AROB_LISMC
ID AROB_LISMC Reviewed; 365 AA.
AC C1KWM7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110}; OrderedLocusNames=Lm4b_01944;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-
CC Rule:MF_00110}.
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:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000255|HAMAP-Rule:MF_00110}.
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DR EMBL; FM242711; CAS05702.1; -; Genomic_DNA.
DR RefSeq; WP_012681369.1; NC_012488.1.
DR AlphaFoldDB; C1KWM7; -.
DR SMR; C1KWM7; -.
DR KEGG; lmc:Lm4b_01944; -.
DR HOGENOM; CLU_001201_0_1_9; -.
DR OMA; YGVIWDA; -.
DR BioCyc; LMON568819:LM4B_RS09830-MON; -.
DR UniPathway; UPA00053; UER00085.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 HAMAP; MF_00110; DHQ_synthase; 1.
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..365
FT /note="3-dehydroquinate synthase"
FT /id="PRO_1000202914"
FT BINDING 106..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 130..131
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 169..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
SQ SEQUENCE 365 AA; 41199 MW; 83D2C2B014547BBA CRC64;
MPEITVRAKS KTYPVYINEF ALEDVREKWT ESLAKFSHVF VLTDEHVAEL HKAKLDAVLA
DLPVVTYYVA PNGEEAKTFR VYEDVMTKLI ETGLDRKAVL IAFGGGVIGD LGGFVAATYM
RGIPFYQVPT TVLAHDSAVG GKVAINHPLG KNMIGNFYQP EAVIYDTQFF ATLPEREMRS
GFAEMIKHAL ISDQTLLRAL MDTFTEPKDF YTKDLTPFLQ RGIEIKANIV AQDETEQGVR
AYLNFGHTFG HALEAYGNFG KWLHGEAITY GMIYALTMSE TIYGLDFDLA EFKTWLKQLG
YDTTFDATVP FNKILENMRH DKKTTFNEIS MVLLEEIGKP VIFKAEDDLI FETYKRVMRN
GGNGI
