ID A0A0H5DRX0_9BACT Unreviewed; 377 AA.
AC A0A0H5DRX0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:CRX39377.1};
GN ORFNames=ELAC_2056 {ECO:0000313|EMBL:CRX39377.1};
OS Estrella lausannensis.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Estrella.
OX NCBI_TaxID=483423 {ECO:0000313|EMBL:CRX39377.1, ECO:0000313|Proteomes:UP000220251};
RN [1] {ECO:0000313|Proteomes:UP000220251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-30 {ECO:0000313|Proteomes:UP000220251};
RA Bertelli C.;
RL Submitted (JUN-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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DR EMBL; CWGJ01000028; CRX39377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5DRX0; -.
DR OrthoDB; 9806583at2; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000220251; 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 GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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:CRX39377.1};
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:UP000220251};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 59..317
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 377 AA; 41045 MW; 49C84B31E16C370D CRC64;
MLSSEVVFTE ERNASKEAAR FARSLQKKVA IISDACVAGL YAPDLMEALI QDGVEANLFT
FPAGEEHKSR LTKERLEDAM FSAGLTRDTL LFALGGGVTL DLAGFVAATY CRGIPLVMIP
TTLLAMVDAA HGGKNGVNAS SGKNLIGSFH LPQKILVDPF YLHSEPLFQI ASGLAEMLKV
ALLFHPDLFF RLQSIALGFS DAALPAIASN IPAAIALKEY VVKQDLHDNG MRHLLNFGHT
IGHALESALD YRIPHGLAVL LGMQLESRIS TRMGILPPED LKVIEEAVSP LLKVYRHNLE
GLSFEKIQRP LYLDKKNKGE GVKMVLLKTI GAALEDKGCF SHPVELSLVR EETDAFFLAI
DASERNGRVF SALEPVL
//
