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Database: UniProt
Entry: G4FBY6_9GAMM
LinkDB: G4FBY6_9GAMM
Original site: G4FBY6_9GAMM 
ID   G4FBY6_9GAMM            Unreviewed;       272 AA.
AC   G4FBY6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
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 {ECO:0000256|HAMAP-Rule:MF_00222};
GN   ORFNames=HAL1_19606 {ECO:0000313|EMBL:EHA13749.1};
OS   Halomonas sp. HAL1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA13749.1, ECO:0000313|Proteomes:UP000005692};
RN   [1] {ECO:0000313|EMBL:EHA13749.1, ECO:0000313|Proteomes:UP000005692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX   PubMed=22156396; DOI=10.1128/JB.06359-11;
RA   Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA   Wang G., Rensing C.;
RT   "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT   Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL   J. Bacteriol. 194:199-200(2012).
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}.
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:EHA13749.1}.
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DR   EMBL; AGIB01000088; EHA13749.1; -; Genomic_DNA.
DR   RefSeq; WP_008959775.1; NZ_CP130610.1.
DR   AlphaFoldDB; G4FBY6; -.
DR   PATRIC; fig|550984.5.peg.3802; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000005692; 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}.
FT   DOMAIN          7..89
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          117..192
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          237..267
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         15..17
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         62
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         87
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         103
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         127..131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         151..156
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         216
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         244
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   272 AA;  29148 MW;  304AF72CC6EB3944 CRC64;
     MTDRYCVFGN PIKHSKSPLI HAEFAHQTQQ ALEYTAEEAP LDGFAGAWRA FIDAGGRGAN
     VTVPFKEDAF ALCDTLSHRA RRAGAVNTLI LGGNGRTYGD TTDGIGLVRD LTFHRVALAG
     KRILVVGAGG AVRGILEPLL VEQPSEVVVV NRTAAKAAQL ASDFVDLGTV HGGGFDTVSG
     VFDVVINGTS ASLTGELPPL PDTLFAPHAW AYDMMYGAEP TVFLQWAGPR GAKLLDGLGM
     LVEQAAESFF LWRNVRPDTV PVREILRQSL NY
//
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