AROB_CORP2
ID AROB_CORP2 Reviewed; 359 AA.
AC P96749; D9QAN8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=CpC231_1138;
OS Corynebacterium pseudotuberculosis (strain C231).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=681645;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C231;
RX PubMed=9234753; DOI=10.1128/iai.65.8.3048-3056.1997;
RA Simmons C.P., Hodgson A.L.M., Strugnell R.A.;
RT "Attenuation and vaccine potential of aroQ mutants of Corynebacterium
RT pseudotuberculosis.";
RL Infect. Immun. 65:3048-3056(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231;
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL PLoS ONE 6:E18551-E18551(2011).
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=NAD(+); Xref=ChEBI:CHEBI:57540;
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 -!- 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,
CC ECO:0000305}.
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DR EMBL; U88628; AAB71614.1; -; Genomic_DNA.
DR EMBL; CP001829; ADL10614.1; -; Genomic_DNA.
DR RefSeq; WP_014367126.1; NC_017301.2.
DR AlphaFoldDB; P96749; -.
DR SMR; P96749; -.
DR STRING; 1719.CPTC_01705; -.
DR EnsemblBacteria; ADL10614; ADL10614; CpC231_1138.
DR GeneID; 12299569; -.
DR KEGG; cpq:CPC231_05760; -.
DR PATRIC; fig|681645.3.peg.1191; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_3_11; -.
DR OMA; YGVIWDA; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000000276; Chromosome.
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;
KW Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140735"
FT BINDING 69..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 103..107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 127..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT CONFLICT 208..213
FT /note="VEGYLP -> GRILA (in Ref. 1; AAB71614)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> G (in Ref. 1; AAB71614)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> A (in Ref. 1; AAB71614)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="G -> D (in Ref. 1; AAB71614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 38553 MW; 58BF78A771F4F59F CRC64;
MQTIEVNGAS PYEVTIGHNL FKDVAKSMSQ LGANQAAIIT QPVMGETAKK LVGAIEALGK
EATIITVPDA EDGKNLNVAG DCWDVLGRKA FGRKDVIISL GGGAVTDLAG FVAACWMRGI
AVIHVPTTLL SMVDAAVGGK TGINTSAGKN LVGAFHEPSG VFIDLDMIAT LPDREKISGS
AEIIKTGFIA DTKILSLYEE DPEACFNVEG YLPELIARSV AVKARVVASD LREAGQREIL
NYGHTFGHAV ELKEKYEWRH GNAVSVGMMF VAALARNRGL ITDELYLRHK NILSSVGLPT
TYPEGHFAEL YQAMLRDKKN RDGRIRFVAL IGAGKTIRIE DADRAELIAA YETLNKGGV
