(data stored in ACNUC7421 zone)

SWISSPROT: Q2IMD1_ANADE

ID   Q2IMD1_ANADE            Unreviewed;       156 AA.
AC   Q2IMD1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078243};
DE            Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00169};
DE            EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078243};
DE   AltName: Full=Type II DHQase {ECO:0000256|HAMAP-Rule:MF_00169};
GN   Name=aroQ {ECO:0000256|HAMAP-Rule:MF_00169};
GN   OrderedLocusNames=Adeh_0189 {ECO:0000313|EMBL:ABC79966.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79966.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate
CC       intermediate. {ECO:0000256|HAMAP-Rule:MF_00169}.
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:0000256|HAMAP-
CC         Rule:MF_00169, ECO:0000256|SAAS:SAAS01115812};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_00169}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000256|HAMAP-Rule:MF_00169,
CC       ECO:0000256|SAAS:SAAS01078239}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078241}.
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DR   EMBL; CP000251; ABC79966.1; -; Genomic_DNA.
DR   RefSeq; WP_011419249.1; NC_007760.1.
DR   STRING; 290397.Adeh_0189; -.
DR   EnsemblBacteria; ABC79966; ABC79966; Adeh_0189.
DR   KEGG; ade:Adeh_0189; -.
DR   eggNOG; ENOG4108Z38; Bacteria.
DR   eggNOG; COG0757; LUCA.
DR   HOGENOM; HOG000217278; -.
DR   KO; K03786; -.
DR   OMA; CAGIVIN; -.
DR   BioCyc; ADEH290397:G1G5W-195-MONOMER; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
DR   PRODOM; Q2IMD1.
DR   SWISS-2DPAGE; Q2IMD1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00169};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00169};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078240,
KW   ECO:0000313|EMBL:ABC79966.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   REGION       99    100       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00169, ECO:0000256|PIRSR:
FT                                PIRSR001399-2}.
FT   ACT_SITE     21     21       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   ACT_SITE     98     98       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   BINDING      72     72       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      78     78       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      85     85       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING     109    109       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   SITE         16     16       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00169,
FT                                ECO:0000256|PIRSR:PIRSR001399-3}.
SQ   SEQUENCE   156 AA;  17051 MW;  C68355AE5E918CB3 CRC64;
     MILIVNGPNL NLLGEREPDV YGRSTLADVE QLVRDACAAW DVEVKAFQSN HEGAILDFLQ
     EHRKKARGVI LNAGALTHTS YALHDCLKAM PAPAVEVHIS NIHQREAFRH VSVIAPACRG
     QIVGLGIRGY LLAAEWLCAE IGAQPRGSED RKKPSP
//

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