ID A0A0T9Y3Y1_SALET Unreviewed; 362 AA.
AC A0A0T9Y3Y1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684, ECO:0000256|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031, ECO:0000256|HAMAP-Rule:MF_00110};
GN Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110,
GN ECO:0000313|EMBL:SUE45688.1};
GN ORFNames=B7N00_17725 {ECO:0000313|EMBL:EDG5018788.1}, B7N01_11040
GN {ECO:0000313|EMBL:EDG4994961.1}, B7N35_03765
GN {ECO:0000313|EMBL:EDG5125148.1}, B7N72_07800
GN {ECO:0000313|EMBL:EDG5370009.1}, B7N78_06790
GN {ECO:0000313|EMBL:EDG5279484.1}, B7N80_01630
GN {ECO:0000313|EMBL:EDG5287091.1}, B7N84_12230
GN {ECO:0000313|EMBL:EDG5267102.1}, DRU31_07595
GN {ECO:0000313|EMBL:EBS2452190.1}, E0916_12700
GN {ECO:0000313|EMBL:ECF1446809.1}, EJV93_15365
GN {ECO:0000313|EMBL:ECA2722567.1}, ERS008202_03420
GN {ECO:0000313|EMBL:CNU73503.1}, ERS008207_04417
GN {ECO:0000313|EMBL:CNV14620.1}, EWC73_03230
GN {ECO:0000313|EMBL:ECE8535241.1}, G0B02_04330
GN {ECO:0000313|EMBL:HAC6378363.1}, G0D18_07660
GN {ECO:0000313|EMBL:HAC6680540.1}, G2206_10790
GN {ECO:0000313|EMBL:HAE0435247.1}, NCTC5754_00470
GN {ECO:0000313|EMBL:SUE45688.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45688.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000042394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU73503.1,
RC ECO:0000313|Proteomes:UP000039541}, and D4891
RC {ECO:0000313|EMBL:CNV14620.1, ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6378363.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378363.1}, M123
RC {ECO:0000313|EMBL:HAC6680540.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435247.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE45688.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45688.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2452190.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4994961.1}, 138330
RC {ECO:0000313|EMBL:EDG5287091.1}, 143652
RC {ECO:0000313|EMBL:EDG5370009.1}, 273631
RC {ECO:0000313|EMBL:EDG5018788.1}, 330535
RC {ECO:0000313|EMBL:EDG5267102.1}, 333944
RC {ECO:0000313|EMBL:EDG5279484.1}, 337042
RC {ECO:0000313|EMBL:EDG5125148.1}, 387147
RC {ECO:0000313|EMBL:EBS2452190.1}, 470200
RC {ECO:0000313|EMBL:ECE8535241.1}, 598023
RC {ECO:0000313|EMBL:ECA2722567.1}, and 692616
RC {ECO:0000313|EMBL:ECF1446809.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAC6680540.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378363.1}, M123
RC {ECO:0000313|EMBL:HAC6680540.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435247.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC {ECO:0000256|ARBA:ARBA00003485, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001393, ECO:0000256|HAMAP-
CC Rule:MF_00110};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|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:0000256|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00110}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412,
CC ECO:0000256|HAMAP-Rule:MF_00110}.
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DR EMBL; CQPC01000052; CNU73503.1; -; Genomic_DNA.
DR EMBL; CQPD01000065; CNV14620.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000004; EBS2452190.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000007; ECA2722567.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000002; ECE8535241.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000006; ECF1446809.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000009; EDG4994961.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000013; EDG5018788.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000002; EDG5125148.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000005; EDG5267102.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000003; EDG5279484.1; -; Genomic_DNA.
DR EMBL; AAMEML010000001; EDG5287091.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000005; EDG5370009.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000002; HAC6378363.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000004; HAC6680540.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000009; HAE0435247.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE45688.1; -; Genomic_DNA.
DR RefSeq; WP_000439824.1; NZ_WFIN01000005.1.
DR AlphaFoldDB; A0A0T9Y3Y1; -.
DR SMR; A0A0T9Y3Y1; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; Unassembled WGS sequence.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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 HAMAP; MF_00110; DHQ_synthase; 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, ECO:0000256|HAMAP-
KW Rule:MF_00110};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00110};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_00110};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00110};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00110};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00110};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 67..325
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 71..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 129..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 169..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 362 AA; 38680 MW; 53978398882E2FFB CRC64;
MERITVTLGE RSYPITIAAG LFNEPASFLP LKSGDQVMLV TNETLAPLYL DKVRGVLERA
GVNVDSVILP DGEQYKSLTV LDTVFTALLK KPHGRDTTLV ALGGGVIGDL TGFAAASYQR
GVRFIQVPTT LLSQVDSSVG GKTAVNHPLG KNMIGAFYQP ASVVVDLDCL KTLPARELAS
GLAEVIKYGI ILDADFFTWL EGNLDALLRL DGPAMAYCIR RCCELKAEVV AADEREAGLR
ALLNLGHTFG HAIEAEMGYG NWLHGEAVAA GIVMAARASE RLGQFSSADT QRIIALLERA
GLPVNGPCEM SAQDYLPHML RDKKVLAGEL RLVLPLAIGK SEVRGGVSHE VVLSAIADCQ
QA
//
