ID   AROB_CHLFF              Reviewed;         379 AA.
AC   Q255H6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=CF0290;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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; AP006861; BAE81062.1; -; Genomic_DNA.
DR   RefSeq; WP_011457843.1; NC_007899.1.
DR   AlphaFoldDB; Q255H6; -.
DR   SMR; Q255H6; -.
DR   STRING; 264202.CF0290; -.
DR   KEGG; cfe:CF0290; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_0; -.
DR   OMA; YGVIWDA; -.
DR   OrthoDB; 1677032at2; -.
DR   UniPathway; UPA00053; UER00085.
DR   Proteomes; UP000001260; 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   TIGRFAMs; TIGR01357; aroB; 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..379
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000094485"
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         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPX9"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPX9"
SQ   SEQUENCE   379 AA;  42360 MW;  E10C9F12593A3E89 CRC64;
     MIEHFISDPH NVKFVESIFN KKLFSSISTD YPLVIISDSH VAEKILPPVL GFIDSLGYRV
     ILLTFPPGEK NKTWEIFISL QNQLVDHGVS LGATIMGIGG GIVLDMAGFL ASTYCRGIQL
     FLIPTTMTAM IDASIGGKNG INLRGLKNRL GTFYPPKDVW VCPEFLTTLS KQEWCYGISE
     SIKHGCVADA YIWEFLHSYG DTLFSSRTIL NEFIKRNCQI KAVIAAKDPK DKNLRKILNF
     GHTIAHALET LSEGHIPHGL AVSVGMMIEI KISLESGIMK NPSLVEQLYN LSNNFNLPTT
     LEELRDLIPQ HFLHRFYHPE NIITTLGYDK KNLSNKALRM VMIEHLGRVA PCSGSYCATP
     KMGILYEVLK SECDAVRNN