ID M1NMJ9_9CORY Unreviewed; 279 AA.
AC M1NMJ9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:AGF72583.1};
GN ORFNames=A605_07905 {ECO:0000313|EMBL:AGF72583.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72583.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF72583.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72583.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(2012).
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; CP003697; AGF72583.1; -; Genomic_DNA.
DR RefSeq; WP_015401002.1; NZ_JIAJ01000001.1.
DR AlphaFoldDB; M1NMJ9; -.
DR STRING; 1121362.A605_07905; -.
DR KEGG; chn:A605_07905; -.
DR PATRIC; fig|1121362.3.peg.1596; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_0_0_11; -.
DR OrthoDB; 9776868at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000011723; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 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; IPR041121; SDH_C.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR010110; Shikimate_DH_AroM-type.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR01809; Shik-DH-AROM; 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 Oxidoreductase {ECO:0000313|EMBL:AGF72583.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011723}.
FT DOMAIN 15..97
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 130..204
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 248..275
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
SQ SEQUENCE 279 AA; 29705 MW; BAF232235CCCE3DD CRC64;
MTGPQNPGIA HRTAVLGSPI EHSRSPILHS AGYRALGMDD WEYTRIECGA EELPHIVGAA
DESFVGFSVT MPGKFAALKF ADEVTDRARE IGSANTLVRT DGGWRADNTD CDGITGALNE
LFDGELGQIR RALVIGGGGT ARPALWSLAQ AGVGEITVVN RSDRSAELAP LVKPRGADFR
MVGYDADLET LAVAADVIVS TVPSAAIEGR ETELGHAPVL DVIYDPWPTP LIVSAAANGY
PSVGGHIMLA NQAFRQFEQF TGRQAPRAAM RRALEESLR
//
