AROD_STRMU
ID AROD_STRMU Reviewed; 225 AA.
AC Q8DUW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SMU_777;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RA Su X.-D., Huang Y.H., Liu X.;
RT "The crystal structure of smu.777 from Streptococcus mutans UA159.";
RL Submitted (JAN-2010) to the PDB data bank.
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 -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; AE014133; AAN58497.1; -; Genomic_DNA.
DR RefSeq; NP_721191.1; NC_004350.2.
DR RefSeq; WP_002261931.1; NC_004350.2.
DR PDB; 3L9C; X-ray; 1.60 A; A/B=1-225.
DR PDBsum; 3L9C; -.
DR AlphaFoldDB; Q8DUW4; -.
DR SMR; Q8DUW4; -.
DR STRING; 210007.SMU_777; -.
DR PRIDE; Q8DUW4; -.
DR EnsemblBacteria; AAN58497; AAN58497; SMU_777.
DR GeneID; 66817779; -.
DR KEGG; smu:SMU_777; -.
DR PATRIC; fig|210007.7.peg.688; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; FATMSMG; -.
DR PhylomeDB; Q8DUW4; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q8DUW4; -.
DR Proteomes; UP000002512; 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; Reference proteome; Schiff base.
FT CHAIN 1..225
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000043194"
FT ACT_SITE 118
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 143
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 30..32
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 62
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 186
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 205
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 209
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:3L9C"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3L9C"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3L9C"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:3L9C"
SQ SEQUENCE 225 AA; 25783 MW; D312E76A8E919789 CRC64;
MKIVVPVMPQ NIEEANQLDL TRIDSTDIIE WRADYLVKDD ILTVAPAIFE KFSGHEVIFT
LRTEKEGGNI SLSNEDYLAI IRDIAALYQP DYIDFEYFSY RDVLEEMYDF SNLILSYHNF
EETPENLMEV FSELTALAPR VVKIAVMPKN EQDVLDLMNY TRGFKTLNPN QEYVTMSMSK
LGRISRLAAD LIGSSWTFAS LEQESAPGQI SLADMRKIKE VLDAN
