AROE_HELPX
ID AROE_HELPX Reviewed; 263 AA.
AC Q56S04;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:16972983};
DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:16972983};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:16972983};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:16972983};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=SS1;
RX PubMed=16972983; DOI=10.1111/j.1742-4658.2006.05469.x;
RA Han C., Wang L., Yu K., Chen L., Hu L., Chen K., Jiang H., Shen X.;
RT "Biochemical characterization and inhibitor discovery of shikimate
RT dehydrogenase from Helicobacter pylori.";
RL FEBS J. 273:4682-4692(2006).
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). It can also use NAD to oxidize shikimate. {ECO:0000255|HAMAP-
CC Rule:MF_00222, ECO:0000269|PubMed:16972983}.
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:16972983};
CC -!- ACTIVITY REGULATION: Inhibited by curcumin, 3-(2-naphthyloxy)-4-oxo-2-
CC (trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate, butyl 2-{[3-(2-
CC naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl]oxy}propanoate,
CC 2-({2-[(2-{[2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl}-1,3-
CC benzothiazol-6-yl)amino]-2-oxoethyl}sulfanyl)-N-(2-naphthyl)acetamide,
CC and maesaquinone diacetate. {ECO:0000269|PubMed:16972983}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=148 uM for shikimate (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16972983};
CC KM=182 uM for NADP (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16972983};
CC KM=2900 uM for NAD (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16972983};
CC Note=kcat is 5.2 sec(-1) for dehydrogenase activity with NAD (at pH 8
CC and 25 degrees Celsius). kcat is 7.1 sec(-1) for dehydrogenase
CC activity with NADP (at pH 8 and 25 degrees Celsius). kcat is 7.7
CC sec(-1) for dehydrogenase activity with shikimate (at pH 8 and 25
CC degrees Celsius). {ECO:0000269|PubMed:16972983};
CC pH dependence:
CC Optimum pH is between 8 and 9. {ECO:0000269|PubMed:16972983};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:16972983};
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; AY738333; AAW22052.1; -; Genomic_DNA.
DR RefSeq; WP_077232384.1; NZ_AP017633.1.
DR AlphaFoldDB; Q56S04; -.
DR SMR; Q56S04; -.
DR STRING; 1345592.CBOM010000005_gene539; -.
DR eggNOG; COG0169; Bacteria.
DR BRENDA; 1.1.1.25; 2604.
DR UniPathway; UPA00053; UER00087.
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; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR PANTHER; PTHR21089; PTHR21089; 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 Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW Oxidoreductase.
FT CHAIN 1..263
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000431403"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 16..18
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 65
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 90
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 105
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 125..129
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 210
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
SQ SEQUENCE 263 AA; 28976 MW; 82F0CD1BFB2C3737 CRC64;
MKLKSFGVFG NPIKHSKSPL IHNACFLTFQ KELGFLGHYH PILLPLESHI KSEFLHLGLS
GANVTLPFKE RAFQICDKIK GIALECGAVN TLVVENDELV GYNTDALGFW LSLGGEGYQS
ALILGSGGSA KALACELQKQ GLKVSVLNRS ARGLDFFQRL GCDCFMDPPK STFDLIINAT
SASLNNELPL NKEVLKGYFK EGKLAYDLAY GFLTPFLSLA KELETPFQDG KDMLIYQAAL
SFEKFSASQI PYPKAFEVMR SVF
