ID A0A177QZL4_9PROT Unreviewed; 278 AA.
AC A0A177QZL4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN ORFNames=AYO46_04475 {ECO:0000313|EMBL:OAI52809.1};
OS Betaproteobacteria bacterium SCGC AG-212-J23.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI52809.1, ECO:0000313|Proteomes:UP000077532};
RN [1] {ECO:0000313|Proteomes:UP000077532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAI52809.1}.
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; LSTF01000031; OAI52809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177QZL4; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000077532; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077532}.
FT DOMAIN 7..94
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 118..187
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 278 AA; 29085 MW; A202B051DCED39FD CRC64;
MSILCGLIGA GIQGSRSPAL HQAEARAQGL DLTYRLIDLE VLRVGIEALP RLLDDAVRQG
YAGLNITFPC KQAVMPLLFG VSEEARAIGA VNTVVIAGGK SAGHNTDGPG WAWGFRRALP
DADVSRVALL GAGGAGSACA DAVLRLGARE LVVVDREAER AADLARRMNA IHGARCSAAI
DIAQALRGAS GLIHATPTGM AGILGMPLPQ SLLRRGLWVS DIVYVPLETE LLKAAKRAGC
RIMDGGHMNV GQALGAFRLF TGRNADPARM DAHFRSLG
//
