ID A0A0N7HX60_9BACT Unreviewed; 335 AA.
AC A0A0N7HX60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:ALJ01145.1};
GN ORFNames=DC20_02470 {ECO:0000313|EMBL:ALJ01145.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ01145.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALJ01145.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALJ01145.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP012643; ALJ01145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N7HX60; -.
DR STRING; 512763.DC20_02470; -.
DR KEGG; rti:DC20_02470; -.
DR PATRIC; fig|512763.3.peg.550; -.
DR Proteomes; UP000061382; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR NCBIfam; TIGR01357; aroB; 1.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..298
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 335 AA; 37973 MW; A9368BC59CDB1D4A CRC64;
MGQWQQLLQN RAFKKTVVLV DENTHRHCYA LLKPYLPQEH HVVHIKSGEE NKNLATCEHV
WRELTEQGLD RWSLLVNLGG GVLTDLGGFC ASLYKRGIRF VNVPTTLLSQ VDASVGGKTG
IDFMGFKNHI GVFQEPLAVL VNPTFLQTLD MRQMKSGYAE IIKHWLIMDA EKFYEQRYIG
MFTEDWTDLI RHSIDIKSRV VTADPLENGL RKILNFGHTI GHAVESFYLE QPGQVLLHGE
AIAVGMLCEA WLSVQKGLLP EDELNQIETF ILSIYEKVNL AQADLQAISQ LCLHDKKNDG
ATINCTLLQK IGEAVYDQPI TLPEVQSALR YYQLL
//