(data stored in SCRATCH zone)

SWISSPROT: D1YUW7_METPS

ID   D1YUW7_METPS            Unreviewed;       268 AA.
AC   D1YUW7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222};
DE            Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222};
GN   Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222,
GN   ECO:0000313|EMBL:BAI60239.1};
GN   OrderedLocusNames=MCP_0167 {ECO:0000313|EMBL:BAI60239.1};
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:BAI60239.1, 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 biosynthesis of the chorismate, which leads
CC       to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC       NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC       (SA). {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00222};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR   EMBL; AP011532; BAI60239.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0167; -.
DR   EnsemblBacteria; BAI60239; BAI60239; MCP_0167.
DR   KEGG; mpd:MCP_0167; -.
DR   PATRIC; fig|304371.9.peg.173; -.
DR   eggNOG; arCOG01033; Archaea.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) 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   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR011342; Shikimate_DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00507; aroE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YUW7.
DR   SWISS-2DPAGE; D1YUW7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   DOMAIN          7..88
FT                   /note="Shikimate_dh_N"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          113..188
FT                   /note="Shikimate_DH"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          235..265
FT                   /note="SDH_C"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   NP_BIND         123..127
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   NP_BIND         146..151
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   REGION          15..17
FT                   /note="Shikimate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         62
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         86
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         99
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         212
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         214
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         235
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         242
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   268 AA;  28279 MW;  C7847C6E594E31F9 CRC64;
     MITLYGVIGD PVAHSLSPAM HNAAFKALGM DCYYAPFHVK GRYLYEAVNG ARALGFGGLN
     VTVPHKEAVI RFVEADQAVR DIGAANTIDF HTNKAYNTDA PGAIASLRDS GVRVKGRNVL
     VMGAGGAARA VTYGLLKEGA TVTIANRTAP KAADLAAYMR EYGDVFGTGM DSLAEKVAIS
     DVIVNTTTVG MGEDRTLVTA AMLGPEQAVF DLVYKPVETQ LLKEAKAAGA KAIDGITMLA
     RQGALSFEIW TGVKPPLDVM ERSARDAV
//

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