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Database: UniProt
Entry: A0A0N7HX60_9BACT
LinkDB: A0A0N7HX60_9BACT
Original site: A0A0N7HX60_9BACT 
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
//
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