AROE_VIBCH
ID AROE_VIBCH Reviewed; 278 AA.
AC Q9KVT3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=VC_0056;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH SHIKIMATE, AND
RP SUBUNIT.
RA Halavaty A.S., Light S.H., Shuvalova L., Papazisi L., Anderson W.F.;
RT "2.49 Angstrom resolution crystal structure of shikimate 5-dehydrogenase
RT (aroE) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with
RT shikimate.";
RL Submitted (NOV-2010) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP,
RP AND SUBUNIT.
RA Halavaty A.S., Light S.H., Minasov G., Shuvalova L., Papazisi L.,
RA Anderson W.F.;
RT "2.4 Angstrom resolution crystal structure of shikimate 5-dehydrogenase
RT (aroE) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with
RT shikimate and NADPH.";
RL Submitted (JUN-2011) 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 or homotetramer. {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; AE003852; AAF93234.1; -; Genomic_DNA.
DR PIR; G82370; G82370.
DR RefSeq; NP_229715.1; NC_002505.1.
DR RefSeq; WP_000168154.1; NZ_LT906614.1.
DR PDB; 3PGJ; X-ray; 2.49 A; A/B/C/D=1-278.
DR PDB; 3SEF; X-ray; 2.40 A; A/B/C/D=1-278.
DR PDBsum; 3PGJ; -.
DR PDBsum; 3SEF; -.
DR AlphaFoldDB; Q9KVT3; -.
DR SMR; Q9KVT3; -.
DR STRING; 243277.VC_0056; -.
DR DNASU; 2614442; -.
DR EnsemblBacteria; AAF93234; AAF93234; VC_0056.
DR GeneID; 57741444; -.
DR KEGG; vch:VC_0056; -.
DR PATRIC; fig|243277.26.peg.54; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_2_1_6; -.
DR OMA; FGNPIKH; -.
DR BioCyc; VCHO:VC0056-MON; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000000584; Chromosome 1.
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..278
FT /note="Shikimate dehydrogenase (NADP(+))"
FT /id="PRO_0000136048"
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 18..20
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 65
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
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"
FT BINDING 106
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 130..134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 154..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.3"
FT BINDING 223
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222"
FT BINDING 248
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00222,
FT ECO:0000269|Ref.2"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:3SEF"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3SEF"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:3SEF"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:3SEF"
SQ SEQUENCE 278 AA; 30250 MW; CC84863333B19066 CRC64;
MASQIDQYAV FGNPINHSKS PFIHTLFARQ TQQSMIYTAQ CVPVDGFTEA AKHFFAQGGR
GCNVTVPFKE EAYRFADRLT ERARLAGAVN TLKKLDDGEI LGDNTDGEGL VQDLLAQQVL
LKGATILLIG AGGAARGVLK PLLDQQPASI TVTNRTFAKA EQLAELVAAY GEVKAQAFEQ
LKQSYDVIIN STSASLDGEL PAIDPVIFSS RSVCYDMMYG KGYTVFNQWA RQHGCAQAID
GLGMLVGQAA ESFMLWRGLR PGTKQILREL RKNLEGAL
