ID Q6YBA0_STAEP Unreviewed; 160 AA.
AC Q6YBA0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
DE Flags: Fragment;
OS Staphylococcus epidermidis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282 {ECO:0000313|EMBL:AAO60583.1};
RN [1] {ECO:0000313|EMBL:AAO60583.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MCL8827 {ECO:0000313|EMBL:AAO60583.1};
RA Anderson A.S., Wang X.-M., McClements W., Noble L., Jansen K.;
RT "Establishment of a multilocus sequence typing system for Staphylococcus
RT epidermidis.";
RL Submitted (OCT-2002) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY163304; AAO60583.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YBA0; -.
DR UniPathway; UPA00053; UER00087.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
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 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:SF35; 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;
FT DOMAIN 2..60
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 82..157
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAO60583.1"
FT NON_TER 160
FT /evidence="ECO:0000313|EMBL:AAO60583.1"
SQ SEQUENCE 160 AA; 17850 MW; 65692DA75217FC81 CRC64;
LENTYEAINV PVNQFQDIKK IISEKSIDGF NVTIPHKERI IPYLDDINEQ AKSVGAVNTV
LVKDGKWIGY NTDGIGYVNG LKQIYEGIED AYILILGAGG ASKGISNELY KIVRPTLTVA
NRTMSRFNNW SLNINKINLS HAERHLDEFD IIINTTPAGM
//