ID   AROQ_BACSU              Reviewed;         148 AA.
AC   P54517;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase;
GN   Name=yqhS; OrderedLocusNames=BSU24470;
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 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-144, AND SUBUNIT.
RA   Robinson D.A., Roszak A.W., Coggins J.R., Lapthorn A.J.;
RT   "Crystal structure of the type II dehydroquinase from Bacillus subtilis.";
RL   Submitted (NOV-2001) to the PDB data bank.
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;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Phe-23 is present instead of the conserved Tyr which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; D84432; BAA12556.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14378.1; -; Genomic_DNA.
DR   PIR; B69960; B69960.
DR   RefSeq; NP_390327.1; NC_000964.3.
DR   RefSeq; WP_003230223.1; NC_000964.3.
DR   PDB; 1GQO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/X/Y=2-144.
DR   AlphaFoldDB; P54517; -.
DR   SMR; P54517; -.
DR   FunCoup; P54517; 244.
DR   STRING; 224308.BSU24470; -.
DR   PaxDb; 224308-BSU24470; -.
DR   EnsemblBacteria; CAB14378; CAB14378; BSU_24470.
DR   GeneID; 938557; -.
DR   KEGG; bsu:BSU24470; -.
DR   PATRIC; fig|224308.179.peg.2665; -.
DR   eggNOG; COG0757; Bacteria.
DR   InParanoid; P54517; -.
DR   OrthoDB; 9790793at2; -.
DR   PhylomeDB; P54517; -.
DR   BioCyc; BSUB:BSU24470-MONOMER; -.
DR   BRENDA; 4.2.1.10; 658.
DR   UniPathway; UPA00053; UER00086.
DR   EvolutionaryTrace; P54517; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; Dehydroquinase, class II; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   NCBIfam; TIGR01088; aroQ; 1.
DR   NCBIfam; NF003805; PRK05395.1-2; 1.
DR   NCBIfam; NF003806; PRK05395.1-3; 1.
DR   NCBIfam; NF003807; PRK05395.1-4; 1.
DR   PANTHER; PTHR21272; CATABOLIC 3-DEHYDROQUINASE; 1.
DR   PANTHER; PTHR21272:SF3; CATABOLIC 3-DEHYDROQUINASE; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; Type II 3-dehydroquinate dehydratase; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
DR   PDBsum; 1GQO; -.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Lyase; Reference proteome.
FT   CHAIN           1..148
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_0000159872"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           28..42
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           54..64
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:1GQO"
FT   HELIX           130..140
FT                   /evidence="ECO:0007829|PDB:1GQO"
SQ   SEQUENCE   148 AA;  16431 MW;  71B253931B43EFE7 CRC64;
     MPHFLILNGP NVNRLGSREP EVFGRQTLTD IETDLFQFAE ALHIQLTFFQ SNHEGDLIDA
     IHEAEEQYSG IVLNPGALSH YSYAIRDAVS SISLPVVEVH LSNLYAREEF RHQSVIAPVA
     KGQIVGLGAE GYKLAVRYLL SQQGGESR
//