ID   AROE_METJA              Reviewed;         282 AA.
AC   Q58484;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 149.
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=MJ1084;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX   PubMed=12906831; DOI=10.1016/s0969-2126(03)00159-x;
RA   Padyana A.K., Burley S.K.;
RT   "Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP:
RT   insights into function and evolution.";
RL   Structure 11:1005-1013(2003).
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       ECO:0000269|PubMed:12906831}.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR   EMBL; L77117; AAB99086.1; -; Genomic_DNA.
DR   PIR; C64435; C64435.
DR   RefSeq; WP_010870596.1; NC_000909.1.
DR   PDB; 1NVT; X-ray; 2.35 A; A/B=1-282.
DR   PDBsum; 1NVT; -.
DR   AlphaFoldDB; Q58484; -.
DR   SMR; Q58484; -.
DR   STRING; 243232.MJ_1084; -.
DR   PaxDb; 243232-MJ_1084; -.
DR   EnsemblBacteria; AAB99086; AAB99086; MJ_1084.
DR   GeneID; 1451980; -.
DR   KEGG; mja:MJ_1084; -.
DR   eggNOG; arCOG01033; Archaea.
DR   HOGENOM; CLU_044063_4_1_2; -.
DR   InParanoid; Q58484; -.
DR   OrthoDB; 8744at2157; -.
DR   PhylomeDB; Q58484; -.
DR   BioCyc; MetaCyc:MONOMER-18802; -.
DR   BRENDA; 1.1.1.25; 3260.
DR   UniPathway; UPA00053; UER00087.
DR   EvolutionaryTrace; Q58484; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..282
FT                   /note="Shikimate dehydrogenase (NADP(+))"
FT                   /id="PRO_0000136060"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         19..21
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         66
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         91
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         106
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         130..134
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT                   ECO:0000269|PubMed:12906831"
FT   BINDING         152..157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT                   ECO:0000269|PubMed:12906831"
FT   BINDING         196
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT                   ECO:0000269|PubMed:12906831"
FT   BINDING         200
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:12906831"
FT   BINDING         224
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:12906831"
FT   BINDING         226
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   BINDING         247
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           21..31
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           51..58
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           82..87
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           106..118
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          125..129
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           133..142
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          144..151
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           155..169
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           232..238
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   TURN            239..241
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           248..263
FT                   /evidence="ECO:0007829|PDB:1NVT"
FT   HELIX           269..280
FT                   /evidence="ECO:0007829|PDB:1NVT"
SQ   SEQUENCE   282 AA;  30877 MW;  E7398E5D642F7BD1 CRC64;
     MINAKTKVIG LIGHPVEHSF SPIMHNAAFK DKGLNYVYVA FDVLPENLKY VIDGAKALGI
     VGFNVTIPHK IEIMKYLDEI DKDAQLIGAV NTIKIEDGKA IGYNTDGIGA RMALEEEIGR
     VKDKNIVIYG AGGAARAVAF ELAKDNNIII ANRTVEKAEA LAKEIAEKLN KKFGEEVKFS
     GLDVDLDGVD IIINATPIGM YPNIDVEPIV KAEKLREDMV VMDLIYNPLE TVLLKEAKKV
     NAKTINGLGM LIYQGAVAFK IWTGVEPNIE VMKNAIIDKI TK
//