(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJY6_PSEAB

ID   A0A0H2ZJY6_PSEAB        Unreviewed;       274 AA.
AC   A0A0H2ZJY6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00228653};
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:ABJ14981.1};
GN   OrderedLocusNames=PA14_00290 {ECO:0000313|EMBL:ABJ14981.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ14981.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ14981.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ14981.1,
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       ECO:0000256|SAAS:SAAS00642229}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000256|HAMAP-Rule:MF_00222,
CC       ECO:0000256|SAAS:SAAS00048714}.
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       ECO:0000256|SAAS:SAAS00179298}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00634670}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000438; ABJ14981.1; -; Genomic_DNA.
DR   RefSeq; WP_003097314.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJY6; -.
DR   EnsemblBacteria; ABJ14981; ABJ14981; PA14_00290.
DR   KEGG; pau:PA14_00290; -.
DR   KO; K00014; -.
DR   OMA; PLIHNAC; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; 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; A0A0H2ZJY6.
DR   SWISS-2DPAGE; A0A0H2ZJY6.
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, ECO:0000256|SAAS:SAAS00058194};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW   ECO:0000256|SAAS:SAAS00808825}.
FT   DOMAIN        6     87       Shikimate_dh_N. {ECO:0000259|Pfam:
FT                                PF08501}.
FT   DOMAIN      116    165       Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
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      76     76       NADP. {ECO:0000256|HAMAP-Rule: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   274 AA;  29490 MW;  670456834297D792 CRC64;
     MDRYCVFGNP IGHSKSPLIH RLFAEQTGEA LVYDAQLAPL DDFPGFARRF FEQGKGANVT
     VPFKEEAYRL VDELSERATR AGAVNTLIRL ADGRLRGDNT DGAGLLRDLT ANAGVELRGK
     RVLLLGAGGA VRGVLEPFLG ECPAELLIAN RTARKAVDLA ERFADLGAVR GCGFAEVEGP
     FDLVVNGTSA SLAGDVPPLA QSVIEPGRTV CYDMMYAKEP TAFNRWAAER GAARTLDGLG
     MLVEQAAEAF FLWRGVRPAS APVLETLRRQ LATV
//

If you have problems or comments...

PBIL Back to PBIL home page