AROE_METJA
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 03-AUG-2022, entry version 143.
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 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 OMA; FGNPIKH; -.
DR OrthoDB; 98644at2157; -.
DR PhylomeDB; Q58484; -.
DR BioCyc; MetaCyc:MON-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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR046346; Aminiacid_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 PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR TIGRFAMs; TIGR00507; aroE; 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
