AROD_GEOKA
ID AROD_GEOKA Reviewed; 257 AA.
AC Q5KY94;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=GK2057;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of 3-dehydroquinate dehydratase from Geobacillus
RT kaustophilus HTA426.";
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 ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; BA000043; BAD76342.1; -; Genomic_DNA.
DR RefSeq; WP_011231543.1; NC_006510.1.
DR PDB; 2YR1; X-ray; 2.00 A; A/B=1-257.
DR PDBsum; 2YR1; -.
DR AlphaFoldDB; Q5KY94; -.
DR SMR; Q5KY94; -.
DR STRING; 235909.GK2057; -.
DR PRIDE; Q5KY94; -.
DR EnsemblBacteria; BAD76342; BAD76342; GK2057.
DR KEGG; gka:GK2057; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; FATMSMG; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q5KY94; -.
DR Proteomes; UP000001172; 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..257
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000325524"
FT ACT_SITE 147
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 174
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 50..52
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 86
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 216
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 235
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 239
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2YR1"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2YR1"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2YR1"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2YR1"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:2YR1"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:2YR1"
SQ SEQUENCE 257 AA; 28564 MW; D988D5A96B791D6A CRC64;
MNISPKAIKV RNIWIGGTEP CICAPVVGED DRKVLREAEE VCRKQPDLLE WRADFFRAID
DQERVLATAN GLRNIAGEIP ILFTIRSERE GGQPIPLNEA EVRRLIEAIC RSGAIDLVDY
ELAYGERIAD VRRMTEECSV WLVVSRHYFD GTPRKETLLA DMRQAERYGA DIAKVAVMPK
SPEDVLVLLQ ATEEARRELA IPLITMAMGG LGAITRLAGW LFGSAVTFAV GNQSSAPGQI
PIDDVRTVLS ILQTYSR
