ID   A0A0G1U921_9BACT        Unreviewed;       362 AA.
AC   A0A0G1U921;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:KKU90621.1};
GN   ORFNames=UY21_C0021G0021 {ECO:0000313|EMBL:KKU90621.1};
OS   Microgenomates group bacterium GW2011_GWA1_48_10.
OC   Bacteria.
OX   NCBI_TaxID=1618496 {ECO:0000313|EMBL:KKU90621.1, ECO:0000313|Proteomes:UP000034718};
RN   [1] {ECO:0000313|EMBL:KKU90621.1, ECO:0000313|Proteomes:UP000034718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU90621.1}.
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DR   EMBL; LCPD01000021; KKU90621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1U921; -.
DR   PATRIC; fig|1618496.3.peg.936; -.
DR   Proteomes; UP000034718; Unassembled WGS sequence.
DR   GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
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   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          61..320
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   362 AA;  40512 MW;  C0FBAD84D3B46834 CRC64;
     MDTFTINSRF KQYSVAFTEQ FGFFKRLASL ENAVYVVDEN VLRLYPEHFA AIDKERLFPF
     HAVEEKKNME SVLGFVRVLL RQDVRRNTTL VSIGGGITQD VTGCVASILY RGIPWIFVPT
     TLLAQVDSCI GSKTSLNLDS YKNVLGAFYP PDEIYVDVGF VDTLSALDRW SGIGELVKLL
     LMDVSEAADL KRVKREIETL TQNKEGLFAG VKKGLAIKKS YIEEDEFDHG RRNLLNYGHT
     LGHALEGVSD FRIPHGIGVV IGMLHENLIA LRRGRVTPET VGEVNRGILL PNLHLEEMDI
     RAQDFEAGPL LEKMSRDKKR TGAGLAMILP RAPFALERVQ DVSPKECTQT LADLAMQLSL
     RG
//