(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJJ3_PSEAB

ID   A0A0H2ZJJ3_PSEAB        Unreviewed;       284 AA.
AC   A0A0H2ZJJ3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 16.
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:ABJ15193.1};
GN   OrderedLocusNames=PA14_03020 {ECO:0000313|EMBL:ABJ15193.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15193.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15193.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15193.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of the chorismate, which
CC       leads to the biosynthesis of aromatic amino acids. Catalyzes the
CC       reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to
CC       yield shikimate (SA). {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00179153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00634670}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR   EMBL; CP000438; ABJ15193.1; -; Genomic_DNA.
DR   RefSeq; WP_003137120.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJJ3; -.
DR   EnsemblBacteria; ABJ15193; ABJ15193; PA14_03020.
DR   KEGG; pau:PA14_03020; -.
DR   KO; K00014; -.
DR   OMA; HEHEGDA; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJJ3.
DR   SWISS-2DPAGE; A0A0H2ZJJ3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00179157};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00179155};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00808825}.
FT   DOMAIN       11     98       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   NP_BIND     135    139       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   REGION       19     21       Shikimate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     75     75       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      71     71       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      96     96       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     111    111       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     227    227       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     229    229       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     250    250       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     257    257       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
SQ   SEQUENCE   284 AA;  29733 MW;  6CC3CAE85790722E CRC64;
     MSAPRSVLAG LIGAGIQASR TPALHEREGD AQGIRYLYRL IDLDPLGKSA DDLEFLLAAA
     SDLGFTGLNV TFPCKQAIIP LLDELSAEAR GIGAVNTVVL RDGRRIGHNT DCLGFAEGFR
     RGLADAPRQR VVQMGAGGAG AAVAHALLAE GVERLVLFDV DPARAQALAD NLNQHFGAPR
     ALAGSDLAGA LGDAQGLVNT TPVGMAKLPG MPVPAELLRA DLWVAEVIYF PLETELLRQA
     RALGCRTLDG GTMAVFQAVK AFELFSGVEA DAARMQAHFA SLGD
//

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