(data stored in ACNUC7421 zone)

SWISSPROT: B8IUC5_METNO

ID   B8IUC5_METNO            Unreviewed;       141 AA.
AC   B8IUC5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
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=Mnod_0123 {ECO:0000313|EMBL:ACL55170.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55170.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55170.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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; CP001349; ACL55170.1; -; Genomic_DNA.
DR   RefSeq; WP_015926883.1; NC_011894.1.
DR   STRING; 460265.Mnod_0123; -.
DR   EnsemblBacteria; ACL55170; ACL55170; Mnod_0123.
DR   KEGG; mno:Mnod_0123; -.
DR   eggNOG; ENOG4108Z38; Bacteria.
DR   eggNOG; COG0757; LUCA.
DR   HOGENOM; HOG000217278; -.
DR   KO; K03786; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000008207; 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; B8IUC5.
DR   SWISS-2DPAGE; B8IUC5.
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:UP000008207};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00169, ECO:0000256|SAAS:SAAS01078240,
KW   ECO:0000313|EMBL:ACL55170.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   REGION      100    101       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00169, ECO:0000256|PIRSR:
FT                                PIRSR001399-2}.
FT   ACT_SITE     23     23       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   ACT_SITE     99     99       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                1}.
FT   BINDING      73     73       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      79     79       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING      86     86       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   BINDING     110    110       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00169, ECO:0000256|PIRSR:PIRSR001399-
FT                                2}.
FT   SITE         18     18       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00169,
FT                                ECO:0000256|PIRSR:PIRSR001399-3}.
SQ   SEQUENCE   141 AA;  15007 MW;  C8AAC989885C25FF CRC64;
     MRDIHVLNGP NLNLLGIREP GIYGALTLAD IERRLRDRAG ARAALTFRQS NHEGDLVTWV
     HEAGAAGAGV ILNAGAYTHT SVALRDAISG AKAEVIEVHL SNVHARESFR HHSYIAPVAR
     GVIAGFGPLS YDLALEALLA A
//

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