ID A4ZPQ6_BACTS Unreviewed; 238 AA.
AC A4ZPQ6;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
DE Flags: Fragment;
GN Name=aroE {ECO:0000313|EMBL:ABP82676.1};
OS Bacillus thuringiensis subsp. sotto.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=29340 {ECO:0000313|EMBL:ABP82676.1};
RN [1] {ECO:0000313|EMBL:ABP82676.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IEBC-T04 001 {ECO:0000313|EMBL:ABP82676.1};
RA Soufiane B., Cote J.-C.;
RT "Phylogenetic relationships of Bacillus thuringiensis serovar finitimus
RT with strains in the Bacillus cereus group sensu lato inferred from the
RT aroE, gyrB and 16S rRNA gene sequence analyses.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001648};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|ARBA:ARBA00004871}.
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DR EMBL; EF210225; ABP82676.1; -; Genomic_DNA.
DR AlphaFoldDB; A4ZPQ6; -.
DR UniPathway; UPA00053; UER00087.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0009073; P:aromatic amino acid family 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 CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_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 InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR00507; aroE; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21089:SF35; SHIKIMATE DEHYDROGENASE (NADP(+)); 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW NADP {ECO:0000256|ARBA:ARBA00022857}.
FT DOMAIN 1..75
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 101..192
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABP82676.1"
FT NON_TER 238
FT /evidence="ECO:0000313|EMBL:ABP82676.1"
SQ SEQUENCE 238 AA; 25899 MW; A68A6BEDB13E703E CRC64;
SLSPVMHNNA FEHLNMDAHY HAFLVEEEVL GEAVRGLKAL GISGFNVTTP HKVAIMEYLD
EIDPLARKIG AVNTVVHKNG RLIGYNTDGI GFVRALQSIS HEPLQGKRIL LLGAGGASRA
IYFSLADVGV KEIDVANRTV DKAKELIAAR TADVNSVALS LEKATEEQGN YDIIIQTTTI
GMHPHVEHTP LQICSLKKGT IVSDIIYNPF ETKILCEAKE QGAIIQNGID MFVYQGAL
//
