AROD_STRP1
ID AROD_STRP1 Reviewed; 228 AA.
AC P63590; Q48ZH6; Q9A0E5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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};
GN OrderedLocusNames=SPy_0809, M5005_Spy0624;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "The structure of a putative 3-dehydroquinate dehydratase from
RT Streptococcus pyogenes.";
RL Submitted (JUL-2011) 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; AE004092; AAK33746.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51242.1; -; Genomic_DNA.
DR RefSeq; NP_269025.1; NC_002737.2.
DR PDB; 2OCZ; X-ray; 1.85 A; A=1-228.
DR PDBsum; 2OCZ; -.
DR AlphaFoldDB; P63590; -.
DR SMR; P63590; -.
DR STRING; 1314.HKU360_00635; -.
DR PaxDb; P63590; -.
DR EnsemblBacteria; AAK33746; AAK33746; SPy_0809.
DR KEGG; spy:SPy_0809; -.
DR KEGG; spz:M5005_Spy0624; -.
DR PATRIC; fig|160490.10.peg.692; -.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; FATMSMG; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; P63590; -.
DR Proteomes; UP000000750; 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..228
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138818"
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:2OCZ"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:2OCZ"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2OCZ"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2OCZ"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2OCZ"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:2OCZ"
SQ SEQUENCE 228 AA; 26101 MW; C1E41938E1A2E424 CRC64;
MRIVAPVMPR HFDEAQAIDI SKYEDVNLIE WRADFLPKDE IVAVAPAIFE KFAGKEIIFT
LRTVQEGGNI TLSSQEYVDI IKEINAIYNP DYIDFEYFTH KSVFQEMLDF PNLILSYHNF
EETPENLMEA FSEMTKLAPR VVKIAVMPQS EQDVLDLMNY TRGFKTLNPE QEFATISMGK
LGRLSRFAGD VIGSSWTYVS LDHVSGPGQV TLNDMKRIIE VLEMDISN
