(data stored in ACNUC7421 zone)

SWISSPROT: AROE_ANADF

ID   AROE_ANADF              Reviewed;         279 AA.
AC   A7H6S7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=Anae109_0205;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC       to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC       NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC       (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; EC=1.1.1.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00222};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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; CP000769; ABS24423.1; -; Genomic_DNA.
DR   RefSeq; WP_011984529.1; NC_009675.1.
DR   SMR; A7H6S7; -.
DR   STRING; 404589.Anae109_0205; -.
DR   PRIDE; A7H6S7; -.
DR   EnsemblBacteria; ABS24423; ABS24423; Anae109_0205.
DR   KEGG; afw:Anae109_0205; -.
DR   eggNOG; ENOG4105E2X; Bacteria.
DR   eggNOG; COG0169; LUCA.
DR   HOGENOM; HOG000237875; -.
DR   KO; K00014; -.
DR   OMA; FKESCMP; -.
DR   OrthoDB; 1054867at2; -.
DR   BioCyc; ASP404589:G1G9J-209-MONOMER; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000006382; 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; A7H6S7.
DR   SWISS-2DPAGE; A7H6S7.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..279
FT                   /note="Shikimate dehydrogenase (NADP(+))"
FT                   /id="PRO_0000325099"
FT   NP_BIND         129..133
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   REGION          19..21
FT                   /note="Shikimate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         66
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         91
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         106
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         222
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         224
FT                   /note="Shikimate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         243
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   279 AA;  28596 MW;  1339CB641E0FB808 CRC64;
     MITGRTALYG VLGNPVRHSR SPQMQAAAFE HLGLDATYVA LPVEPERLPA AVAGAHALGF
     QGLNVTVPHK RAVVALCEAV DPVAREVGAV NTLRRTERGW EGFNTDAAAC LMLLREEGLR
     PGAPALLAGA GGAARAAAWA LVRAGAVLRI AARRQDAAER LAAELGPLAG PGTPAPVAVP
     WGALEAEADA AEAVVNGTTV GLHPEDAPLP LRVRAGQLVA DFVYGDTPLA RAARDAGARL
     VSGERILVRQ GALSFALWTG RAAPEALMAA AIAAPGRAT
//

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