ID   AROD_BACSU              Reviewed;         255 AA.
AC   P35146;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 151.
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}; Synonyms=aroC;
GN   OrderedLocusNames=BSU23080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA   Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT   "The organization of the Bacillus subtilis 168 chromosome region between
RT   the spoVA and serA genetic loci, based on sequence data.";
RL   Mol. Microbiol. 10:385-395(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; L09228; AAA67501.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14240.1; -; Genomic_DNA.
DR   PIR; S45563; S45563.
DR   RefSeq; NP_390189.1; NC_000964.3.
DR   RefSeq; WP_003230523.1; NC_000964.3.
DR   AlphaFoldDB; P35146; -.
DR   SMR; P35146; -.
DR   FunCoup; P35146; 139.
DR   STRING; 224308.BSU23080; -.
DR   PaxDb; 224308-BSU23080; -.
DR   EnsemblBacteria; CAB14240; CAB14240; BSU_23080.
DR   GeneID; 938963; -.
DR   KEGG; bsu:BSU23080; -.
DR   PATRIC; fig|224308.179.peg.2515; -.
DR   eggNOG; COG0710; Bacteria.
DR   InParanoid; P35146; -.
DR   OrthoDB; 9813659at2; -.
DR   PhylomeDB; P35146; -.
DR   BioCyc; BSUB:BSU23080-MONOMER; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P35146; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00502; DHQase_I; 1.
DR   FunFam; 3.20.20.70:FF:000047; 3-dehydroquinate dehydratase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00214; AroD; 1.
DR   InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR050146; Type-I_3-dehydroquinase.
DR   NCBIfam; TIGR01093; aroD; 1.
DR   PANTHER; PTHR43699; 3-DEHYDROQUINATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43699:SF1; 3-DEHYDROQUINATE DEHYDRATASE; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome; Schiff base.
FT   CHAIN           1..255
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000138793"
FT   ACT_SITE        143
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   ACT_SITE        170
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         46..48
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         82
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         213
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         232
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT   BINDING         236
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   255 AA;  28132 MW;  2B5E9833C6539726 CRC64;
     MNVLTIKGVS IGEGMPKIII PLMGKTEKQI LNEAEAVKLL NPDIVEWRVD VFEKANDREA
     VTKLISKLRK SLEDKLFLFT FRTHKEGGSM EMDESSYLAL LESAIQTKDI DLIDIELFSG
     DANVKALVSL AEENNVYVVM SNHDFEKTPV KDEIISRLRK MQDLGAHIPK MAVMPNDTGD
     LLTLLDATYT MKTIYADRPI ITMSMAATGL ISRLSGEVFG SACTFGAGEE ASAPGQIPVS
     ELRSVLDILH KNTRG
//