ID G8X7B3_FLACA Unreviewed; 360 AA.
AC G8X7B3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN OrderedLocusNames=FCOL_00360 {ECO:0000313|EMBL:AEW84927.1};
OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW84927.1, ECO:0000313|Proteomes:UP000005638};
RN [1] {ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW84927.1, ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RX PubMed=22535941; DOI=10.1128/JB.00281-12;
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT 49512.";
RL J. Bacteriol. 194:2763-2764(2012).
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; CP003222; AEW84927.1; -; Genomic_DNA.
DR AlphaFoldDB; G8X7B3; -.
DR STRING; 1041826.FCOL_00360; -.
DR KEGG; fco:FCOL_00360; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_1_10; -.
DR Proteomes; UP000005638; Chromosome.
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:UP000005638};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 67..324
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 360 AA; 40828 MW; DAB7EF7E4DE1A02C CRC64;
MHKKLNSQKM QVSSSIHFVN DNYSILNLFL KKNHFSKIFI LVDENTNEYC LPRFLPYLET
EVSLEIIELE AGEETKTIDT CVNVWEALTE LEADRKSLII NIGGGVITDM GGFIASSFKR
GLSFINIPTT LLSMVDASIG GKNGVDLGGL KNQIGTITQP DMVLIDTQYL HSLSQRELRS
GLAEMLKHGL IANKNHWNHF KDISRINFQD FDSIIEESIA IKTKIVEQDP KEKGIRKTLN
FGHTLGHAIE TYFLEHPNKE RLLHGEAIAC GMILEAFLSF KKELLSVDEY LEIKNLIRTL
YDSISFDTDE IQAIMNLLIH DKKNEFGKVQ FSLLNSIGQC VINQIVEEVD ILTAFNDYKN
//
