ID A0A374VB91_9BACE Unreviewed; 353 AA.
AC A0A374VB91;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN Name=aroB {ECO:0000313|EMBL:RGM48845.1};
GN ORFNames=DXC10_04340 {ECO:0000313|EMBL:RGM48845.1};
OS Bacteroides sp. OM08-11.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292284 {ECO:0000313|EMBL:RGM48845.1, ECO:0000313|Proteomes:UP000262405};
RN [1] {ECO:0000313|EMBL:RGM48845.1, ECO:0000313|Proteomes:UP000262405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM08-11 {ECO:0000313|EMBL:RGM48845.1,
RC ECO:0000313|Proteomes:UP000262405};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGM48845.1}.
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DR EMBL; QSTJ01000002; RGM48845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374VB91; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000262405; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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:RGM48845.1};
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:UP000262405};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 56..313
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 353 AA; 39155 MW; 3393670538B370E0 CRC64;
MSKQKVILCE GLGNSLTLAI EQCPHDKLFI LTDEHTHRLC LPQLKDIAVL KNATEIIIGA
EDLHKNLETL ASVWQALSEQ GATRHSLLIN LGGGMVTDLG GFAASTFKRG IAYINIPTTL
LAMVDASVGG KTGINFNGLK NEIGVFAPAT SVLLETEFLR SLDAHNFFSG YAEMLKHGLI
STPEHLAELL SFDTEKIDYV GLKTMVGRSV RVKEDIVEQD PQEHGIRKAL NLGHTVGHAF
ESLALAENRP VLHGYAVAWG LVCELYLSYI KVGFPKDRMR QVIQFVNENY GGFVFNCKQY
DRLYELMGHD KKNAAGIINF TLLKEVGEIC LNQTTDKATI FEMFDFYREC MGV
//
