AROE_HAEIN
ID AROE_HAEIN Reviewed; 272 AA.
AC P43876;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
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};
GN OrderedLocusNames=HI_0655 {ECO:0000312|EMBL:AAC22314.1};
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=12837789; DOI=10.1128/jb.185.14.4144-4151.2003;
RA Ye S., Von Delft F., Brooun A., Knuth M.W., Swanson R.V., McRee D.E.;
RT "The crystal structure of shikimate dehydrogenase (AroE) reveals a unique
RT NADPH binding mode.";
RL J. Bacteriol. 185:4144-4151(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:12837789}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; L42023; AAC22314.1; -; Genomic_DNA.
DR PIR; H64084; H64084.
DR RefSeq; NP_438815.1; NC_000907.1.
DR RefSeq; WP_005694487.1; NC_000907.1.
DR PDB; 1P74; X-ray; 2.40 A; A/B=1-272.
DR PDB; 1P77; X-ray; 1.95 A; A=1-272.
DR PDBsum; 1P74; -.
DR PDBsum; 1P77; -.
DR AlphaFoldDB; P43876; -.
DR SMR; P43876; -.
DR STRING; 71421.HI_0655; -.
DR DrugBank; DB02363; 2'-Monophosphoadenosine-5'-Diphosphate.
DR EnsemblBacteria; AAC22314; AAC22314; HI_0655.
DR KEGG; hin:HI_0655; -.
DR PATRIC; fig|71421.8.peg.684; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_2_1_6; -.
DR OMA; FGNPIKH; -.
DR PhylomeDB; P43876; -.
DR BioCyc; HINF71421:G1GJ1-690-MON; -.
DR BRENDA; 1.1.1.25; 2529.
DR SABIO-RK; P43876; -.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; P43876; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
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..272
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136006"
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 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:12837789"
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:12837789"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12837789"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 215
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1P77"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1P74"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1P77"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1P74"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:1P77"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:1P77"
SQ SEQUENCE 272 AA; 29760 MW; 3B7A92AF22D4470B CRC64;
MDLYAVWGNP IAQSKSPLIQ NKLAAQTHQT MEYIAKLGDL DAFEQQLLAF FEEGAKGCNI
TSPFKERAYQ LADEYSQRAK LAEACNTLKK LDDGKLYADN TDGIGLVTDL QRLNWLRPNQ
HVLILGAGGA TKGVLLPLLQ AQQNIVLANR TFSKTKELAE RFQPYGNIQA VSMDSIPLQT
YDLVINATSA GLSGGTASVD AEILKLGSAF YDMQYAKGTD TPFIALCKSL GLTNVSDGFG
MLVAQAAHSF HLWRGVMPDF VSVYEQLKKA ML
