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Database: UniProt
Entry: A0A3P5W669_9RHOB
LinkDB: A0A3P5W669_9RHOB
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ID   A0A3P5W669_9RHOB        Unreviewed;       276 AA.
AC   A0A3P5W669;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
DE            Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
GN   Name=aroE_1 {ECO:0000313|EMBL:VDC16941.1};
GN   Synonyms=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN   ORFNames=PARPLA_00281 {ECO:0000313|EMBL:VDC16941.1};
OS   Rhodobacteraceae bacterium THAF1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2483814 {ECO:0000313|EMBL:VDC16941.1, ECO:0000313|Proteomes:UP000275054};
RN   [1] {ECO:0000313|EMBL:VDC16941.1, ECO:0000313|Proteomes:UP000275054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATHAF1 {ECO:0000313|EMBL:VDC16941.1};
RA   Criscuolo A.;
RL   Submitted (NOV-2018) 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:0000256|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:0000256|ARBA:ARBA00001648, ECO:0000256|HAMAP-
CC         Rule:MF_00222};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7. {ECO:0000256|ARBA:ARBA00004871, ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00222}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR   EMBL; UXAS01000011; VDC16941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P5W669; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000275054; Unassembled WGS sequence.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
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   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR046346; Aminoacid_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   NCBIfam; TIGR00507; aroE; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00222};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00222};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00222}; Reference proteome {ECO:0000313|Proteomes:UP000275054}.
FT   DOMAIN          10..92
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          129..196
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          244..267
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         18..20
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         65
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         81
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         90
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         106
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         132..136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         221
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         223
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         244
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         251
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   276 AA;  29337 MW;  971B1B73E73E11FC CRC64;
     MTDTIPVAAV LGHPIAHSRS PRVHGHWLAR YGIAGHYVPL DVAPDNLGAV LAQMPSMGFV
     GCNVTLPHKE AALQIAHHVT DRAALIGAAN TVTFRADGTI HADNTDGVGF IENLRQNAPD
     WRPRSGPAAV YGAGGAARAV VVALLDAGVP QIRIANRSRG RAEGLRQEFG SRLEVVDWSQ
     AGNILDDAET VVNTTSLGMQ GKPAFRVPLD GLRRGATVTD IVYTPLETPF LATAREAGCT
     CVDGLGMLLH QAVPGFERWF GQRPEVDDEL RAVVLA
//
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