AROE_HELPY
ID AROE_HELPY Reviewed; 263 AA.
AC P56119;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=HP_1249;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP,
RP AND SUBUNIT.
RA Cheng W.C., Lin S.C., Wang W.C.;
RT "Crystal structure of the shikimate 5-dehydrogenase (aroE) from
RT Helicobacter pylori in complex with shikimate and NADPH.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH SHIKIMATE, AND
RP SUBUNIT.
RA Cheng W.C., Lin S.C., Wang W.C.;
RT "Crystal structure of shikimate dehydrogenase (aroE) mutants from
RT Helicobacter pylori in complex with shikimate.";
RL Submitted (DEC-2012) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH SHIKIMATE.
RA Cheng W.C., Chen T.J., Wang W.C.;
RT "Crystal structure of shikimate dehydrogenase (aroE) clinical v2356 from
RT Helicobacter pylori in complex with shikimate.";
RL Submitted (JAN-2013) to the PDB data bank.
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|Ref.2, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00222}.
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DR EMBL; AE000511; AAD08294.1; -; Genomic_DNA.
DR PIR; A64676; A64676.
DR RefSeq; NP_208041.1; NC_000915.1.
DR RefSeq; WP_000769617.1; NC_018939.1.
DR PDB; 3PHG; X-ray; 1.57 A; A/B=1-263.
DR PDB; 3PHH; X-ray; 1.42 A; A=1-263.
DR PDB; 3PHI; X-ray; 2.04 A; A/B=1-263.
DR PDB; 3PHJ; X-ray; 2.30 A; A/B=1-263.
DR PDB; 4FOO; X-ray; 2.55 A; A/B=1-263.
DR PDB; 4FOS; X-ray; 1.72 A; A=1-263.
DR PDB; 4FPX; X-ray; 2.40 A; A/B=1-263.
DR PDB; 4FQ8; X-ray; 2.07 A; A/B=1-263.
DR PDB; 4FR5; X-ray; 2.20 A; A/B=1-263.
DR PDB; 4FSH; X-ray; 2.85 A; A/B=1-263.
DR PDBsum; 3PHG; -.
DR PDBsum; 3PHH; -.
DR PDBsum; 3PHI; -.
DR PDBsum; 3PHJ; -.
DR PDBsum; 4FOO; -.
DR PDBsum; 4FOS; -.
DR PDBsum; 4FPX; -.
DR PDBsum; 4FQ8; -.
DR PDBsum; 4FR5; -.
DR PDBsum; 4FSH; -.
DR AlphaFoldDB; P56119; -.
DR SMR; P56119; -.
DR IntAct; P56119; 1.
DR STRING; 85962.C694_06455; -.
DR PaxDb; P56119; -.
DR EnsemblBacteria; AAD08294; AAD08294; HP_1249.
DR KEGG; hpy:HP_1249; -.
DR PATRIC; fig|85962.47.peg.1341; -.
DR eggNOG; COG0169; Bacteria.
DR OMA; FGNPIKH; -.
DR PhylomeDB; P56119; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000429; 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; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR PANTHER; PTHR21089; PTHR21089; 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..263
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136007"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000305|Ref.2, ECO:0000305|Ref.3"
FT BINDING 16..18
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT BINDING 65
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT BINDING 90
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 105
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 125..129
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 210
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2"
FT BINDING 237
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3PHG"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3PHG"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:3PHH"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:3PHH"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3PHH"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:3PHH"
SQ SEQUENCE 263 AA; 29273 MW; A34E5BD3E54C4937 CRC64;
MKLKSFGVFG NPIKHSKSPL IHNACFLTFQ KELRFLGHYH PILLPLESHI KSEFLHLGLS
GANVTLPFKE RAFQVCDKIK GIALECGAVN TLVLENDELV GYNTDALGFY LSLKQKNYQN
ALILGAGGSA KALACELKKQ GLQVSVLNRS SRGLDFFQRL GCDCFMEPPK SAFDLIINAT
SASLHNELPL NKEVLKGYFK EGKLAYDLAY GFLTPFLSLA KELKTPFQDG KDMLIYQAAL
SFEKFSASQI PYSKAFEVMR SVF
