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Database: UniProt
Entry: A0A0D3E2R7_BRAOL
LinkDB: A0A0D3E2R7_BRAOL
Original site: A0A0D3E2R7_BRAOL 
ID   A0A0D3E2R7_BRAOL        Unreviewed;       437 AA.
AC   A0A0D3E2R7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00013031};
DE            EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN   Name=106318526 {ECO:0000313|EnsemblPlants:Bo9g022160.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g022160.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo9g022160.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo9g022160.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC         dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001393};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000256|ARBA:ARBA00004661}.
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DR   RefSeq; XP_013611997.1; XM_013756543.1.
DR   AlphaFoldDB; A0A0D3E2R7; -.
DR   STRING; 109376.A0A0D3E2R7; -.
DR   EnsemblPlants; Bo9g022160.1; Bo9g022160.1; Bo9g022160.
DR   GeneID; 106318526; -.
DR   Gramene; Bo9g022160.1; Bo9g022160.1; Bo9g022160.
DR   KEGG; boe:106318526; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_001201_0_2_1; -.
DR   OMA; TGINTPY; -.
DR   OrthoDB; 865at2759; -.
DR   Proteomes; UP000032141; Chromosome C9.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd08195; DHQS; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   HAMAP; MF_00110; DHQ_synthase; 1.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   NCBIfam; TIGR01357; aroB; 1.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT   DOMAIN          141..399
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   437 AA;  47235 MW;  F597DEF7BA867CEA CRC64;
     MAANAVSLSI SSTPKTLHSL QAQTRGLIPP PTISFPKSSS SLSSTAISIS RSRVRAGPSQ
     LVNEPANAMA TPPTIVEVDL GSRSYPIYIG AGLLDQSHLL QRHVHGKKVL VVTNERVAPL
     YLDKTVHALT IGNPNVTVES VILPDGEKYK DMDTLMKVFD KAIESRLDRR STFVALGGGV
     IGDMCGYAAA SYLRGVNFIQ IPTTVMAQVD SSVGGKTGIN HRLGKNLIGA FYQPQCVLVD
     TDTLNTLPDR EMASGLAEVI KYGLIRDADF FEWQEKNIEA LLARDPAALA YAIKRSCENK
     ADVVSQDEKE SGLRATLNLG HTFGHAIETG FGYGEWLHGE AVAAGTVMAV DMSYRLGWID
     DSIVERVNNI LKRAKLPTTP PESMTVSMFK SIMAVDKKVA DGLLRLILLK GPLGNCVFTG
     DYDREALDAT LRAFSKS
//
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