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Database: UniProt
Entry: A0A136N232_9BACT
LinkDB: A0A136N232_9BACT
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ID   A0A136N232_9BACT        Unreviewed;       351 AA.
AC   A0A136N232;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE            EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN   ORFNames=UZ09_BCD002000496 {ECO:0000313|EMBL:KXK40230.1};
OS   Bacteroidetes bacterium OLB9.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK40230.1, ECO:0000313|Proteomes:UP000070267};
RN   [1] {ECO:0000313|EMBL:KXK40230.1, ECO:0000313|Proteomes:UP000070267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB9 {ECO:0000313|EMBL:KXK40230.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC       7-phosphate (DAHP) to dehydroquinate (DHQ).
CC       {ECO:0000256|ARBA:ARBA00003485}.
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=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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       2/7. {ECO:0000256|ARBA:ARBA00004661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC       Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412}.
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:KXK40230.1}.
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DR   EMBL; LNBW01000017; KXK40230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136N232; -.
DR   STRING; 1617420.UZ09_BCD002000496; -.
DR   PATRIC; fig|1617420.3.peg.536; -.
DR   Proteomes; UP000070267; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
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:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 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   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KXK40230.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          58..312
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   351 AA;  39510 MW;  AC7CDAC2AB9C7D57 CRC64;
     MKHIVGSEYN IHINNWSALK DTISAIQPSQ VFVLVDENTE KYCLHQLFEH IELQVRIIRI
     PSGERNKTIE TCQHVWSDLL RKGADRHALM LNLGGGVIGD LGGFCAATFM RGIPYIQIPT
     TLLAQVDASL GGKTGVDFGG FKNMIGLIQQ PLAVFVYTDY LETLPDEHMK SGFAELLKHG
     LIADKNEWQT LSKSNLDSLE FENIVYQSLL IKKAVTDQDP GEKGVRKILN FGHTIGHAVE
     SYWMDSRTPL LHGEAVAIGM VSEAFLSYRV GNISETDLFD IRNSIIKLYG HHPKYVKPAE
     QLLDLMKSDK KNYKGEYRFS LLQSIGRAEY DVAVASEFVE ESLLFYKERI G
//
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