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Database: UniProt
Entry: A0A3A2ZM22_9EURO
LinkDB: A0A3A2ZM22_9EURO
Original site: A0A3A2ZM22_9EURO 
ID   A0A3A2ZM22_9EURO        Unreviewed;       366 AA.
AC   A0A3A2ZM22;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=PHISCL_08743 {ECO:0000313|EMBL:RJE18925.1};
OS   Aspergillus sclerotialis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Polypaecilum.
OX   NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE18925.1, ECO:0000313|Proteomes:UP000266188};
RN   [1] {ECO:0000313|Proteomes:UP000266188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA   Tafer H., Lopandic K.;
RL   Submitted (FEB-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:RJE18925.1}.
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DR   EMBL; MVGC01000473; RJE18925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A2ZM22; -.
DR   STRING; 2070753.A0A3A2ZM22; -.
DR   Proteomes; UP000266188; 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:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYROSINE-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:UP000266188};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          50..345
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   366 AA;  39696 MW;  BC8C3761CDBCF677 CRC64;
     MPLVNTTEVN EDTRVLGYDA LLSPQFLQTE IPASKNVTEV VRSGRNQAIE IIEQRDDRLL
     VVVGPCSIHD PETALEYANR LKALSEKLSS DLCIIMRAYL EKPRTTVGWK GLINDPDIDE
     TYNINKGLRV SRKLYADLTG MGMPIASEML DTISPQFLAD LISLGAIGAR TTESQLHREL
     ASGLSFPIGY KNGTDGNLGI AIDAIGSASH PHRFMGVTKQ GLAAITKTSG NEHGFVILRG
     GSRGTNYDRD SVRAAREALR AKKQREILMI DCSHSNSQKN HRNQPIVAKE IADQLREGQD
     AIIGVMVESN INEGNQKVPP EGPSGLAKGV SITDACIDWE TTVDTLENLA DAVRARRAAK
     ASGNGA
//
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