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Database: UniProt
Entry: G2QFC2_MYCTT
LinkDB: G2QFC2_MYCTT
Original site: G2QFC2_MYCTT 
ID   G2QFC2_MYCTT            Unreviewed;       372 AA.
AC   G2QFC2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   10-APR-2019, entry version 37.
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=MYCTH_2307175 {ECO:0000313|EMBL:AEO59151.1};
OS   Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS   (Sporotrichum thermophile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Thermothelomyces.
OX   NCBI_TaxID=573729 {ECO:0000313|EMBL:AEO59151.1, ECO:0000313|Proteomes:UP000007322};
RN   [1] {ECO:0000313|EMBL:AEO59151.1, ECO:0000313|Proteomes:UP000007322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799
RC   {ECO:0000313|Proteomes:UP000007322};
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J.,
RA   Reid I., Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B.,
RA   Coutinho P.M., Lombard V., Natvig D.O., Lindquist E., Schmutz J.,
RA   Lucas S., Harris P., Powlowski J., Bellemare A., Taylor D., Butler G.,
RA   de Vries R.P., Allijn I.E., van den Brink J., Ushinsky S., Storms R.,
RA   Powell A.J., Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J.,
RA   LaBoissiere S., Clutterbuck A.J., Martinez D., Wogulis M.,
RA   de Leon A.L., Rey M.W., Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading
RT   fungi Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(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;
CC         EC=2.5.1.54; Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP003005; AEO59151.1; -; Genomic_DNA.
DR   RefSeq; XP_003664396.1; XM_003664348.1.
DR   STRING; 78579.XP_003664396.1; -.
DR   EnsemblFungi; AEO59151; AEO59151; MYCTH_2307175.
DR   GeneID; 11514261; -.
DR   KEGG; mtm:MYCTH_2307175; -.
DR   eggNOG; ENOG410IF83; Eukaryota.
DR   eggNOG; COG0722; LUCA.
DR   InParanoid; G2QFC2; -.
DR   KO; K01626; -.
DR   OrthoDB; 1034517at2759; -.
DR   Proteomes; UP000007322; Chromosome 4.
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   Complete proteome {ECO:0000313|Proteomes:UP000007322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007322};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN       45    342       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   372 AA;  39803 MW;  8128BAC8B195901E CRC64;
     MAPLQADDMR VLGQDPLIPP ALLISEIPMT EEALQTVVKG RRDAVGVIMG WNDRLLVIVG
     PCSIHDPATA LEYAARLKAL SEKLSGDLVI IMRAYLEKPR TTVGWKGLIN DPDIDETFKI
     NKGLRVSRQL FRDLTSSGMP IASEMLDTIS PQFLADFISV GAIGARTTES QLHRELASGL
     SFPVGFKNGT DGSLGVAIDA IGAAAAKHHF MGVTKQGLAA ITRTKGNEHG FVILRGGSKG
     TNYDKASIQA AKETLIKKGQ KLAIMVDCSH GNSNKDHRNQ PKVAKAVADQ LREGETAIIG
     VMIESNINEG NQKVPPEGPS GLKKGVSITD ACINWETTVE VLEDLAAAVR ERRKVTAGAT
     NGSPKTTPLE ED
//
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