AROE_THEMA
ID AROE_THEMA Reviewed; 253 AA.
AC Q9WYI1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=TM_0346;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35432.1; -; Genomic_DNA.
DR PIR; H72388; H72388.
DR RefSeq; NP_228157.1; NC_000853.1.
DR RefSeq; WP_004083132.1; NZ_CP011107.1.
DR PDB; 3U62; X-ray; 1.45 A; A=1-253.
DR PDBsum; 3U62; -.
DR AlphaFoldDB; Q9WYI1; -.
DR SMR; Q9WYI1; -.
DR STRING; 243274.THEMA_02985; -.
DR EnsemblBacteria; AAD35432; AAD35432; TM_0346.
DR KEGG; tma:TM0346; -.
DR eggNOG; COG0169; Bacteria.
DR InParanoid; Q9WYI1; -.
DR OMA; SIFARND; -.
DR OrthoDB; 1054867at2; -.
DR BRENDA; 1.1.1.25; 6331.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
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; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 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..253
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136046"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 13..15
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 59
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 83
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 94
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 115..119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 139..144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 201
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:3U62"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3U62"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:3U62"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:3U62"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3U62"
SQ SEQUENCE 253 AA; 28889 MW; 64778D10CB07CE0E CRC64;
MKFCIIGYPV RHSISPRLYN EYFKRAGMNH SYGMEEIPPE SFDTEIRRIL EEYDGFNATI
PHKERVMRYV EPSEDAQRIK AVNCVFRGKG YNTDWVGVVK SLEGVEVKEP VVVVGAGGAA
RAVIYALLQM GVKDIWVVNR TIERAKALDF PVKIFSLDQL DEVVKKAKSL FNTTSVGMKG
EELPVSDDSL KNLSLVYDVI YFDTPLVVKA RKLGVKHIIK GNLMFYYQAM ENLKIWGIYD
EEVFKEVFGE VLK
