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Database: UniProt
Entry: A0A1E3PIC7_9ASCO
LinkDB: A0A1E3PIC7_9ASCO
Original site: A0A1E3PIC7_9ASCO 
ID   A0A1E3PIC7_9ASCO        Unreviewed;       370 AA.
AC   A0A1E3PIC7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   11-DEC-2019, entry version 10.
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=NADFUDRAFT_52319 {ECO:0000313|EMBL:ODQ64692.1};
OS   Nadsonia fulvescens var. elongata DSM 6958.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX   NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ64692.1, ECO:0000313|Proteomes:UP000095009};
RN   [1] {ECO:0000313|EMBL:ODQ64692.1, ECO:0000313|Proteomes:UP000095009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ64692.1,
RC   ECO:0000313|Proteomes:UP000095009};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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}.
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DR   EMBL; KV454411; ODQ64692.1; -; Genomic_DNA.
DR   EnsemblFungi; ODQ64692; ODQ64692; NADFUDRAFT_52319.
DR   OrthoDB; 1034517at2759; -.
DR   Proteomes; UP000095009; 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:UP000095009};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          60..355
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   370 AA;  39293 MW;  60BAF327FDA6F16C CRC64;
     MPASPMFGPD GISRGGTPVE ASEDVRILGY DPLIPPGLLQ NQIAPNAISQ HTVSKGRRDA
     IKIISGTSDK LLCIVGPCSI HDPEAALVYA ARMKALADEL NDDLVIIMRA YLEKPRTTVG
     WKGLINDPDV DESFDINKGL SVSRKLFCDI TSSGVPIASE MLDTISPQYL ADLLSLGAIG
     ARTTESQLHR ELASGLSFPI GFKNGTDGGL DVALDAVQAA SHSHHFMGVT KQGIAAITTT
     KGNENCFVIL RGGKNGTNYD EASVKAAKAK LPEGDVLLVD CSHGNSNKDY RNQPLVSAEV
     ARQVANGEDK LIGVMIESNI NEGKQSVGPE GKDGLKYGVS ITDGCVSWEK TVDMLKELAA
     AVKARRALKN
//
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