AROE_THET8
ID AROE_THET8 Reviewed; 263 AA.
AC Q5SJF8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=TTHA1050;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP,
RP REACTION MECHANISM, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=17825835; DOI=10.1016/j.jmb.2007.08.017;
RA Bagautdinov B., Kunishima N.;
RT "Crystal structures of shikimate dehydrogenase AroE from Thermus
RT thermophilus HB8 and its cofactor and substrate complexes: insights into
RT the enzymatic mechanism.";
RL J. Mol. Biol. 373:424-438(2007).
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 ECO:0000269|PubMed:17825835}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AP008226; BAD70873.1; -; Genomic_DNA.
DR RefSeq; WP_011228401.1; NC_006461.1.
DR RefSeq; YP_144316.1; NC_006461.1.
DR PDB; 1WXD; X-ray; 2.10 A; A/B=1-263.
DR PDB; 2CY0; X-ray; 1.90 A; A/B=1-263.
DR PDB; 2D5C; X-ray; 1.65 A; A/B=1-263.
DR PDB; 2EV9; X-ray; 1.90 A; A/B=1-263.
DR PDBsum; 1WXD; -.
DR PDBsum; 2CY0; -.
DR PDBsum; 2D5C; -.
DR PDBsum; 2EV9; -.
DR AlphaFoldDB; Q5SJF8; -.
DR SMR; Q5SJF8; -.
DR STRING; 300852.55772432; -.
DR EnsemblBacteria; BAD70873; BAD70873; BAD70873.
DR GeneID; 3169915; -.
DR KEGG; ttj:TTHA1050; -.
DR PATRIC; fig|300852.9.peg.1030; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_0_1_0; -.
DR OMA; FGNPIKH; -.
DR PhylomeDB; Q5SJF8; -.
DR BRENDA; 1.1.1.25; 2305.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; Q5SJF8; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
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 InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 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..263
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_1000078133"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 14..16
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 60
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 85
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 100
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 123..127
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 146..151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 207
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT BINDING 235
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17825835"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2D5C"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2EV9"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2D5C"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:2D5C"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 229..244
FT /evidence="ECO:0007829|PDB:2D5C"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:2D5C"
SQ SEQUENCE 263 AA; 28284 MW; BF53F1D49A1A82A4 CRC64;
MLRFAVLGHP VAHSLSPAMH AFALESLGLE GSYEAWDTPL EALPGRLKEV RRAFRGVNLT
LPLKEAALAH LDWVSPEAQR IGAVNTVLQV EGRLFGFNTD APGFLEALKA GGIPLKGPAL
VLGAGGAGRA VAFALREAGL EVWVWNRTPQ RALALAEEFG LRAVPLEKAR EARLLVNATR
VGLEDPSASP LPAELFPEEG AAVDLVYRPL WTRFLREAKA KGLKVQTGLP MLAWQGALAF
RLWTGLLPDP SGMEEAARRA LGV
