(data stored in SCRATCH zone)

SWISSPROT: Q3KKD9_PSEPF

ID   Q3KKD9_PSEPF            Unreviewed;       273 AA.
AC   Q3KKD9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 124.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00321572};
DE            Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00321538};
GN   Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN   OrderedLocusNames=Pfl01_0023 {ECO:0000313|EMBL:ABA71767.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71767.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71767.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71767.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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       ECO:0000256|SAAS:SAAS00554845}.
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;
CC         EC=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_00222,
CC         ECO:0000256|SAAS:SAAS01121538};
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:SAAS00315122}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS01143539}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00541574}.
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; CP000094; ABA71767.1; -; Genomic_DNA.
DR   RefSeq; WP_011331751.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0023; -.
DR   PRIDE; Q3KKD9; -.
DR   EnsemblBacteria; ABA71767; ABA71767; Pfl01_0023.
DR   KEGG; pfo:Pfl01_0023; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237876; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   BioCyc; PFLU205922:G1G4S-23-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000002704; 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; Q3KKD9.
DR   SWISS-2DPAGE; Q3KKD9.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00315106};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00315132};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00320209};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00320235, ECO:0000313|EMBL:ABA71767.1}.
FT   DOMAIN        6     87       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN      116    191       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
FT   DOMAIN      238    268       SDH_C. {ECO:0000259|Pfam:PF18317}.
FT   NP_BIND     126    130       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   NP_BIND     150    155       NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   REGION       14     16       Shikimate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     64     64       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      60     60       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING      85     85       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     101    101       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     214    214       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     216    216       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
FT   BINDING     238    238       NADP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00222}.
FT   BINDING     245    245       Shikimate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00222}.
SQ   SEQUENCE   273 AA;  29006 MW;  7E5609769DD5DC7F CRC64;
     MDRYVVFGNP IGHSKSPMIH KLFAEQTGQS LDYSTLLAPL DDFSGCATAF FQEGRGANVT
     VPFKEDAYRL ANSLTARAER AGAVNTLSKL ADGSLLGDNT DGAGLVRDLT VNGGFSLTGK
     RILLLGAGGA VRGALEPLLA EKPASVIIAN RTVDKAELLA ELFCDLGPVS ASGYDWLREP
     VDVIINATSA SLTGDVPPIA ESLIEPGKTL CYDMMYGKEP TAFCRWASEH GAGVVMDGLG
     MLAEQAAEAF FLWRGVRPDT APVLAELRRQ LTL
//

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