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Database: UniProt
Entry: A0A158FGV0_9BURK
LinkDB: A0A158FGV0_9BURK
Original site: A0A158FGV0_9BURK 
ID   A0A158FGV0_9BURK        Unreviewed;       276 AA.
AC   A0A158FGV0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   ORFNames=AWB65_00906 {ECO:0000313|EMBL:SAL18911.1};
OS   Caballeronia humi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL18911.1, ECO:0000313|Proteomes:UP000054977};
RN   [1] {ECO:0000313|EMBL:SAL18911.1, ECO:0000313|Proteomes:UP000054977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL18911.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCNW02000002; SAL18911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158FGV0; -.
DR   STRING; 326474.AWB65_00906; -.
DR   OrthoDB; 3609723at2; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000054977; Unassembled WGS sequence.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE/SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 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}.
FT   DOMAIN          24..107
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          135..208
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
SQ   SEQUENCE   276 AA;  28416 MW;  F1D68A01F270EBF6 CRC64;
     MTEDNAFNAS LDAGLSGATR LYFIVGDPIA QVRSPAGVTA ALRAAGRDAI VVPAHVAPED
     LPAFFAAVTA MRNVDGVIIT VPHKFSAAQF CASFSDQAAF LGAVNTLRRN TDGTWHGTMC
     DGTGFVTALG DAGCNLPAKR ALLVGAGGAG SAIGHALVNQ GVASLAVRDN DAERTDALVA
     RLNALKLGSV SIADGDVRAE TYDVVVNASP MGMRADDPLP VDVSRLAATT FVGDVVTKPP
     LTPFIEAARA RGCATVTGTQ MFGRVCDRIV EFLTEA
//
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