(data stored in ACNUC7421 zone)

SWISSPROT: AROE_PSEHT

ID   AROE_PSEHT              Reviewed;         274 AA.
AC   Q3IDI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 93.
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};
GN   OrderedLocusNames=PSHAa0031;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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:0000255|HAMAP-Rule:MF_00222}.
CC   -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
CC       NADPH. {ECO:0000255|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: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; CR954246; CAI85145.1; -; Genomic_DNA.
DR   RefSeq; WP_011326763.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDI6; -.
DR   SMR; Q3IDI6; -.
DR   STRING; 326442.PSHAa0031; -.
DR   EnsemblBacteria; CAI85145; CAI85145; PSHAa0031.
DR   KEGG; pha:PSHAa0031; -.
DR   PATRIC; fig|326442.8.peg.33; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237876; -.
DR   KO; K00014; -.
DR   OMA; PLIHNAC; -.
DR   OrthoDB; POG091H02DY; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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; Q3IDI6.
DR   SWISS-2DPAGE; Q3IDI6.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN         1    274       Shikimate dehydrogenase (NADP(+)).
FT                                /FTId=PRO_1000021317.
FT   NP_BIND     126    130       NADP. {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   NP_BIND     150    155       NADP. {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   REGION       14     16       Shikimate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     65     65       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING      61     61       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING      86     86       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     102    102       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     214    214       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   BINDING     216    216       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     239    239       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
SQ   SEQUENCE   274 AA;  29680 MW;  FC9EF677F032AD37 CRC64;
     MDKYAVFGNP IKHSKSPAIH KQFAISLGEQ IDYRAILAPI DNFEKTVSNF FAQGGKGANV
     TMPFKEQAFA MADELTPLAK IVGAVNTLKK QADGTLLGDN TDGIGFVSDL LANNVSITGK
     RILIIGAGGA ARGVVLPLLD HQPQEVVIVN RTAEKAQNLA KLFAQHGNVS GYGFNNLPEN
     DYALIINSTS SSMNDELPAL DQKHITNCEV AYDMFYSLQN TIFMNWVAQY NSKTKLLDGS
     GMLVGQAAQA YYVWRNKMPA ILPVVNALKQ GALT
//

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