ID V2X1L2_MONRO Unreviewed; 388 AA.
AC V2X1L2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 11-DEC-2019, entry version 27.
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=Moror_1868 {ECO:0000313|EMBL:ESK87687.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87687.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK87687.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87687.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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|PIRNR:PIRNR001361};
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {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:ESK87687.1}.
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DR EMBL; AWSO01000753; ESK87687.1; -; Genomic_DNA.
DR RefSeq; XP_007853005.1; XM_007854814.1.
DR EnsemblFungi; ESK87687; ESK87687; Moror_1868.
DR KEGG; mrr:Moror_1868; -.
DR KO; K01626; -.
DR OrthoDB; 1034517at2759; -.
DR Proteomes; UP000017559; 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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DHAP_synth_1.
DR PANTHER; PTHR21225; PTHR21225; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR PIRSF; PIRSF001361; DAHP_synthase; 1.
DR TIGRFAMs; TIGR00034; aroFGH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 75..370
FT /note="DAHP_synth_1"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 388 AA; 42296 MW; 4499A940FF403570 CRC64;
MASIKDSTAP FRFPVPQDDM VQPYPDFNDT AKVEQYLQDR RVIGYDPLVQ PALLRHEIVS
SKHSHRTIAT ARYSASRIIS GTDDRILVIV GPCSVHSPEQ AMEYARMLKD KIPSWPNLLI
IMRAYFEKPR TTVGWKGLIN DPEIDGTFQI NKGLRTARKL LCDLTDMGVP VGSELLDTIS
PQYIADLISW GAIGARTTES QLHRELASGV SFPIGFKNGT DGSVTVAVDA MHSASNPHAF
MGVTEQGLAS IVKTRGNQDV HVILRGGTKG PNFVSEYVKE AAKSIAKKRP FASIMVDCSH
GNSQKNHLNQ PKVLADICSQ LAAGERNITG VMIESNIHDG RQDVPASGPS GLKHGISITD
ACVDFATTVT MLDQLNEAVA KRRSVPQA
//
