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Database: UniProt
Entry: A0A0D8CD34_9PROT
LinkDB: A0A0D8CD34_9PROT
Original site: A0A0D8CD34_9PROT 
ID   A0A0D8CD34_9PROT        Unreviewed;       288 AA.
AC   A0A0D8CD34;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=UF64_17700 {ECO:0000313|EMBL:KJE34215.1};
OS   Thalassospira sp. HJ.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1616823 {ECO:0000313|EMBL:KJE34215.1, ECO:0000313|Proteomes:UP000032356};
RN   [1] {ECO:0000313|EMBL:KJE34215.1, ECO:0000313|Proteomes:UP000032356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HJ {ECO:0000313|EMBL:KJE34215.1,
RC   ECO:0000313|Proteomes:UP000032356};
RA   Kiseleva L., Garushyants S.K., Goryanin I.;
RT   "Complete genome of Thalassospira sp. strain HJ.";
RL   Submitted (FEB-2015) 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: 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:KJE34215.1}.
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DR   EMBL; JYII01000020; KJE34215.1; -; Genomic_DNA.
DR   RefSeq; WP_044829902.1; NZ_JYII01000020.1.
DR   AlphaFoldDB; A0A0D8CD34; -.
DR   STRING; 1616823.UF64_17700; -.
DR   PATRIC; fig|1616823.3.peg.2756; -.
DR   OrthoDB; 9792692at2; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000032356; 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; 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; 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:UP000032356}.
FT   DOMAIN          19..101
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          135..206
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   ACT_SITE        78
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         27..29
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         74
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         99
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         115
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         141..145
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         165..170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         231
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         233
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         254
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         261
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   288 AA;  31343 MW;  52BA3BD11F85F67C CRC64;
     MTPRNPYRTL SGTSRLAGVM GWPVSHSKSP RLHGYWLAKY GIDGCYMPLP VEPENFQAAL
     ISLRNLGFSG VNVTIPQKEM AMPECDELSD RARRIGAVNT VTFSKDGRMW GDNTDGYGFI
     ENLRQEAPDI AFASGPAVVL GAGGACRAVL VALLDEGSPE IRLANRTRKR AEDLAKEIND
     PRIKVVDWPL APEAVAGASL VVNTTSLGMV GQPKLEIDLA GLPQTALVTD IVYAPLMTDL
     LLQAKERGNP IVDGLGMLLH QARPGFHRWF GIDPEVTQEL RDFVLSPD
//
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