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Database: UniProt
Entry: C4KC82_THASP
LinkDB: C4KC82_THASP
Original site: C4KC82_THASP 
ID   C4KC82_THASP            Unreviewed;       277 AA.
AC   C4KC82;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 99.
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   OrderedLocusNames=Tmz1t_3680 {ECO:0000313|EMBL:ACR02273.1};
OS   Thauera sp. (strain MZ1T).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=85643 {ECO:0000313|EMBL:ACR02273.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR02273.1, ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|EMBL:ACR02273.1,
RC   ECO:0000313|Proteomes:UP000002186};
RX   PubMed=23407619; DOI=10.4056/sigs.2696029;
RA   Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA   Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA   Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT   "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL   Stand. Genomic Sci. 6:325-335(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}.
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DR   EMBL; CP001281; ACR02273.1; -; Genomic_DNA.
DR   RefSeq; WP_004321312.1; NC_011662.2.
DR   AlphaFoldDB; C4KC82; -.
DR   STRING; 85643.Tmz1t_3680; -.
DR   KEGG; tmz:Tmz1t_3680; -.
DR   eggNOG; COG0169; Bacteria.
DR   HOGENOM; CLU_044063_2_1_4; -.
DR   OMA; GHNTDWY; -.
DR   OrthoDB; 9776868at2; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000002186; 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: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:UP000002186}.
FT   DOMAIN          6..88
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          118..195
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          241..271
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         14..16
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         61
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         86
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         101
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         126..130
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         150..155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         217
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         219
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         241
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT   BINDING         248
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ   SEQUENCE   277 AA;  28858 MW;  9BEE6D5EC05FB798 CRC64;
     MDRYAVVGNP IAHSKSPWIH AAFARQTGQA LTYEALLAPL DDFAATVARF RAEGGRGLNV
     TVPFKLEAFA LADRRTPRAE AAGAVNTLAF GTDGILGDNT DGAGLVRDLA SHLGCPPRGR
     RILLLGAGGA TRGALLPLLD TAPADLCIAN RTAHKAVELA QAFAAHAGTV RIEGCGFEAL
     ADQRFDLVIN ATSASLSGEL PPLPPGLYAQ GALAYDMMYG RGHTPFLRAA LADGAARVAD
     GLGMLVEQAA ESFALWRGVR PDSAPVLAEL RQLIEAG
//
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