(data stored in ACNUC7421 zone)

SWISSPROT: AROE_AERHH

ID   AROE_AERHH              Reviewed;         273 AA.
AC   A0KEX8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=AHA_0266;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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: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;
CC         EC=1.1.1.25; Evidence={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; CP000462; ABK36524.1; -; Genomic_DNA.
DR   RefSeq; WP_011704274.1; NC_008570.1.
DR   RefSeq; YP_854794.1; NC_008570.1.
DR   SMR; A0KEX8; -.
DR   STRING; 380703.AHA_0266; -.
DR   EnsemblBacteria; ABK36524; ABK36524; AHA_0266.
DR   GeneID; 4490197; -.
DR   KEGG; aha:AHA_0266; -.
DR   PATRIC; fig|380703.7.peg.253; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237876; -.
DR   KO; K00014; -.
DR   OMA; FGNPIKH; -.
DR   BioCyc; AHYD380703:G1G7B-267-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000000756; 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; A0KEX8.
DR   SWISS-2DPAGE; A0KEX8.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN         1    273       Shikimate dehydrogenase (NADP(+)).
FT                                /FTId=PRO_1000021253.
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     213    213       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   BINDING     215    215       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     237    237       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
SQ   SEQUENCE   273 AA;  29192 MW;  7D837CC96DD7FED7 CRC64;
     MDRYLVFGHP VRHSKSPFIH TLFARQTQQE LEYGLAEPAV EEFATSLRAF FAQGGKGCNV
     TVPFKEQAFA LVDRLSPRAR RAGAVNTIKL TDDGVLLGDN TDGAGLVADL KAHGVALAGS
     RILLLGAGGA ARGALAPLLA EQPEALVIAN RTHARAEQLA AEFRDLGAVS AQTYERLGGH
     FDLIINSTSA SLQGELPPLV PALIHADIAI YDMMYGATDT PFIAWAKGQG ARQTVDGLGM
     LVEQAAEAFT VWRGIRPGTK QVLRELKRNL GTL
//

If you have problems or comments...

PBIL Back to PBIL home page