ID A0A0C4EWR7_PUCT1 Unreviewed; 385 AA.
AC A0A0C4EWR7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=PTTG_05262 {ECO:0000313|EMBL:OAV87372.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_05262P0, ECO:0000313|Proteomes:UP000005240};
RN [1] {ECO:0000313|EMBL:OAV87372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV87372.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblFungi:PTTG_05262P0}
RP IDENTIFICATION.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_05262P0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:OAV87372.1, ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV87372.1}, and Isolate 1-1
RC / race 1 (BBBD) {ECO:0000313|Proteomes:UP000005240};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EnsemblFungi:PTTG_05262P0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_05262P0};
RX PubMed=27913634; DOI=10.1534/g3.116.032797;
RA Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL G3 (Bethesda) 7:361-376(2017).
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; ADAS01006629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADAS02000440; OAV87372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4EWR7; -.
DR STRING; 630390.A0A0C4EWR7; -.
DR EnsemblFungi; PTTG_05262T0; PTTG_05262P0; PTTG_05262.
DR VEuPathDB; FungiDB:PTTG_05262; -.
DR OMA; DWARRAC; -.
DR OrthoDB; 1404489at2759; -.
DR Proteomes; UP000005240; 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:UP000005240};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 37..333
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 385 AA; 42078 MW; 141B2AA2F54B325A CRC64;
MCFQYEPIVP SQLLRADLRV SENSRKVIDW ARRACSDVIA GKDGRLIVII GPCSIHDPAQ
ALEYARLLAP LIPTLPDLII IMRAYFEKPR TSVGWKGLIN DPDIDGSFKI NKGIKIARKL
LCDLTHLGLP VAVEILDPIS PQYLSELVSW GAIGARTTES QIHREAASGA PHPVGFKNGT
NGDVEVAIEA MKASSFPHSF IGTNDHGLVS IVKTSGNSAL SLILRGGKKG ANFHREAVSE
ARDALQKHRL SFAPSLIIDC SHGNSQKDYR NQAKVVKDIC QQIRAGEKSI HGVMIESNIG
AGRQDVPAEG REGLKHGISI TDGCIDFEST VQVLKDLQNA AADRRSMGRR QSLFDEVYLR
RTSLSHDLQQ FAINTAAIQQ NPSNQ
//
