ID A0A160FTS1_9BURK Unreviewed; 329 AA.
AC A0A160FTS1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222};
DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222};
GN Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN ORFNames=AYM40_30940 {ECO:0000313|EMBL:ANB76605.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB76605.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB76605.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB76605.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR EMBL; CP014579; ANB76605.1; -; Genomic_DNA.
DR RefSeq; WP_063499821.1; NZ_CP014579.1.
DR AlphaFoldDB; A0A160FTS1; -.
DR STRING; 1804984.AYM40_30940; -.
DR KEGG; buz:AYM40_30940; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000076852; Chromosome 2.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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 HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21089:SF34; SHIKIMATE DEHYDROGENASE (NADP(+)); 1.
DR Pfam; PF01262; AlaDh_PNT_C; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00222};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00222}; Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT DOMAIN 54..141
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 165..246
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|Pfam:PF01262"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 62..64
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 114
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 139
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 154
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 178..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 270
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 272
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 300
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ SEQUENCE 329 AA; 34421 MW; 732CE777B249A038 CRC64;
MNTQANTQAN TQANTQANTQ ANTQANTQAN TQANTQANTQ ANAQASPQSF LVGLIGSGIG
GSLTPAMHEE EGSKLGLHYV YRRIDLEALK LDTAALADLL VAAERMGYNG LNITYPCKQA
VIPLLDELSD DARALGAVNT VLFKDGKRIG HNTDWSGFAR AFQRGLPDVS LARVVQLGAG
GAGAAVAHAT LTMGAQTLTL FDVDAARAAS LAAELQKRFP AATVSAGSSL AESLAAANGL
IHATPTGMAK LPGLPLPVEL LHSGLWVSDI VYFPIRTALL QAAEALGCRT LSGGGMAVYQ
AVDAMRIFTG LEPDAERVYT HFQSLLQRP
//
