AROD_STAAR
ID AROD_STAAR Reviewed; 238 AA.
AC Q6GII7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; OrderedLocusNames=SAR0860;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROSHIKIMATE,
RP ACTIVE SITE, AND SUBUNIT.
RC STRAIN=MRSA252;
RX PubMed=15229896; DOI=10.1002/prot.20165;
RA Nichols C.E., Lockyer M., Hawkins A.R., Stammers D.K.;
RT "Crystal structures of Staphylococcus aureus type I dehydroquinase from
RT enzyme turnover experiments.";
RL Proteins 56:625-628(2004).
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC bond of the aromatic ring to yield 3-dehydroshikimate.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00214};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:15229896}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571856; CAG39869.1; -; Genomic_DNA.
DR RefSeq; WP_000150036.1; NC_002952.2.
DR PDB; 1SFJ; X-ray; 2.40 A; A/B=1-238.
DR PDB; 1SFL; X-ray; 1.90 A; A/B=1-238.
DR PDBsum; 1SFJ; -.
DR PDBsum; 1SFL; -.
DR AlphaFoldDB; Q6GII7; -.
DR SMR; Q6GII7; -.
DR DrugBank; DB04347; 3-Dehydroshikimate.
DR KEGG; sar:SAR0860; -.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; ATMAMGE; -.
DR OrthoDB; 1298468at2; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q6GII7; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProt.
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 CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Schiff base.
FT CHAIN 1..238
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138811"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:15229896"
FT ACT_SITE 160
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:15229896"
FT BINDING 35..37
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 70
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:15229896"
FT BINDING 202
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:15229896"
FT BINDING 225
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:15229896"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:1SFL"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:1SFL"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1SFL"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1SFL"
SQ SEQUENCE 238 AA; 27053 MW; A88C60679FCCBCF4 CRC64;
MTHVEVVATI TPQLYIEETL IQKINHRIDA IDVLELRIDQ FENVTVDQVA EMITKLKVMQ
DSFKLLVTYR TKLQGGYGQF TNDSYLNLIS DLANINGIDM IDIEWQADID IEKHQRIITH
LQQYNKEVII SHHNFESTPP LDELQFIFFK MQKFNPEYVK LAVMPHNKND VLNLLQAMST
FSDTMDCKVV GISMSKLGLI SRTAQGVFGG ALTYGCIGEP QAPGQIDVTD LKAQVTLY
