ID A0A2T8HJ40_9SPHI Unreviewed; 354 AA.
AC A0A2T8HJ40;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PVH25390.1};
GN ORFNames=DC487_10775 {ECO:0000313|EMBL:PVH25390.1};
OS Sphingobacterium corticibacter.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=2171749 {ECO:0000313|EMBL:PVH25390.1, ECO:0000313|Proteomes:UP000245627};
RN [1] {ECO:0000313|EMBL:PVH25390.1, ECO:0000313|Proteomes:UP000245627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2c-3 {ECO:0000313|EMBL:PVH25390.1,
RC ECO:0000313|Proteomes:UP000245627};
RA Li Y.;
RT "Sphingobacterium cortibacter sp. nov.";
RL Submitted (APR-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:PVH25390.1}.
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DR EMBL; QDKG01000003; PVH25390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HJ40; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000245627; 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 Reference proteome {ECO:0000313|Proteomes:UP000245627};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..315
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 354 AA; 39269 MW; 09E5EF063D78C64B CRC64;
MQQIESLGYK VYFEDDLASL QPFITDGGYS NVLILVDINT NDHCLPVLQA AIPDIVDYDI
IEVDPGEENK NIDFCIGIWK TMLDFGADRK ALMINLGGGV VTDMGGFAAS TYKRGIDFIQ
IPTTLLAQVD ASVGGKTGID LDNFKNIIGT FTQPKAVFIS GKFLESLDSR QLLSGFAEII
KHGLIQDKAL FKRCQQISIE EIDSQIVYDS VGIKNKIVKE DPTENNIRKI LNFGHTIGHA
VEGYSLANDQ NPLLHGEAVA IGMLCEAYLS TQSGTLPEEE MKEIEQYLLR TYPYYSISPS
IDEELFRLMR NDKKNEANQI GFALLNAIGD CTYNKYVDEA GIKAALDYYR GLEG
//
