AROB_HELPY
ID AROB_HELPY Reviewed; 343 AA.
AC P56081;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000303|PubMed:18503755};
DE EC=4.2.3.4 {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:18503755};
GN Name=aroB {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000303|PubMed:18503755};
GN OrderedLocusNames=HP_0283;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2] {ECO:0007744|PDB:3CLH}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=18503755; DOI=10.1016/j.bbrc.2008.05.070;
RA Liu J.S., Cheng W.C., Wang H.J., Chen Y.C., Wang W.C.;
RT "Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate
RT synthase.";
RL Biochem. Biophys. Res. Commun. 373:1-7(2008).
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, ECO:0000269|PubMed:18503755}.
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 ECO:0000269|PubMed:18503755};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000269|PubMed:18503755};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00110,
CC ECO:0000269|PubMed:18503755};
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18503755}.
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; AE000511; AAD07351.1; -; Genomic_DNA.
DR PIR; C64555; C64555.
DR RefSeq; NP_207081.1; NC_000915.1.
DR RefSeq; WP_001156090.1; NC_018939.1.
DR PDB; 3CLH; X-ray; 2.40 A; A/B=1-343.
DR PDBsum; 3CLH; -.
DR AlphaFoldDB; P56081; -.
DR SMR; P56081; -.
DR IntAct; P56081; 1.
DR STRING; 85962.C694_01430; -.
DR PaxDb; P56081; -.
DR EnsemblBacteria; AAD07351; AAD07351; HP_0283.
DR KEGG; hpy:HP_0283; -.
DR PATRIC; fig|85962.47.peg.303; -.
DR eggNOG; COG0337; Bacteria.
DR OMA; IKMAVCF; -.
DR PhylomeDB; P56081; -.
DR BRENDA; 4.2.3.4; 2604.
DR UniPathway; UPA00053; UER00085.
DR EvolutionaryTrace; P56081; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cobalt; Cytoplasm; Lyase; Metal-binding; NAD; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..343
FT /note="3-dehydroquinate synthase"
FT /id="PRO_0000140745"
FT BINDING 61..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:18503755"
FT BINDING 95..96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:18503755"
FT BINDING 119..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:18503755"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 141
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:0000269|PubMed:18503755"
FT BINDING 159..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110,
FT ECO:0000269|PubMed:18503755"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00110"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3CLH"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:3CLH"
FT TURN 225..230
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3CLH"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 248..265
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:3CLH"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3CLH"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:3CLH"
SQ SEQUENCE 343 AA; 39120 MW; 5AEAC2F4DE816D13 CRC64;
MQEILIPLKE KNYKVFLGEL PEIKLKQKAL IISDSIVAGL HLPYLLERLK ALEVRVCVIE
SGEKYKNFHS LERILNNAFE MQLNRHSLMI ALGGGVISDM VGFASSIYFR GIDFINIPTT
LLAQVDASVG GKTGINTPYG KNLIGSFHQP KAVYMDLAFL KTLEKREFQA GVAEIIKMAV
CFDKNLVERL ETKDLKDCLE EVIFQSVNIK AQVVVQDEKE QNIRAGLNYG HTFGHAIEKE
TDYERFLHGE AIAIGMRMAN DLALSLGMLT LKEYERIENL LKKFDLIFHY KILDLQKFYE
RLFLDKKSEN KTIKFILPKG VGAFEVASHI PKETIIKVLE KWH
