ID A0A0S7DLW4_9EURO Unreviewed; 369 AA.
AC A0A0S7DLW4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ALT_009983 {ECO:0000313|EMBL:GIM37308.1}, CNMCM8060_007876
GN {ECO:0000313|EMBL:KAF4174971.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4174971.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:GIM37308.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM37308.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4174971.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4174971.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4174971.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4174971.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:KAF4174971.1}.
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DR EMBL; BCLY01000005; GIM37308.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000065; KAF4174971.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DLW4; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_3044; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000713487; 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 Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 50..346
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 369 AA; 39996 MW; 357E378782BC8796 CRC64;
MPLVKTTEVN EDTRVLGYDP LLSPQFLQSE IPAPAHAIEA VRSGRNQAIE IIEQRDDRLL
VVVGPCSIHD PATALEYATR LKELSQKLSG ELCVIMRAYL EKPRTTVGWK GLINDPDIDE
TYNINKGLRV SRKLYADLTG MGMPIASEML DTISPQYLAD LISLGAIGAR TTESQLHREL
ASGLSFPIGY KNGTDGNLTV AIDAIGAASH PHRFLGVTKQ GLAAITKTSG NEHGFVILRG
GNKGTNYDRA SIKSAREALR AKKQREVVMV DCSHGNSKKD HRNQPLVAKE VADQLREGED
AIIGVMIESN INEGNQKVPP EGPSGLLKGV SITDACINWE TTVTVLEDLA DAVRTRRTAK
ASKSNGVSQ
//
