ID H8WXL0_CANO9 Unreviewed; 358 AA.
AC H8WXL0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=CORT_0A11310 {ECO:0000313|EMBL:CCG21516.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG21516.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG21516.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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}.
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DR EMBL; HE681719; CCG21516.1; -; Genomic_DNA.
DR RefSeq; XP_003866954.1; XM_003866906.1.
DR AlphaFoldDB; H8WXL0; -.
DR GeneID; 14537344; -.
DR KEGG; cot:CORT_0A11310; -.
DR eggNOG; ENOG502QPSU; Eukaryota.
DR HOGENOM; CLU_030903_0_1_1; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000005018; 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 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 Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 37..344
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 358 AA; 39262 MW; 58FE45558257A591 CRC64;
MEDWRIRGYD PLTPPDLLQH EYPLTPESSK TILEGRNAAV DILNGKDDRL IIVIGPCSIH
DPKAALEYAE RLHKEAEKHK GELLIVMRAY LEKPRTTVGW KGLINDPDIN GTFHINKGLR
IARKLFVELT SKLPIAGEML DTISPQFLSD LFSVGAVGAR TTESQLHREL ASGLSFPVGF
KNGTDGTLGV AIDAVHSASH PHHFLSVTKP GVVAIVGTEG NQDCFVILRG GKQGTNYDET
SVKETQEQLK KAKLITEEKS GPRIMVDCSH GNSNKDHRNQ PKVARIVADQ IEGGDKSICG
LMIESNINEG RQNVPPEEEG GKDALKYGVS ITDACIGWEK TVEVLDLLAN AIKKRRSL
//
