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Database: UniProt
Entry: A0A093Y2H1_TALMA
LinkDB: A0A093Y2H1_TALMA
Original site: A0A093Y2H1_TALMA 
ID   A0A093Y2H1_TALMA        Unreviewed;       385 AA.
AC   A0A093Y2H1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   05-DEC-2018, entry version 16.
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=GQ26_0041070 {ECO:0000313|EMBL:KFX51678.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51678.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular
RT   Mechanisms of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(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;
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFX51678.1}.
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DR   EMBL; JPOX01000004; KFX51678.1; -; Genomic_DNA.
DR   EnsemblFungi; KFX51678; KFX51678; GQ26_0041070.
DR   Proteomes; UP000029285; 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   Complete proteome {ECO:0000313|Proteomes:UP000029285};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029285};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN       56    357       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   385 AA;  41635 MW;  2000E472C85DE34A CRC64;
     MESAPFFIDN PNLGNANSLE DHRIRGYNPL TPPNLLQHEI ALTEKSRKTV LQGRKEAADV
     VKGTDPLNRL LVIIGPCSIH DPDMALEYCD RLLKLKEKYQ DTLLIVMRSY LEKPRTTVGW
     KGLINDPDID GSFKINKGLR LSRQLFVDLT NKGMPIASEM LDTISPQYTA DCLSLGAVGA
     RTTESQVHRE LASGLSFPVG FKNGTDGTLG VAIDAIGAVR HPHHFLSVTK PGVVAIVGTD
     GNDDCFVILR GGTKGTNYDA QSIAEAKENL IKKGLTPRLM VDCSHGNSLK NHKNQPKVAA
     VLAEQIAAGE TAIMGVMIES NINEGNQKVP PEGKSGLKYG VSITDACINW EDTELVLENL
     AQAVHKRQKG AAANDAIKAG GLVHH
//
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