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Database: UniProt
Entry: A5FG37_FLAJ1
LinkDB: A5FG37_FLAJ1
Original site: A5FG37_FLAJ1 
ID   A5FG37_FLAJ1            Unreviewed;       355 AA.
AC   A5FG37;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE            EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN   OrderedLocusNames=Fjoh_2812 {ECO:0000313|EMBL:ABQ05834.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05834.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ05834.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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}.
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DR   EMBL; CP000685; ABQ05834.1; -; Genomic_DNA.
DR   RefSeq; WP_012024872.1; NZ_MUGZ01000005.1.
DR   AlphaFoldDB; A5FG37; -.
DR   STRING; 376686.Fjoh_2812; -.
DR   KEGG; fjo:Fjoh_2812; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_10; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000006694; Chromosome.
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   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:ABQ05834.1};
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          62..319
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   355 AA;  40029 MW;  0D9FE2DCBF2176AA CRC64;
     MQSIQANNYL VHFNQNAYEA LNNHLRENKY SNIFIIVDTE TNEYCLPKLL PIIETDLNIE
     IIEFEAGEAN KNIETCIQIW HVLTELGADR KSLIINLGGG VVTDLGGFVA STFKRGVDFI
     NIPTTLLSMV DASVGGKTGV DLGNLKNQIG VINVPQMVLI DTQYLETLPQ SEMRSGLAEM
     LKHGLIYDAA YWREFLDISS IDYNGLDELI YRSVEIKNEI VIQDPTEKNI RKALNFGHTL
     GHAIESYFLE SEDKTTLLHG EAIAVGMILE SYISLHKNLI SKGEYIEIKT AIQSIYDQVI
     FEENDIDPIL ELLVHDKKNE YGLIQFALIE GIGKIKINQS VENKLILEAF QDYKS
//
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