ID A5I3R7_CLOBH Unreviewed; 379 AA.
AC A5I3R7; A7G571;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:CAL83686.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:CAL83686.1};
GN Name=aroB {ECO:0000313|EMBL:CAL83686.1};
GN OrderedLocusNames=CBO2145 {ECO:0000313|EMBL:CAL83686.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL83686.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL83686.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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};
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DR EMBL; AM412317; CAL83686.1; -; Genomic_DNA.
DR RefSeq; WP_011986649.1; NC_009698.1.
DR RefSeq; YP_001254642.1; NC_009495.1.
DR RefSeq; YP_001387936.1; NC_009698.1.
DR AlphaFoldDB; A5I3R7; -.
DR GeneID; 5186400; -.
DR KEGG; cbh:CLC_2089; -.
DR KEGG; cbo:CBO2145; -.
DR PATRIC; fig|413999.7.peg.2114; -.
DR HOGENOM; CLU_001201_0_1_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR CDD; cd08197; DOIS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAL83686.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 82..339
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 379 AA; 42855 MW; 0BF5C1560EA68219 CRC64;
MYMNLAQKIN DDYYHPEVKL ETNLLESSPI YLGCNIWRES LLEKMMDLNT DKFFLITDDV
VYNLFGKELL EYMNRKVSVK LIKLPSGEKH KNIKVFNDLM EDLFDNNVTK SSILISLGGG
VVGNITGLAA ALAFRGIRFF HIPTTFMSQT DSILSRKQGI NSFYGKNMIG SYYTPLFNFI
DTSFLTFDSE RFIRGSFVET VKNGFIYNAD FLNKLKSVIK NDFNVNQEGI FNLVKMSIES
KLPIMKADPT EKGLAMILEY GHTVGHAIEK LSYGKLSHGE SVSIGMMVAA RVSEKLGYLS
KQDVKEHLDI LSALKTPTKI PSNIKISDII NKIKLDNKKD MNGIRFVVLE SIGKCINTDG
SYMIKVPFNI INEAIEETC
//
