AROE_STAEQ
ID AROE_STAEQ Reviewed; 269 AA.
AC Q5HNV1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:19215302};
DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:19215302};
DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:19215302};
GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000303|PubMed:19215302};
GN OrderedLocusNames=SERP1163;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SHIKIMATE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-211,
RP AND SUBUNIT.
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=19215302; DOI=10.1111/j.1742-4658.2008.06856.x;
RA Han C., Hu T., Wu D., Qu S., Zhou J., Ding J., Shen X., Qu D., Jiang H.;
RT "X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase
RT from Staphylococcus epidermidis.";
RL FEBS J. 276:1125-1139(2009).
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 can also use NAD to oxidize shikimate. {ECO:0000255|HAMAP-
CC Rule:MF_00222, ECO:0000269|PubMed:19215302}.
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:19215302};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73 uM for shikimate (at pH 8 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19215302};
CC KM=100 uM for NADP (at pH 8 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19215302};
CC KM=10.6 mM for NAD (at pH 8 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:19215302};
CC Note=kcat is 22.8 sec(-1) for dehydrogenase activity with shikimate
CC (at pH 8 and at 25 degrees Celsius). kcat is 87 sec(-1) for
CC dehydrogenase activity with NAD (at pH 8 and at 25 degrees Celsius).
CC {ECO:0000269|PubMed:19215302};
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:19215302}.
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; CP000029; AAW54512.1; -; Genomic_DNA.
DR RefSeq; WP_001831091.1; NC_002976.3.
DR PDB; 3DON; X-ray; 2.10 A; A=1-269.
DR PDB; 3DOO; X-ray; 2.20 A; A=1-269.
DR PDBsum; 3DON; -.
DR PDBsum; 3DOO; -.
DR AlphaFoldDB; Q5HNV1; -.
DR SMR; Q5HNV1; -.
DR STRING; 176279.SERP1163; -.
DR EnsemblBacteria; AAW54512; AAW54512; SERP1163.
DR GeneID; 50018602; -.
DR KEGG; ser:SERP1163; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_1_9; -.
DR OMA; FGNPIKH; -.
DR BRENDA; 1.1.1.25; 5875.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; Q5HNV1; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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 NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..269
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136037"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 13..15
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:19215302"
FT BINDING 60
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:19215302"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 85
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:19215302"
FT BINDING 100
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:19215302"
FT BINDING 124..128
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 148..153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 211
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 239
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|PubMed:19215302"
FT SITE 211
FT /note="Plays a major role in the catalytic process and a
FT minor role in the substrate binding"
FT /evidence="ECO:0000269|PubMed:19215302"
FT MUTAGEN 211
FT /note="Y->F: Leads to a 345-fold decrease in the catalytic
FT efficiency and a 3-fold decrease in the affinity binding
FT for shikimate."
FT /evidence="ECO:0000269|PubMed:19215302"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3DON"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3DON"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:3DON"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:3DON"
SQ SEQUENCE 269 AA; 29947 MW; 9F9808764B9C21C4 CRC64;
MKFAVIGNPI SHSLSPLMHH ANFQSLNLEN TYEAINVPVN QFQDIKKIIS EKSIDGFNVT
IPHKERIIPY LDDINEQAKS VGAVNTVLVK DGKWIGYNTD GIGYVNGLKQ IYEGIEDAYI
LILGAGGASK GIANELYKIV RPTLTVANRT MSRFNNWSLN INKINLSHAE SHLDEFDIII
NTTPAGMNGN TDSVISLNRL ASHTLVSDIV YNPYKTPILI EAEQRGNPIY NGLDMFVHQG
AESFKIWTNL EPDIKAMKNI VIQKLKGEL
