(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9C1_METMS

ID   D5E9C1_METMS            Unreviewed;       231 AA.
AC   D5E9C1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 49.
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   OrderedLocusNames=Mmah_0239 {ECO:0000313|EMBL:ADE35772.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35772.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35772.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001994; ADE35772.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADE35772; ADE35772; Mmah_0239.
DR   KEGG; mmh:Mmah_0239; -.
DR   eggNOG; arCOG02097; Archaea.
DR   eggNOG; COG0710; LUCA.
DR   HOGENOM; HOG000105515; -.
DR   KO; K03785; -.
DR   OMA; ATMAMGE; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000001059; 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; D5E9C1.
DR   SWISS-2DPAGE; D5E9C1.
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, ECO:0000313|EMBL:ADE35772.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00214}.
FT   REGION          36..38
FT                   /note="3-dehydroquinate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   ACT_SITE        129
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   ACT_SITE        156
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         15
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         70
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         194
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT   BINDING         217
FT                   /note="3-dehydroquinate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
SQ   SEQUENCE   231 AA;  25543 MW;  CBCD42E2E599ED1A CRC64;
     MTGFVAGKDV KIVASIDSDP LLQARIAKVL GADILEIRLD FLEIKEAVQA KKLFDLLDQQ
     GGVPRIATNR VHTEGGSWQG TEEQRITLLE DLIPYVDMID IERKCTDCLR NRLVEEAKSQ
     GTKVIMSSHF FETTPPEKDM VAILNECTDK GADIAKLAVM PQKPEDILEL FHAALQARGE
     VCVIAMGELG RHSRVVACRY GSLLTYGCVE KPVAPGQIRI DQLKRALETT V
//

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