 39367 MW; 0BB99D71E416DD4F CRC64;
MSPLHQINQK IGDRTQTEDW RVRGYSPLIA PDLLQSEIPL TTKSYEKIIE GREAATAVLN
GTDDRLLVVV GPCSIHDPKA AVEYCEKLAK LNEELKGDLL IIMRAYLEKP RTTVGWKGLI
NDPDIDGSFK INKGLRIARE LFVKLTSMLP IAGEMLDTIS PQFLSDLFSL GAIGARTTEC
QLHRELASGL SFPVGFKNGT DGGLQVAIDA MGSAAHPHHF LSVTKPGNVA IVGTNGNQDT
FAILRGGKNG TNYDKDSVND AWAKLLKSGV AKEGSARIMI DCSHGNSLKN HNNQPKVVDA
VVEQVAGGQK AICGVMIESN LVAGRQNDPV VYGQSITDAC IDWETTEKCL RELAQAAKDR
RSH
//
