ID AROB_CHLTA Reviewed; 373 AA.
AC Q3KLY7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000250|UniProtKB:P07639};
DE Short=DHQS {ECO:0000250|UniProtKB:P07639};
DE EC=4.2.3.4 {ECO:0000250|UniProtKB:P07639};
GN Name=aroB {ECO:0000250|UniProtKB:P07639}; OrderedLocusNames=CTA_0401;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC {ECO:0000250|UniProtKB:P07639}.
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:0000250|UniProtKB:P07639};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07639};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000250|UniProtKB:P07639};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000250|UniProtKB:P07639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07639}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000305}.
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DR EMBL; CP000051; AAX50635.1; -; Genomic_DNA.
DR RefSeq; WP_009871722.1; NC_007429.1.
DR AlphaFoldDB; Q3KLY7; -.
DR SMR; Q3KLY7; -.
DR KEGG; cta:CTA_0401; -.
DR HOGENOM; CLU_001201_0_1_0; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000002532; Chromosome.
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 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; Aromatic amino acid biosynthesis; Cobalt;
KW Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc.
FT CHAIN 1..373
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000231077"
FT BINDING 67..72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 101..105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 125..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q6GGU4"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P9WPX9"
SQ SEQUENCE 373 AA; 41153 MW; 30A300C4C37E7EAA CRC64;
MIELVTDSPH PIHLVDSLQN PKLFASLSTD FPLIFITNTK LNALILPPLL DLARSLGFSV
ETLTIPEGEE TKTGDTFLSL HQQLTDLNVP RQATLIGVGG GVILDIAGFV AATHCRGMPF
IAIPTTLVAM IDASIGGKNG INLNHIKNRI GSFYLPKAVW ICPRKLSFLP QQELHHGIAE
CIKHAYIADS AILPLLQDPN ALKKEDKLSL LIKKNCLCKA SVVQQDVRDY AKRQILNFGH
TLGHALEMLF IGKIPHSCAI SVGMVLETKL SLSLGVARSP AILHSLIQDL LRYQLPVSLK
DLYMRAQIPP HNCDQILSAL TYDKKKQNTP LPPFVMIEEI GLAASFDGRF CQTISKHILT
KVLEEEFYAM HNN
//
