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Database: UniProt
Entry: F4RQX6_MELLP
LinkDB: F4RQX6_MELLP
Original site: F4RQX6_MELLP 
ID   F4RQX6_MELLP            Unreviewed;       312 AA.
AC   F4RQX6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE            EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
DE   Flags: Fragment;
GN   ORFNames=MELLADRAFT_36969 {ECO:0000313|EMBL:EGG05246.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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}.
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DR   EMBL; GL883114; EGG05246.1; -; Genomic_DNA.
DR   RefSeq; XP_007411611.1; XM_007411549.1.
DR   AlphaFoldDB; F4RQX6; -.
DR   STRING; 747676.F4RQX6; -.
DR   EnsemblFungi; EGG05246; EGG05246; MELLADRAFT_36969.
DR   GeneID; 18927598; -.
DR   KEGG; mlr:MELLADRAFT_36969; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_36969; -.
DR   eggNOG; ENOG502QPSU; Eukaryota.
DR   HOGENOM; CLU_030903_1_0_1; -.
DR   InParanoid; F4RQX6; -.
DR   OrthoDB; 72311at2759; -.
DR   Proteomes; UP000001072; 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:UP000001072}.
FT   DOMAIN          30..293
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGG05246.1"
SQ   SEQUENCE   312 AA;  33642 MW;  30410B65D05AD7E8 CRC64;
     LILPLILKSK GGTSLSSAAV VDGSRQACAD VISGKAHRLI VLVGPYTEED IDYAKSCLSK
     VERLPNVVII MCSYFEKPRT TAGWKGFIHD PDLDGSSNIN EGIRKAGELS KTVTDMGMPV
     GVELFNTISP QFASVLVSWG AVGSESQLHQ ELASGACHPI CFKSRTQGDM QVAINSIRAA
     ARPHSFLGVD DLGFASIFHT SGNPDVNVIS RGEKVPNYEA ESVKEARDQL SKARPNLHPA
     IALMEIVDHC HQTKVVNKIC EQLINGDQSI VGVMIKSHIN EGHQNGPIQG HLAPKPGVSI
     MFLLHFIPLL LL
//
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