AROE_GEOKA
ID AROE_GEOKA Reviewed; 276 AA.
AC Q5KWX7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=GK2524;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT.
RA Bagautdinov B., Kunishima N.;
RT "Crystal structure of shikimate 5-dehydrogenase (AroE) from Geobacillus
RT kaustophilus.";
RL Submitted (FEB-2007) 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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000043; BAD76809.1; -; Genomic_DNA.
DR RefSeq; WP_011232003.1; NC_006510.1.
DR PDB; 2EGG; X-ray; 2.25 A; A/B=1-276.
DR PDBsum; 2EGG; -.
DR AlphaFoldDB; Q5KWX7; -.
DR SMR; Q5KWX7; -.
DR STRING; 235909.GK2524; -.
DR EnsemblBacteria; BAD76809; BAD76809; GK2524.
DR KEGG; gka:GK2524; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_1_9; -.
DR OMA; FGNPIKH; -.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; Q5KWX7; -.
DR Proteomes; UP000001172; Chromosome.
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 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..276
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000431402"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 15..17
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 62
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 87
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 102
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 151..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 220
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2EGG"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2EGG"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:2EGG"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:2EGG"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:2EGG"
SQ SEQUENCE 276 AA; 30427 MW; 1054EC5195AD3B06 CRC64;
MEKVYGLIGF PVEHSLSPLM HNDAFARLGI PARYHLFSVE PGQVGAAIAG VRALGIAGVN
VTIPHKLAVI PFLDEVDEHA RRIGAVNTII NNDGRLVGYN TDGLGYVQAL EEEMNITLDG
KRILVIGAGG GARGIYFSLL STAAERIDMA NRTVEKAERL VREGDERRSA YFSLAEAETR
LAEYDIIINT TSVGMHPRVE VQPLSLERLR PGVIVSDIIY NPLETKWLKE AKARGARVQN
GVGMLVYQGA LAFEKWTGQW PDVNRMKQLV IEALRR
