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Database: UniProt
Entry: A0A0Q6LHN0_9BURK
LinkDB: A0A0Q6LHN0_9BURK
Original site: A0A0Q6LHN0_9BURK 
ID   A0A0Q6LHN0_9BURK        Unreviewed;       279 AA.
AC   A0A0Q6LHN0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   Name=aroE {ECO:0000313|EMBL:KQU67219.1};
GN   ORFNames=ASC88_09440 {ECO:0000313|EMBL:KQU67219.1};
OS   Rhizobacter sp. Root29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU67219.1, ECO:0000313|Proteomes:UP000051195};
RN   [1] {ECO:0000313|EMBL:KQU67219.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU67219.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU67219.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU67219.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQU67219.1}.
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DR   EMBL; LMCN01000042; KQU67219.1; -; Genomic_DNA.
DR   RefSeq; WP_056806250.1; NZ_LMCN01000042.1.
DR   AlphaFoldDB; A0A0Q6LHN0; -.
DR   STRING; 1736511.ASC88_09440; -.
DR   OrthoDB; 9776868at2; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000051195; Unassembled WGS sequence.
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   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; 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   NCBIfam; TIGR00507; aroE; 1.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR   Pfam; PF18317; SDH_C; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KQU67219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051195}.
FT   DOMAIN          6..88
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          115..196
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          241..271
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   279 AA;  28793 MW;  B1878944B88C57DA CRC64;
     MDRYVVAGNP VEHSQSPFIH ARFAAQTGQA LHYDRLLCPL DGFADTVRRF AADGGRGCNI
     TVPFKFDAFA LAARRTDRAT LAGAANILRF DAEGWLADNA DGCGLVRDIE RNAGHALAGQ
     RVLVIGAGGG AAGALGPLLA ARPAQLVLAN RSVDKAQALV ARHAAPARAA GAELQATGLA
     DCGEAFDIVV NASASSLQGA GIPVSPRVLR AGSLALDMMY GPAAQHFVAW AAQHGAVGRD
     GLGMLVEQAG EAFFVWRGVR PDTAPVLAEL QALLSGAGR
//
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