AROE_AZOC5
ID AROE_AZOC5 Reviewed; 281 AA.
AC A8IFY6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222};
DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; OrderedLocusNames=AZC_0003;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC (SA). {ECO:0000255|HAMAP-Rule:MF_00222}.
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:0000255|HAMAP-Rule:MF_00222};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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; AP009384; BAF86001.1; -; Genomic_DNA.
DR RefSeq; WP_012168534.1; NC_009937.1.
DR AlphaFoldDB; A8IFY6; -.
DR SMR; A8IFY6; -.
DR STRING; 438753.AZC_0003; -.
DR EnsemblBacteria; BAF86001; BAF86001; AZC_0003.
DR KEGG; azc:AZC_0003; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_2_0_5; -.
DR OMA; FGNPIKH; -.
DR OrthoDB; 1054867at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000270; Chromosome.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR TIGRFAMs; TIGR00507; aroE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..281
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000325101"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 14..16
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 61
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 86
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 101
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 127..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 151..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 218
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
SQ SEQUENCE 281 AA; 29633 MW; B671580DF7A5C194 CRC64;
MKRVAIFGHP VIHSRSPLVH GYWLKQHGIA GDYVRHDVAP DEAEAFFARF AEQGYAGGNV
TIPHKEVAFN ALAEADPVAR ALGVANTLWL EDGRLFGANT DAPGFLSNLD VTAPGWDANP
RVALVLGAGG ASRAVLYGFL QRGFDKVLLA NRTLARAEAL AAHFGPRVVP IGWDGVSASL
KEAQVVANTT SLGMKGQPPL DLDLSVLADD AVVADVVYVP LETPLLKAAK ARGLRTVDGL
GMLLHQAVPG FARWFGVTPQ VDAGLRDLIV ADLAAKGQLG A
