AROQ_BACSU
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 03-AUG-2022, entry version 141.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000036.1.
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 PDBsum; 1GQO; -.
DR AlphaFoldDB; P54517; -.
DR SMR; P54517; -.
DR STRING; 224308.BSU24470; -.
DR PaxDb; P54517; -.
DR PRIDE; P54517; -.
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 OMA; AYTHYSY; -.
DR PhylomeDB; P54517; -.
DR BioCyc; BSUB:BSU24470-MON; -.
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: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 GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
DR CDD; cd00466; DHQase_II; 1.
DR Gene3D; 3.40.50.9100; -; 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 PANTHER; PTHR21272; PTHR21272; 1.
DR Pfam; PF01220; DHquinase_II; 1.
DR PIRSF; PIRSF001399; DHquinase_II; 1.
DR SUPFAM; SSF52304; SSF52304; 1.
DR TIGRFAMs; TIGR01088; aroQ; 1.
DR PROSITE; PS01029; DEHYDROQUINASE_II; 1.
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
