AROE_LISMO
ID AROE_LISMO Reviewed; 291 AA.
AC Q8Y9N5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=lmo0490;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP,
RP AND SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RT "Crystal structure of shikimate 5-dehydrogenase Listeria monocytogenes in
RT complex with shikimate and NAD.";
RL Submitted (SEP-2011) to the PDB data bank.
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 or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00222,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AL591975; CAC98569.1; -; Genomic_DNA.
DR PIR; AC1136; AC1136.
DR RefSeq; NP_464018.1; NC_003210.1.
DR RefSeq; WP_003725703.1; NZ_CP023861.1.
DR PDB; 3TNL; X-ray; 1.45 A; A/B/C/D=1-291.
DR PDB; 3TOZ; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-291.
DR PDBsum; 3TNL; -.
DR PDBsum; 3TOZ; -.
DR AlphaFoldDB; Q8Y9N5; -.
DR SMR; Q8Y9N5; -.
DR STRING; 169963.lmo0490; -.
DR PaxDb; Q8Y9N5; -.
DR EnsemblBacteria; CAC98569; CAC98569; CAC98569.
DR GeneID; 61188351; -.
DR GeneID; 66485488; -.
DR GeneID; 985396; -.
DR KEGG; lmo:lmo0490; -.
DR PATRIC; fig|169963.11.peg.509; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_4_9; -.
DR OMA; SIFARND; -.
DR PhylomeDB; Q8Y9N5; -.
DR BioCyc; LMON169963:LMO0490-MON; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..291
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136014"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
FT BINDING 26..28
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2"
FT BINDING 73
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
FT BINDING 98
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
FT BINDING 113
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
FT BINDING 137..141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
FT BINDING 161..164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2"
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,
FT ECO:0000305|Ref.2"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3TNL"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3TNL"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:3TNL"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3TNL"
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
