ID   Q8YDW5_BRUME            Unreviewed;       261 AA.
AC   Q8YDW5; D0B5P1;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   OrderedLocusNames=BMEII0059 {ECO:0000313|EMBL:AAL53300.1};
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL53300.1, ECO:0000313|Proteomes:UP000000419};
RN   [1] {ECO:0000313|EMBL:AAL53300.1, ECO:0000313|Proteomes:UP000000419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094
RC   {ECO:0000313|Proteomes:UP000000419};
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA   Haselkorn R., Kyrpides N., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53300.1; -; Genomic_DNA.
DR   PIR; AI3516; AI3516.
DR   RefSeq; WP_002966545.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YDW5; -.
DR   GeneID; 55591776; -.
DR   KEGG; bme:BMEII0059; -.
DR   KEGG; bmel:DK63_3187; -.
DR   PATRIC; fig|224914.52.peg.3338; -.
DR   eggNOG; COG0169; Bacteria.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000000419; Chromosome II.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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   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; SHIKIMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21089:SF34; 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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          12..95
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          123..173
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
SQ   SEQUENCE   261 AA;  27247 MW;  3DE83971878FF80F CRC64;
     MTVTGHTRVF AIIADPVHHV RTPQALNALF AARGYDGIVV PAAVPASGLK YAAAALRAFG
     NWGGFIVTVP HKTEMPAFCD RLTPRAQAAG AVNVIRREAD GSLTGELLDG VGFVRGLANA
     GHDVKGRSVY LAGAGGAASA IAFALAEAGV VRLTVVNRSS EKAGQLVARL KEHFPAGMFV
     SQGTPAGHDI IVNGTSLGLK EGDALPVDPQ YLRPEMLVAE VIMSPEVTPL LQIAKDSGCS
     IHPGKAMLDG QLAEMFDFFT R
//