ID B0D7J1_LACBS Unreviewed; 417 AA.
AC B0D7J1;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
GN ORFNames=LACBIDRAFT_318960 {ECO:0000313|EMBL:EDR09661.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR09661.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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 -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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DR EMBL; DS547099; EDR09661.1; -; Genomic_DNA.
DR RefSeq; XP_001880010.1; XM_001879975.1.
DR AlphaFoldDB; B0D7J1; -.
DR STRING; 486041.B0D7J1; -.
DR GeneID; 6075681; -.
DR KEGG; lbc:LACBIDRAFT_318960; -.
DR HOGENOM; CLU_030903_0_1_1; -.
DR InParanoid; B0D7J1; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000001194; 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; 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 SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 59..361
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 45062 MW; FCF1A249E58EFD7F CRC64;
MYNVSPFPDF EDAQKVHQYI QDRRVIGYDP LVQPALLRHE IVSSKNSQRT IASARYNAAR
ILAGHDDRVL VVVGPCSIHS PEQALEYAHL LKAKLNDWPN LLIVMRAYFE KPRTTVGWKG
LINDPDIDGS FKINKGLRIA RQLLCDLTDL GVPVGSELLD TISPQYIADL ISWGAIGART
TESQLHRELA SGVSFPIGFK NGTDGSVSVA IDAMSSASNP HAFMGVTEQG LASIVKTRGN
QDVHVILRGG TGGPNYASEH VRKAVAVIEK KSKGKEDGKI PSVMIDCSHG NSLKNHNNQP
KVLSDIAEQL AAGEKNITGV MIESHIHAGR QDVPADGPSA LKWGVSITDA CVDWDTTVKM
LTELDEAVSK RRETLIAEGF KRPAAFELAQ AADVSAPPQT AEATVQTQAL DAPVSTS
//
