AROE_LISMF
ID AROE_LISMF Reviewed; 291 AA.
AC Q723F9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=LMOf2365_0520;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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}.
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DR EMBL; AE017262; AAT03302.1; -; Genomic_DNA.
DR RefSeq; WP_003725703.1; NC_002973.6.
DR AlphaFoldDB; Q723F9; -.
DR SMR; Q723F9; -.
DR GeneID; 61188351; -.
DR GeneID; 66485488; -.
DR KEGG; lmf:LMOf2365_0520; -.
DR HOGENOM; CLU_044063_4_4_9; -.
DR OMA; SIFARND; -.
DR UniPathway; UPA00053; UER00087.
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:0008652; P:cellular amino acid 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; IPR046346; Aminiacid_DH-like_N_sf.
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 PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR TIGRFAMs; TIGR00507; aroE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW Oxidoreductase.
FT CHAIN 1..291
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136013"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 26..28
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 73
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 98
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 113
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 137..141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 240
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
SQ SEQUENCE 291 AA; 32161 MW; BDBDFF2732CD7D5D CRC64;
MTNKITERIT GHTELIGLIA TPIRHSLSPT MHNEAFAKLG LDYVYLAFEV GDKELKDVVQ
GFRAMNLRGW NVSMPNKTNI HKYLDKLSPA AELVGAVNTV VNDDGVLTGH ITDGTGYMRA
LKEAGHDIIG KKMTICGAGG AATAICIQAA LDGVKEISIF NRKDDFYANA EKTVEKINSK
TDCKAQLFDI EDHEQLRKEI AESVIFTNAT GVGMKPFEGE TLLPSADMLR PELIVSDVVY
KPTKTRLLEI AEEQGCQTLN GLGMMLWQGA KAFEIWTHKE MPVDYIKEIL F
