ID A0A1V3RNV3_9BACT Unreviewed; 347 AA.
AC A0A1V3RNV3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN ORFNames=B0E43_02940 {ECO:0000313|EMBL:OOG78083.1};
OS Algoriphagus sp. A40.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1945863 {ECO:0000313|EMBL:OOG78083.1, ECO:0000313|Proteomes:UP000188460};
RN [1] {ECO:0000313|EMBL:OOG78083.1, ECO:0000313|Proteomes:UP000188460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A40 {ECO:0000313|EMBL:OOG78083.1,
RC ECO:0000313|Proteomes:UP000188460};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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:OOG78083.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUNY01000035; OOG78083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RNV3; -.
DR STRING; 1945863.B0E43_02940; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000188460; Unassembled WGS sequence.
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: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};
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 53..307
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 347 AA; 38310 MW; 6E4B401A7AB9DD87 CRC64;
MDPVIFTSEA KQTLSAVLAQ LSFSRLVVLT DTNTQSNCLP LIGTVLPEGT LFISVTPGEI
HKNLETCSVI WSKMTEAALD RKALMVNLGG GVITDMGGFC ASIYKRGIRF INMPTTLLSQ
VDASVGGKLG VDFNGLKNHL GVFNEPETVL IAPEFLETLS KAELRSGYAE ILKHGLIRDK
VYFSSLKSAN WEDQDWESLI YHSVAIKNAV VTADPKEAGL RKILNFGHTI GHAFESFYLD
TPNHLLHGEA IALGMICEGF LSFQKVGFSY EELDQLTKTL LQIYGKVDFS VNELDPILDL
CLQDKKNEGS TLMFSLLTSI GDCTYNIPVT REEIREAIIH YHNLKTA
//
