ID A0A2B7ZMX0_9EURO Unreviewed; 373 AA.
AC A0A2B7ZMX0;
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=GX50_02835 {ECO:0000313|EMBL:PGH34352.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH34352.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH34352.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH34352.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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:PGH34352.1}.
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DR EMBL; PDND01000042; PGH34352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZMX0; -.
DR STRING; 73230.A0A2B7ZMX0; -.
DR VEuPathDB; FungiDB:EMCG_01305; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000226031; 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:UP000226031};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 55..356
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 373 AA; 40374 MW; 1C8CDC4DC2D0A55F CRC64;
MASQWYIENK DVGNTEHAED WRIRGYNPLT PPNLLQHEIP QTPASKKTVL SSRKEAAAIV
NGKDPLNRLL VIIGPCSIHD PEAAMDYCNR LLQQKEKHKD ELLIVMRSYL EKPRTTVGWK
GLINDPDIDN SFQINKGLRV SRQLFVDLTD KGMPIASEML DTISPQFLAD LLSVGAIGAR
TTESQLHREL ASGLSFPVGF KNGTDGSLDV AVDAIGAVKH PHHFLSVTKP GVVAIVGTVG
NEDCFAILRG GKKGTNYDAT SIAEAKAKLA GKDLNARLMV DCSHGNSLKD HRNQPKVAAV
LAEQITAGEQ AIMGVMIESN INEGSQKVSP QGKAGLKYGV SITDACIGWD DTESVLQVLA
DAVRQRREGG QAA
//
