SitesBLAST
Comparing WP_009562611.1 NCBI__GCF_000021485.1:WP_009562611.1 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)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 88% coverage: 15:275/298 of query aligns to 3:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V79), G130 (= G143), G133 (= G146), A134 (= A147), N153 (= N167), R154 (= R168), T155 (≠ H169), K158 (≠ R172), T188 (≠ S209), S189 (≠ T210), V190 (≠ R211), I214 (= I235), M238 (= M261), L239 (= L262)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S31), S21 (= S33), N64 (= N76), T66 (= T78), K70 (= K82), N91 (= N103), D106 (= D118), Y216 (= Y237), L239 (= L262), Q242 (= Q265)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 88% coverage: 15:275/298 of query aligns to 3:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V79), G132 (= G145), G133 (= G146), A134 (= A147), N153 (= N167), R154 (= R168), T155 (≠ H169), T188 (≠ S209), S189 (≠ T210), V190 (≠ R211)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S31), S21 (= S33), N64 (= N76), K70 (= K82), N91 (= N103), D106 (= D118), Y216 (= Y237), L239 (= L262), Q242 (= Q265)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
38% identity, 88% coverage: 15:275/298 of query aligns to 3:252/269 of O67049
- SLS 19:21 (= SLS 31:33) binding shikimate
- D82 (≠ A94) binding NADP(+)
- N91 (= N103) binding shikimate
- D106 (= D118) binding shikimate
- GAGGA 130:134 (= GAGGA 143:147) binding NADP(+)
- I214 (= I235) binding NADP(+)
- Y216 (= Y237) binding shikimate
- G235 (= G258) binding NADP(+)
- Q242 (= Q265) binding shikimate
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
33% identity, 91% coverage: 21:292/298 of query aligns to 3:266/269 of Q5HNV1
- SLS 13:15 (= SLS 31:33) binding shikimate
- T60 (= T78) binding shikimate
- N85 (= N103) binding shikimate
- D100 (= D118) binding shikimate
- Y211 (= Y237) 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 (= Q265) binding shikimate
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)
32% identity, 94% coverage: 18:297/298 of query aligns to 6:282/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 94% coverage: 18:297/298 of query aligns to 11:287/287 of 1nvtB
- active site: K75 (= K82), D111 (= D118)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V79), G135 (= G145), G137 (≠ A147), G138 (≠ A148), A139 (≠ R149), N157 (= N167), R158 (= R168), T159 (≠ H169), K162 (≠ R172), A200 (≠ T208), T201 (≠ S209), P202 (≠ T210), I203 (≠ R211), M205 (≠ L213), L229 (≠ I235), Y231 (= Y237), M255 (= M261), L256 (= L262)
- binding zinc ion: E22 (≠ N29), H23 (= H30)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 94% coverage: 18:297/298 of query aligns to 11:287/287 of 1nvtA
- active site: K75 (= K82), D111 (= D118)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G145), A139 (≠ R149), N157 (= N167), R158 (= R168), T159 (≠ H169), K162 (≠ R172), A200 (≠ T208), T201 (≠ S209), P202 (≠ T210), I203 (≠ R211), M205 (≠ L213), L229 (≠ I235), Y231 (= Y237), G252 (= G258), M255 (= M261), L256 (= L262)
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
32% identity, 91% coverage: 21:292/298 of query aligns to 3:257/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S31), S15 (= S33), N58 (= N76), T60 (= T78), K64 (= K82), N85 (= N103), D100 (= D118), F227 (≠ L262), Q230 (= Q265)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
41% identity, 90% coverage: 21:289/298 of query aligns to 4:259/263 of 2ev9B
- active site: K64 (= K82), D100 (= D118)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S31), S16 (= S33), N58 (= N76), T60 (= T78), K64 (= K82), N85 (= N103), D100 (= D118), Q235 (= Q265)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
41% identity, 90% coverage: 21:289/298 of query aligns to 4:259/263 of Q5SJF8
- SLS 14:16 (= SLS 31:33) binding shikimate
- T60 (= T78) binding shikimate
- K64 (= K82) active site, Proton acceptor
- N85 (= N103) binding shikimate
- D100 (= D118) binding shikimate
- GAGGA 123:127 (= GAGGA 143:147) binding NADP(+)
- NRTPQR 146:151 (≠ NRHLPR 167:172) binding NADP(+)
- L205 (≠ I235) binding NADP(+)
- Y207 (= Y237) binding shikimate
- G228 (= G258) binding NADP(+)
- Q235 (= Q265) binding shikimate
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
41% identity, 90% coverage: 21:289/298 of query aligns to 4:259/262 of 2cy0A
- active site: K64 (= K82), D100 (= D118)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G143), G126 (= G146), A127 (= A147), N146 (= N167), R147 (= R168), T148 (≠ H169), R151 (= R172), T179 (≠ S209), R180 (≠ T210), V181 (≠ R211), L205 (≠ I235), L232 (= L262)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
33% identity, 91% coverage: 16:287/298 of query aligns to 11:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G143), A138 (= A144), G139 (= G145), G140 (= G146), A141 (= A147), N161 (= N167), R162 (= R168), D164 (vs. gap), F166 (vs. gap), T210 (≠ S209), G211 (≠ T210), V212 (≠ R211), M214 (≠ L213), F217 (≠ G215), V238 (≠ I235), Y240 (= Y237), G261 (= G258), M264 (= M261), M265 (≠ L262)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
33% identity, 91% coverage: 16:287/298 of query aligns to 11:290/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
33% identity, 91% coverage: 16:287/298 of query aligns to 8:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V79), G134 (= G143), A135 (= A144), G136 (= G145), G137 (= G146), A138 (= A147), N158 (= N167), R159 (= R168), D161 (vs. gap), F163 (vs. gap), T207 (≠ S209), V209 (≠ R211), M211 (≠ L213), F214 (≠ G215), V235 (≠ I235), Y237 (= Y237), M261 (= M261), M262 (≠ L262)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S31), S25 (= S33), N68 (= N76), S70 (≠ T78), K74 (= K82), N95 (= N103), D110 (= D118), Q265 (= Q265)
3pgjA 2.49 angstrom resolution crystal structure of shikimate 5- dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate
35% identity, 91% coverage: 21:292/298 of query aligns to 4:271/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S31), S16 (= S33), N59 (= N76), T61 (= T78), K65 (= K82), N86 (= N103), D102 (= D118), Q244 (= Q265)
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
35% identity, 91% coverage: 21:292/298 of query aligns to 8:275/278 of Q9KVT3
- SKS 18:20 (≠ SLS 31:33) binding shikimate
- N90 (= N103) binding shikimate
- D106 (= D118) binding shikimate
- NRTFAK 154:159 (≠ NRHLPR 167:172) binding NADP(+)
- Q248 (= Q265) binding shikimate
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 85% coverage: 22:275/298 of query aligns to 5:266/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A144), G127 (= G145), G128 (= G146), A129 (= A147), R150 (= R168), F154 (vs. gap), K199 (≠ T210), V200 (≠ R211), M202 (≠ L213), C226 (≠ I235), Y228 (= Y237), M252 (= M261), L253 (= L262)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
32% identity, 85% coverage: 22:275/298 of query aligns to 11:272/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A144), G133 (= G145), G134 (= G146), A135 (= A147), N155 (= N167), R156 (= R168), D158 (vs. gap), F160 (vs. gap), T204 (≠ S209), K205 (≠ T210), V206 (≠ R211), M208 (≠ L213), C232 (≠ I235), M258 (= M261), L259 (= L262)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 85% coverage: 22:275/298 of query aligns to 11:272/288 of P0A6D5
- S22 (= S33) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y50) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T78) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K82) 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 (= N103) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T117) 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 (= D118) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 144:147) binding NAD(+)
- NRRD 155:158 (≠ NRH- 167:169) binding NAD(+)
- K205 (≠ T210) binding NAD(+)
- CVYN 232:235 (≠ IVYN 235:238) binding NAD(+)
- G255 (= G258) binding NAD(+)
- Q262 (= Q265) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
33% identity, 85% coverage: 22:275/298 of query aligns to 11:272/288 of Q8ZPR4
Query Sequence
>WP_009562611.1 NCBI__GCF_000021485.1:WP_009562611.1
MPSAQSDLRHCWHPDGGTSVYGILGFPVNHSLSPWLHRLFAAQQELDLVYVPFPVREEDI
AVALAGLPALGIRGVNVTVPHKEAVLPLMQWLSAEALAIGAVNTICFTPSGMQGHNTDAP
GFLRALERATGDGWRQCPATVIGAGGAARAIVYALGHAGCPAIYLANRHLPRAEVLAAQF
PGLPVHPIPLDRAALSAVLPRSRLLVNTSTRGLHGEGHPELDLARMPGNGSVYDIVYNPL
ETPLLQAARQAGLGAVDGLGMLVEQGAESFRIWTGTLPQTAAVEEILRRWLQTRNTSR
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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