AROE_AQUAE
ID AROE_AQUAE Reviewed; 269 AA.
AC O67049;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:17649975};
DE Short=SD {ECO:0000303|PubMed:17649975};
DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:17649975};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:17649975};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:17649975};
GN OrderedLocusNames=aq_901;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP REACTION MECHANISM, AND SUBUNIT.
RX PubMed=17649975; DOI=10.1021/bi602601e;
RA Gan J., Wu Y., Prabakaran P., Gu Y., Li Y., Andrykovitch M., Liu H.,
RA Gong Y., Yan H., Ji X.;
RT "Structural and biochemical analyses of shikimate dehydrogenase AroE from
RT Aquifex aeolicus: implications for the catalytic mechanism.";
RL Biochemistry 46:9513-9522(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, ECO:0000269|PubMed:17649975}.
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 ECO:0000269|PubMed:17649975};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42.4 uM for shikimate (at pH 9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17649975};
CC KM=42.4 uM for NADP (at pH 9 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17649975};
CC Note=kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25
CC degrees Celsius). {ECO:0000269|PubMed:17649975};
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:17649975}.
CC -!- MISCELLANEOUS: AroE is dependent on the hydrogen ion concentration of
CC the environment. A low pH environment favors the formation of SA and
CC NADP, whereas a high pH condition favors the formation of DHSA and
CC NADPH. {ECO:0000303|PubMed:17649975}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AE000657; AAC07007.1; -; Genomic_DNA.
DR PIR; F70377; F70377.
DR RefSeq; NP_213611.1; NC_000918.1.
DR RefSeq; WP_010880549.1; NC_000918.1.
DR PDB; 2HK7; X-ray; 2.50 A; A/B=1-269.
DR PDB; 2HK8; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-269.
DR PDB; 2HK9; X-ray; 2.20 A; A/B/C/D=1-269.
DR PDBsum; 2HK7; -.
DR PDBsum; 2HK8; -.
DR PDBsum; 2HK9; -.
DR AlphaFoldDB; O67049; -.
DR SMR; O67049; -.
DR STRING; 224324.aq_901; -.
DR EnsemblBacteria; AAC07007; AAC07007; aq_901.
DR KEGG; aae:aq_901; -.
DR PATRIC; fig|224324.8.peg.703; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_1_0; -.
DR InParanoid; O67049; -.
DR OMA; FGNPIKH; -.
DR OrthoDB; 1054867at2; -.
DR BRENDA; 1.1.1.25; 396.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; O67049; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0019632; P:shikimate metabolic process; IDA:UniProtKB.
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..269
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000135990"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|PubMed:17649975"
FT BINDING 19..21
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 66
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 91
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 106
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 130..134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 153..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|PubMed:17649975"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 216
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT BINDING 242
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:17649975"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2HK9"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:2HK9"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:2HK9"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:2HK9"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:2HK9"
SQ SEQUENCE 269 AA; 30106 MW; 3F2E5E490FB9ADB7 CRC64;
MINAQTQLYG VIGFPVKHSL SPVFQNALIR YAGLNAVYLA FEINPEELKK AFEGFKALKV
KGINVTVPFK EEIIPLLDYV EDTAKEIGAV NTVKFENGKA YGYNTDWIGF LKSLKSLIPE
VKEKSILVLG AGGASRAVIY ALVKEGAKVF LWNRTKEKAI KLAQKFPLEV VNSPEEVIDK
VQVIVNTTSV GLKDKDPEIF NYDLIKKDHV VVDIIYKETK LLKKAKEKGA KLFDGLPMLL
WQGIEAFKIW NGCEVPYSVA ERSVRDLRG
