ID A0A2P7YLJ4_9ASCO Unreviewed; 423 AA.
AC A0A2P7YLJ4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
GN ORFNames=C7M61_003711 {ECO:0000313|EMBL:PSK36847.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK36847.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK36847.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK36847.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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 -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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:PSK36847.1}.
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DR EMBL; PYFQ01000010; PSK36847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YLJ4; -.
DR STRING; 418784.A0A2P7YLJ4; -.
DR EnsemblFungi; C7M61_003711_t1; PSK36847.1; C7M61_003711.
DR VEuPathDB; FungiDB:C7M61_003711; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
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 SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107}.
FT DOMAIN 49..349
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 423 AA; 46474 MW; EFE53BDAD0566CCE CRC64;
MSQTPIPEEY DDTRIMGYDP LIPPALLQTE IKASKKSLDT VIKGRIDSSR IISGKDDRCL
VIVGPCSIHD PEAAIEYANR LKKLAGELSD DLVIIMRAYL EKPRTTVGWK GLINDPNVDN
TFDINEGLRV SRKLYADLTG EVGIPIGSEM LDTISPQYFS DLLSFGAVGA RTTESQLHRE
LASGLSFPIG FKNGTDGNVG VALDAVQASS KGHHFMGVTK NGLAAITTTK GNDHCFVILR
GGKNLTNYDS ESVKNAKAAI AKSTNPNIKI MVDCSHDNSK KDYKNQPSVL QSVVEQIEAG
EHALMGVMIE SHINEGKQSM PPGNEGKAAL KYGVSITDSC VSWETTVDML KNLSKAEENI
LKRVLRKWFD ENPTFDLIDQ FVNDLSSFEL EQPVITPRFG QRACLYLCSA ARDDQYCLLI
LKK
//
