(data stored in SCRATCH zone)

SWISSPROT: AROE_BACSU

ID   AROE_BACSU              Reviewed;         280 AA.
AC   P54374;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 140.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222};
DE            Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222};
GN   Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; Synonyms=aroD;
GN   OrderedLocusNames=BSU25660;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 139.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00222}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00222}.
DR   EMBL; D84432; BAA12445.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14508.2; -; Genomic_DNA.
DR   PIR; A69590; A69590.
DR   RefSeq; NP_390444.2; NC_000964.3.
DR   RefSeq; WP_003229967.1; NZ_JNCM01000036.1.
DR   SMR; P54374; -.
DR   STRING; 224308.BSU25660; -.
DR   PaxDb; P54374; -.
DR   PRIDE; P54374; -.
DR   EnsemblBacteria; CAB14508; CAB14508; BSU25660.
DR   GeneID; 937820; -.
DR   KEGG; bsu:BSU25660; -.
DR   PATRIC; fig|224308.179.peg.2789; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   InParanoid; P54374; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   PhylomeDB; P54374; -.
DR   BioCyc; BSUB:BSU25660-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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; P54374.
DR   SWISS-2DPAGE; P54374.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..280
FT                   /note="Shikimate dehydrogenase (NADP(+))"
FT                   /id="PRO_0000135992"
FT   NP_BIND         127..131
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   NP_BIND         151..156
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   REGION          15..17
FT                   /note="Shikimate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         62
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         78
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         87
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         102
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         219
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         221
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         242
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   CONFLICT        139
FT                   /note="I -> F (in Ref. 1; BAA12445)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  30608 MW;  8530CE97F50D7DE3 CRC64;
     MKKLYGVIGN PIGHSMSPDI HNASLKDLGL DGHYHAFKVE ENDLEDAVKG IRALGVQGIN
     VTVPHKVSIM DYLDHIDESA KVLGAVNTVR REGDKLVGYN TDGEGFVKSL MKVLDKPISE
     LSFLMIGAGG AARAIFTTIV RNTPKKFDIC NRTLEKAKRL TEATPSFHNK EVLSIKEAEE
     RLEQYDVIIH TTSVGMYPNV DDVPLSLQRA ASSAVVCDIV YNPIQTALLK EASQKGLKTL
     DGVGMFVEQA ALSFQLWTGQ EPNIEKMRSI VIGKLGGTEC
//

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