ID A0A3Q9IXH8_9MICO Unreviewed; 271 AA.
AC A0A3Q9IXH8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN ORFNames=CVS47_01135 {ECO:0000313|EMBL:AZS36529.1};
OS Microbacterium lemovicicum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1072463 {ECO:0000313|EMBL:AZS36529.1, ECO:0000313|Proteomes:UP000276888};
RN [1] {ECO:0000313|EMBL:AZS36529.1, ECO:0000313|Proteomes:UP000276888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Viu22 {ECO:0000313|EMBL:AZS36529.1,
RC ECO:0000313|Proteomes:UP000276888};
RA ORTET P.;
RT "Microbacterium lemovicicum sp. nov., a bacterium isolated from a natural
RT uranium-rich soil.";
RL Submitted (AUG-2018) 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; CP031423; AZS36529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9IXH8; -.
DR KEGG; mlv:CVS47_01135; -.
DR OrthoDB; 9792692at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000276888; Chromosome.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
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:SF9; SHIKIMATE DEHYDROGENASE-LIKE PROTEIN HI_0607; 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:AZS36529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276888}.
FT DOMAIN 24..92
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 115..168
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 271 AA; 28349 MW; 58F569C7BF5FD1EB CRC64;
MPILNKDMTL CISLAARPSN LGTRFHNFLY EELGLNFIYK AFTTQDIEGA ISGVRALGIR
GCSVSMPFKE AVIPLVDEIE ESAAAIESVN TIVNDGGRLT ASNTDYEAIA QLIAEHRLDS
ASTVLVRGSG GMAKAVVAAF RGAGFDDLTV LARNETKGAA LAEKYGYAAV TEDPAPGARI
IVNVTPLGMD GTDAAAQAFG DDHVAAAEVV FDVVAFPAET PLIRAGRAAG AKVITGAEVI
ALQAARQFER YTGVAITPDQ VARASAFSRE G
//
