(data stored in ACNUC10043 zone)

SWISSPROT: D1YVQ2_METPS

ID   D1YVQ2_METPS            Unreviewed;       218 AA.
AC   D1YVQ2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 48.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00214};
DE            Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214};
DE            EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00214};
DE   AltName: Full=Type I DHQase {ECO:0000256|HAMAP-Rule:MF_00214};
DE   AltName: Full=Type I dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214};
DE            Short=DHQ1 {ECO:0000256|HAMAP-Rule:MF_00214};
GN   Name=aroD {ECO:0000256|HAMAP-Rule:MF_00214,
GN   ECO:0000313|EMBL:BAI60524.1};
GN   OrderedLocusNames=MCP_0452 {ECO:0000313|EMBL:BAI60524.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60524.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00214}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00214}.
CC   -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00214}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00214}.
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DR   EMBL; AP011532; BAI60524.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0452; -.
DR   EnsemblBacteria; BAI60524; BAI60524; MCP_0452.
DR   KEGG; mpd:MCP_0452; -.
DR   eggNOG; arCOG02097; Archaea.
DR   eggNOG; COG0710; LUCA.
DR   HOGENOM; HOG000105515; -.
DR   KO; K03785; -.
DR   OMA; ATMAMGE; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001882; 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; cd00502; DHQase_I; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00214; AroD; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001381; DHquinase_I.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   TIGRFAMs; TIGR01093; aroD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVQ2.
DR   SWISS-2DPAGE; D1YVQ2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00214};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00214};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00214};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00214}.
FT   REGION          29..31
FT                   /note="3-dehydroquinate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   ACT_SITE        115
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   ACT_SITE        141
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         58
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         179
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         202
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   218 AA;  24125 MW;  C0CD098A4A7B469B CRC64;
     MEFPPKVVAT VTSLDEAKEA ISLGADIIEI RVDLLDEGPQ PLVERIYKLN KPLIITVRPT
     WEGGAFKGSD RDRVKIFKAL VPVADYIDVE LRAPNVEELV ALTGGTDALS IISYHDFEKM
     PSKKEMMDIV VQCHEKGDIA KLAVTPASLR DVLRLFEVTL KSKRPLCTIA MGEMGAHSRI
     VGPVYGSQFT YGYVRKPVAP GQIRVDKILE GLRLLGLR
//

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