ID A0A318ZQY2_9EURO Unreviewed; 373 AA.
AC A0A318ZQY2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=BP01DRAFT_352458 {ECO:0000313|EMBL:PYH49926.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH49926.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH49926.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH49926.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; KZ821218; PYH49926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZQY2; -.
DR STRING; 1450539.A0A318ZQY2; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000248349; 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:UP000248349};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 56..355
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 373 AA; 40527 MW; 522BD69B987801F1 CRC64;
MSFFIENPNV GDRTSLEDSR IRGYNPLTPP NLLQHEIALT DKSRQTVLEG REEATAIVQG
TDTDRHRLLV VIGPCSIHDP EMALEYCDRL MKMKEKYKDE LLIVMRSYLE KPRTTVGWKG
LINDPDIDNS FRINKGLRVS RQLFVDLTNK GMPIASEMLD TISPQFLADC LSVGAVGART
TESQVHRELA SGLSFPVGFK NGTDGSLGVA VDAIGSVKHP HHFLSVTKPG VAAIVGTVGN
PDCFVILRGG TKGPNYDAQS IAEAKAKLAA QGLPPRLMVD CSHGNSQKNH KNQPKVAAVL
AEQIAAGETA IMGVMIESNI NEGNQKVPPE GKAGLKYGVS ITDACIHWED TELVLENLAQ
AVRTRKVKLT ASQ
//
