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Database: UniProt
Entry: B6JV24_SCHJY
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Original site: B6JV24_SCHJY 
ID   B6JV24_SCHJY            Unreviewed;       369 AA.
AC   B6JV24;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=SJAG_00224 {ECO:0000313|EMBL:EEB05225.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB05225.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB05225.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(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; 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; KE651166; EEB05225.1; -; Genomic_DNA.
DR   RefSeq; XP_002171518.1; XM_002171482.2.
DR   AlphaFoldDB; B6JV24; -.
DR   STRING; 402676.B6JV24; -.
DR   EnsemblFungi; EEB05225; EEB05225; SJAG_00224.
DR   GeneID; 7047811; -.
DR   JaponicusDB; SJAG_00224; -.
DR   VEuPathDB; FungiDB:SJAG_00224; -.
DR   eggNOG; ENOG502QPSU; Eukaryota.
DR   HOGENOM; CLU_030903_1_0_1; -.
DR   OMA; QPLVMEN; -.
DR   OrthoDB; 72311at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IBA:GO_Central.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
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:UP000001744};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          56..352
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   369 AA;  39754 MW;  0874AEA6FD0BE4E7 CRC64;
     MSPAFQANGS INTESIEDQR ILGYNPLVPP ALLQQELPVS EASANVVRQG RRDIQAVLGG
     KDDRLVVVVG PCSIHDPVLA MEYAKLLKPK AEELKNELVI IMRCYLEKPR TTVGWKGLVN
     DPDLDGSYAI NKGLRISRKM YCDVTNFGVP LGSEMLDTIS PQFFSDMLSF GAIGARTTES
     QLHRELASAL SFPIGFKNST DGSVGIAIDA IGATAHPHTM LGVNKQGIAA ICMTAGNKDT
     FIILRGGKHG PNYDAKNVAA VREALEKANI TPRIMIDCSH GNSSKDHRNQ PKVCHSIAEQ
     VAAGDEALMG VMIESHINEG RQNAKIAPGV KETLKYGVSI TDACVSWEQT APMLEELAAA
     VRARRAGRA
//
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