AROE_ECOLI
ID AROE_ECOLI Reviewed; 272 AA.
AC P15770; Q2M6U6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000303|PubMed:3883995};
DE Short=SD {ECO:0000303|PubMed:3883995};
DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000269|PubMed:12637497};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:3883995};
GN OrderedLocusNames=b3281, JW3242;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30.
RX PubMed=3277621; DOI=10.1042/bj2490319;
RA Anton I.A., Coggins J.R.;
RT "Sequencing and overexpression of the Escherichia coli aroE gene encoding
RT shikimate dehydrogenase.";
RL Biochem. J. 249:319-326(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=3883995; DOI=10.1042/bj2260217;
RA Chaudhuri S., Coggins J.R.;
RT "The purification of shikimate dehydrogenase from Escherichia coli.";
RL Biochem. J. 226:217-223(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10739937; DOI=10.1107/s0907444900002377;
RA Maclean J., Campbell S.A., Pollock K., Chackrewarthy S., Coggins J.R.,
RA Lapthorn A.J.;
RT "Crystallization and preliminary X-ray analysis of shikimate dehydrogenase
RT from Escherichia coli.";
RL Acta Crystallogr. D 56:512-515(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=12637497; DOI=10.1074/jbc.m300794200;
RA Michel G., Roszak A.W., Sauve V., Maclean J., Matte A., Coggins J.R.,
RA Cygler M., Lapthorn A.J.;
RT "Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common
RT structural framework for different activities.";
RL J. Biol. Chem. 278:19463-19472(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). It displays no activity in the presence of NAD.
CC {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:12637497,
CC ECO:0000269|PubMed:3883995}.
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 ECO:0000269|PubMed:12637497};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for NADP {ECO:0000269|PubMed:12637497};
CC KM=65 uM for shikimate {ECO:0000269|PubMed:12637497};
CC Note=kcat is 14.2 min(-1) for dehydrogenase activity with NADP or
CC shikimate. {ECO:0000269|PubMed:12637497};
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: Monomer or homodimer. {ECO:0000255|HAMAP-Rule:MF_00222,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:3883995}.
CC -!- INTERACTION:
CC P15770; P31064: yedE; NbExp=2; IntAct=EBI-544087, EBI-544094;
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00710; CAA68700.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58078.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76306.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78010.1; -; Genomic_DNA.
DR PIR; S00252; S00252.
DR RefSeq; NP_417740.1; NC_000913.3.
DR RefSeq; WP_000451243.1; NZ_SSZK01000040.1.
DR PDB; 1NYT; X-ray; 1.50 A; A/B/C/D=1-271.
DR PDBsum; 1NYT; -.
DR AlphaFoldDB; P15770; -.
DR SMR; P15770; -.
DR BioGRID; 4261870; 147.
DR BioGRID; 852088; 3.
DR DIP; DIP-9153N; -.
DR IntAct; P15770; 6.
DR STRING; 511145.b3281; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR jPOST; P15770; -.
DR PaxDb; P15770; -.
DR PRIDE; P15770; -.
DR EnsemblBacteria; AAC76306; AAC76306; b3281.
DR EnsemblBacteria; BAE78010; BAE78010; BAE78010.
DR GeneID; 947776; -.
DR KEGG; ecj:JW3242; -.
DR KEGG; eco:b3281; -.
DR PATRIC; fig|1411691.4.peg.3450; -.
DR EchoBASE; EB0075; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_2_1_6; -.
DR InParanoid; P15770; -.
DR OMA; FGNPIKH; -.
DR PhylomeDB; P15770; -.
DR BioCyc; EcoCyc:AROE-MON; -.
DR BioCyc; MetaCyc:AROE-MON; -.
DR BRENDA; 1.1.1.25; 2026.
DR SABIO-RK; P15770; -.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; P15770; -.
DR PRO; PR:P15770; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IDA:EcoCyc.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:EcoCyc.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0019632; P:shikimate metabolic process; IDA:UniProtKB.
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 Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..272
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136002"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 14..16
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 61
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 86
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 102
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 126..130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:12637497"
FT BINDING 149..154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:12637497"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:12637497"
FT BINDING 215
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:12637497"
FT BINDING 244
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1NYT"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 238..253
FT /evidence="ECO:0007829|PDB:1NYT"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1NYT"
SQ SEQUENCE 272 AA; 29414 MW; 62D3797ECA1EC1E8 CRC64;
METYAVFGNP IAHSKSPFIH QQFAQQLNIE HPYGRVLAPI NDFINTLNAF FSAGGKGANV
TVPFKEEAFA RADELTERAA LAGAVNTLMR LEDGRLLGDN TDGVGLLSDL ERLSFIRPGL
RILLIGAGGA SRGVLLPLLS LDCAVTITNR TVSRAEELAK LFAHTGSIQA LSMDELEGHE
FDLIINATSS GISGDIPAIP SSLIHPGIYC YDMFYQKGKT PFLAWCEQRG SKRNADGLGM
LVAQAAHAFL LWHGVLPDVE PVIKQLQEEL SA
