SitesBLAST
Comparing WP_012045996.1 NCBI__GCF_000015165.1:WP_012045996.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
44% identity, 92% coverage: 11:279/293 of query aligns to 3:279/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ I137), G135 (= G140), G136 (= G141), V137 (= V142), D157 (= D162), L158 (≠ T163), R162 (= R167), T201 (= T201), P202 (= P202), M205 (= M205), V227 (≠ A227), A254 (= A254)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S24), N66 (= N72), T68 (= T74), N93 (= N99), D109 (= D114), Q257 (= Q257)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
44% identity, 92% coverage: 11:279/293 of query aligns to 3:279/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ I137), G135 (= G140), V137 (= V142), D157 (= D162), L158 (≠ T163), R162 (= R167), T201 (= T201), P202 (= P202), M205 (= M205), A212 (≠ P212), V227 (≠ A227), Y229 (= Y229), A254 (= A254)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (= S24), T18 (≠ S26), N66 (= N72), T68 (= T74), K72 (= K78), N93 (= N99), D109 (= D114), Q257 (= Q257)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
44% identity, 92% coverage: 11:279/293 of query aligns to 3:279/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ I137), G135 (= G140), V137 (= V142), D157 (= D162), L158 (≠ T163), R162 (= R167), T201 (= T201), P202 (= P202), M205 (= M205), V227 (≠ A227), Y229 (= Y229), A254 (= A254)
Q9X5C9 Quinate/shikimate dehydrogenase (NAD(+)); QSDH; EC 1.1.1.-; EC 1.1.1.24 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
44% identity, 92% coverage: 11:279/293 of query aligns to 4:280/283 of Q9X5C9
- S17 (= S24) binding shikimate
- SRT 17:19 (≠ SAS 24:26) binding L-quinate
- T69 (= T74) binding L-quinate; binding shikimate
- K73 (= K78) active site, Proton acceptor; binding L-quinate; binding shikimate
- N94 (= N99) binding L-quinate; binding shikimate
- D110 (= D114) binding L-quinate; binding shikimate
- GV 137:138 (= GV 141:142) binding NAD(+)
- D158 (= D162) binding NAD(+)
- R163 (= R167) binding NAD(+)
- PMGM 203:206 (≠ PIGM 202:205) binding NAD(+)
- A213 (≠ P212) binding NAD(+)
- V228 (≠ A227) binding NAD(+)
- G251 (= G250) binding NAD(+)
- Q258 (= Q257) binding L-quinate; binding shikimate
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 94% coverage: 5:279/293 of query aligns to 5:281/287 of 1nvtB
- active site: K75 (= K78), D111 (= D114)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ Y75), G135 (= G138), G137 (= G140), G138 (= G141), A139 (≠ V142), N157 (≠ L158), R158 (= R159), T159 (≠ I160), K162 (≠ T163), A200 (≠ G200), T201 (= T201), P202 (= P202), I203 (= I203), M205 (= M205), L229 (≠ A227), Y231 (= Y229), M255 (≠ L253), L256 (≠ A254)
- binding zinc ion: E22 (≠ A22), H23 (= H23)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 94% coverage: 5:279/293 of query aligns to 5:281/287 of 1nvtA
- active site: K75 (= K78), D111 (= D114)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G138), A139 (≠ V142), N157 (≠ L158), R158 (= R159), T159 (≠ I160), K162 (≠ T163), A200 (≠ G200), T201 (= T201), P202 (= P202), I203 (= I203), M205 (= M205), L229 (≠ A227), Y231 (= Y229), G252 (= G250), M255 (≠ L253), L256 (≠ A254)
Q58484 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
36% identity, 93% coverage: 7:279/293 of query aligns to 2:276/282 of Q58484
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
30% identity, 89% coverage: 16:275/293 of query aligns to 5:257/269 of Q5HNV1
- SLS 13:15 (≠ SAS 24:26) binding shikimate
- T60 (= T74) binding shikimate
- N85 (= N99) binding shikimate
- D100 (= D114) binding shikimate
- Y211 (= Y229) Plays a major role in the catalytic process and a minor role in the substrate binding; mutation to F: Leads to a 345-fold decrease in the catalytic efficiency and a 3-fold decrease in the affinity binding for shikimate.
- Q239 (= Q257) binding shikimate
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 89% coverage: 7:267/293 of query aligns to 2:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ Y75), G130 (= G138), G133 (= G141), A134 (≠ V142), N153 (≠ D162), R154 (≠ T163), T155 (≠ E164), K158 (≠ R167), T188 (= T201), S189 (≠ P202), V190 (≠ I203), I214 (≠ A227), M238 (≠ L253), L239 (≠ A254)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S24), S21 (= S26), N64 (= N72), T66 (= T74), K70 (= K78), N91 (= N99), D106 (= D114), Y216 (= Y229), L239 (≠ A254), Q242 (= Q257)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 89% coverage: 7:267/293 of query aligns to 2:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ Y75), G132 (= G140), G133 (= G141), A134 (≠ V142), N153 (≠ D162), R154 (≠ T163), T155 (≠ E164), T188 (= T201), S189 (≠ P202), V190 (≠ I203)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S24), S21 (= S26), N64 (= N72), K70 (= K78), N91 (= N99), D106 (= D114), Y216 (= Y229), L239 (≠ A254), Q242 (= Q257)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
31% identity, 89% coverage: 7:267/293 of query aligns to 2:252/269 of O67049
- SLS 19:21 (≠ SAS 24:26) binding shikimate
- D82 (≠ P90) binding NADP(+)
- N91 (= N99) binding shikimate
- D106 (= D114) binding shikimate
- GAGGA 130:134 (≠ GAGGV 138:142) binding NADP(+)
- I214 (≠ A227) binding NADP(+)
- Y216 (= Y229) binding shikimate
- G235 (= G250) binding NADP(+)
- Q242 (= Q257) binding shikimate
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
36% identity, 87% coverage: 13:266/293 of query aligns to 15:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G138), A138 (= A139), G139 (= G140), G140 (= G141), A141 (≠ V142), N161 (vs. gap), R162 (vs. gap), D164 (= D162), F166 (≠ E164), T210 (= T201), G211 (≠ P202), V212 (≠ I203), M214 (= M205), F217 (≠ N208), V238 (≠ A227), Y240 (= Y229), G261 (= G250), M264 (≠ L253), M265 (≠ A254)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
36% identity, 87% coverage: 13:266/293 of query aligns to 15:277/291 of Q8Y9N5
- SLS 26:28 (≠ SAS 24:26) binding shikimate
- NRKD 161:164 (≠ ---D 162) binding NAD(+)
- M214 (= M205) binding NADP(+)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
36% identity, 87% coverage: 13:266/293 of query aligns to 12:274/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ Y75), G134 (= G138), A135 (= A139), G136 (= G140), G137 (= G141), A138 (≠ V142), N158 (vs. gap), R159 (vs. gap), D161 (= D162), F163 (≠ E164), T207 (= T201), V209 (≠ I203), M211 (= M205), F214 (≠ N208), V235 (≠ A227), Y237 (= Y229), M261 (≠ L253), M262 (≠ A254)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S24), S25 (= S26), N68 (= N72), S70 (≠ T74), K74 (= K78), N95 (= N99), D110 (= D114), Q265 (= Q257)
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
30% identity, 89% coverage: 16:275/293 of query aligns to 5:248/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S24), S15 (= S26), N58 (= N72), T60 (= T74), K64 (= K78), N85 (= N99), D100 (= D114), F227 (≠ A254), Q230 (= Q257)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
38% identity, 90% coverage: 16:278/293 of query aligns to 6:256/262 of 2cy0A
- active site: K64 (= K78), D100 (= D114)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (vs. gap), G126 (≠ K144), A127 (= A145), N146 (≠ E164), R147 (= R165), T148 (≠ A166), R151 (≠ E169), T179 (= T201), R180 (≠ P202), V181 (≠ I203), L205 (≠ A227), L232 (≠ A254)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
38% identity, 90% coverage: 16:278/293 of query aligns to 6:256/263 of 2ev9B
- active site: K64 (= K78), D100 (= D114)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S24), S16 (= S26), N58 (= N72), T60 (= T74), K64 (= K78), N85 (= N99), D100 (= D114), Q235 (= Q257)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
38% identity, 90% coverage: 16:278/293 of query aligns to 6:256/263 of Q5SJF8
- SLS 14:16 (≠ SAS 24:26) binding shikimate
- T60 (= T74) binding shikimate
- K64 (= K78) active site, Proton acceptor
- N85 (= N99) binding shikimate
- D100 (= D114) binding shikimate
- GAGGA 123:127 (≠ --GKA 143:145) binding NADP(+)
- NRTPQR 146:151 (≠ ERARAE 164:169) binding NADP(+)
- L205 (≠ A227) binding NADP(+)
- Y207 (= Y229) binding shikimate
- G228 (= G250) binding NADP(+)
- Q235 (= Q257) binding shikimate
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
33% identity, 88% coverage: 9:267/293 of query aligns to 5:272/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A139), G133 (= G140), G134 (= G141), A135 (≠ V142), N155 (vs. gap), R156 (vs. gap), D158 (= D162), F160 (≠ E164), T204 (= T201), K205 (≠ P202), V206 (≠ I203), M208 (= M205), C232 (≠ A227), M258 (≠ L253), L259 (≠ A254)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 88% coverage: 9:267/293 of query aligns to 5:272/288 of P0A6D5
- S22 (= S26) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y43) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T74) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K78) mutation to A: 3200-fold decrease in the affinity for quinate. 170-fold decrease in the affinity for shikimate.; mutation to G: 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- N92 (= N99) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T113) mutation to A: 2000-fold decrease in the affinity for quinate. 70-fold decrease in the affinity for shikimate. 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- D107 (= D114) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ AGGV 139:142) binding NAD(+)
- NRRD 155:158 (≠ ---D 162) binding NAD(+)
- K205 (≠ P202) binding NAD(+)
- CVYN 232:235 (≠ AVYS 227:230) binding NAD(+)
- G255 (= G250) binding NAD(+)
- Q262 (= Q257) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_012045996.1 NCBI__GCF_000015165.1:WP_012045996.1
MPDFTALKARKFLTGLIGAPIAHSASPAMHEHAAAALGVRCHYQLIEVAGADRAGLATLL
EGVRRLGFAGVNVTYPYKEAVVELLDELAPKAAAMGAVNTVVVRDGRLIGHNTDTTGFER
AVAPLLSQTGRGAVALIGAGGVGKAIAFALANLNVAGLRIYDTERARAERLARLLPASTG
AVVVDSVERALQGAAGVVNGTPIGMLPNRGTPVPDHLLRTDLWVADAVYSPLWTPLLKAA
KARGAQVLLGRELAIYQAADAFELFTGLAPSTEAMGAAFDNHMAERYPAVDAA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory