(data stored in ACNUC7421 zone)

SWISSPROT: AROE_ANADE

ID   AROE_ANADE              Reviewed;         278 AA.
AC   Q2IMC7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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=Adeh_0185;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC79962.1; -; Genomic_DNA.
DR   RefSeq; WP_011419245.1; NC_007760.1.
DR   SMR; Q2IMC7; -.
DR   STRING; 290397.Adeh_0185; -.
DR   PRIDE; Q2IMC7; -.
DR   EnsemblBacteria; ABC79962; ABC79962; Adeh_0185.
DR   KEGG; ade:Adeh_0185; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   KO; K00014; -.
DR   OMA; IPHKERA; -.
DR   BioCyc; ADEH290397:G1G5W-191-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000001935; Chromosome.
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   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMC7.
DR   SWISS-2DPAGE; Q2IMC7.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN         1    278       Shikimate dehydrogenase (NADP(+)).
FT                                /FTId=PRO_0000325098.
FT   NP_BIND     129    133       NADP. {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   REGION       19     21       Shikimate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   ACT_SITE     70     70       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING      66     66       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING      91     91       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     106    106       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     221    221       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
FT   BINDING     223    223       Shikimate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00222}.
FT   BINDING     242    242       NADP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00222}.
SQ   SEQUENCE   278 AA;  28771 MW;  296E78778629592F CRC64;
     MITGRTALYG VVGHPVAHSR SPEMQNAAFA KLGVDAAYVA LPVAPERIDE ALRGAHALGF
     QGLNVTVPHK PRAASLCHAL DPVATAVGAA NTLRRTRDGW EGFNTDAPAC RTLLEAAGVA
     RGARALLVGA GGAARAAAWA LLQLGTELRV AARREEAAAE LCRDLAAAVP GADAATADFE
     DLEAEADAAA VVVNGTSVEL PGHEGRLPPL RFRADQVVLD FVYGDTELAR AARAGGARLV
     TGEQVLVRQG ALAFTIWTGL PAPEADMARA LEAREGAR
//

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