ID K3ZTD5_SETIT Unreviewed; 438 AA.
AC K3ZTD5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00013031};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN Name=101782627 {ECO:0000313|EnsemblPlants:KQL25495};
GN ORFNames=SETIT_2G290400v2 {ECO:0000313|EMBL:RCV12707.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV12707.1};
RN [1] {ECO:0000313|EMBL:RCV12707.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL25495,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV12707.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV12707.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV12707.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQL25495}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL25495};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; AGNK02001215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003529; RCV12707.1; -; Genomic_DNA.
DR RefSeq; XP_004957492.1; XM_004957435.2.
DR AlphaFoldDB; K3ZTD5; -.
DR STRING; 4555.K3ZTD5; -.
DR EnsemblPlants; KQL25495; KQL25495; SETIT_029865mg.
DR GeneID; 101782627; -.
DR Gramene; KQL25495; KQL25495; SETIT_029865mg.
DR KEGG; sita:101782627; -.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_001201_0_2_1; -.
DR InParanoid; K3ZTD5; -.
DR OMA; TGINTPY; -.
DR OrthoDB; 865at2759; -.
DR Proteomes; UP000004995; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003856; F:3-dehydroquinate 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 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:UP000004995}.
FT DOMAIN 142..400
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 438 AA; 47057 MW; 99C30A9936FDB378 CRC64;
MAASASSLLA AAVSSSCAAI SSRLPRGAPA AASVPSPSRQ SCSSLRASLA RRQQSRFVAS
VAPTMQPPAE SRVSTVVDVD LGDRSYPIYI GAGLLDEPDL LQRHVHGKRV LVVTNTTVAP
LYLEKVSWAL THNNPNVSVE SVILPDGEKY KDMDTMMKVF DKAIESRLDR RCTFVALGGG
VIGDMCGFAA AAFLRGVNFI QIPTTLMAQV DSSVGGKTGI NHPLGKNLIG AFYQPQCVLI
DTDTLNTLPD RELASGIAEV VKYGLIRDAP FFEWQEQNMS ALLAREPSAL VYAIKRSCEN
KAEVVAQDEK ESGLRATLNL GHTFGHAIET GTGYGAWLHG EAVAAGTVMA ADMSHRLGWI
DESIKKRTVD ILAQAKLPIT PPETMTVEKF KSIMAVDKKV ADGLLRLILL KGPLGSCVFT
GEYDRKALDE TLHAFCNN
//
