SitesBLAST
Comparing WP_029000245.1 NCBI__GCF_000430725.1:WP_029000245.1 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)
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, 95% coverage: 12:269/271 of query aligns to 11:282/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 95% coverage: 12:269/271 of query aligns to 16:287/287 of 1nvtB
- active site: K75 (= K67), D111 (= D103)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ M64), G135 (= G126), G137 (= G128), G138 (= G129), A139 (= A130), N157 (= N149), R158 (= R150), T159 (= T151), K162 (= K154), A200 (= A184), T201 (= T185), P202 (≠ A186), I203 (≠ A187), M205 (vs. gap), L229 (≠ A210), Y231 (≠ F212), M255 (= M236), L256 (≠ M237)
- binding zinc ion: E22 (vs. gap), H23 (vs. gap)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 95% coverage: 12:269/271 of query aligns to 16:287/287 of 1nvtA
- active site: K75 (= K67), D111 (= D103)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G126), A139 (= A130), N157 (= N149), R158 (= R150), T159 (= T151), K162 (= K154), A200 (= A184), T201 (= T185), P202 (≠ A186), I203 (≠ A187), M205 (vs. gap), L229 (≠ A210), Y231 (≠ F212), G252 (= G233), M255 (= M236), L256 (≠ M237)
P44774 Shikimate dehydrogenase-like protein HI_0607; SDH-L; EC 1.1.1.25 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
34% identity, 96% coverage: 8:266/271 of query aligns to 8:262/271 of P44774
- K67 (= K67) mutation K->A,H,N: Loss of activity.
- D103 (= D103) mutation D->A,N: Loss of activity.
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 84% coverage: 24:250/271 of query aligns to 25:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M64), G130 (= G126), G133 (= G129), A134 (= A130), N153 (= N149), R154 (= R150), T155 (= T151), K158 (= K154), T188 (= T185), S189 (≠ A186), V190 (≠ A187), I214 (≠ F212), M238 (= M236), L239 (≠ M237)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N64 (= N61), T66 (≠ S63), K70 (= K67), N91 (= N88), D106 (= D103), Y216 (≠ P214), L239 (≠ M237), Q242 (= Q240)
Sites not aligning to the query:
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
34% identity, 84% coverage: 24:250/271 of query aligns to 25:252/269 of O67049
Sites not aligning to the query:
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 84% coverage: 24:250/271 of query aligns to 25:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M64), G132 (= G128), G133 (= G129), A134 (= A130), N153 (= N149), R154 (= R150), T155 (= T151), T188 (= T185), S189 (≠ A186), V190 (≠ A187)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N64 (= N61), K70 (= K67), N91 (= N88), D106 (= D103), Y216 (≠ P214), L239 (≠ M237), Q242 (= Q240)
Sites not aligning to the query:
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
35% identity, 89% coverage: 23:264/271 of query aligns to 31:291/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G126), A138 (= A127), G139 (= G128), G140 (= G129), A141 (= A130), N161 (= N149), R162 (= R150), D164 (vs. gap), F166 (vs. gap), T210 (= T185), G211 (≠ A186), V212 (≠ A187), M214 (vs. gap), F217 (= F189), V238 (≠ A210), Y240 (≠ F212), G261 (= G233), M264 (= M236), M265 (= M237)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
35% identity, 89% coverage: 23:264/271 of query aligns to 31:291/291 of Q8Y9N5
- NRKD 161:164 (≠ NRT- 149:151) binding
- M214 (vs. gap) binding
Sites not aligning to the query:
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
35% identity, 89% coverage: 23:264/271 of query aligns to 28:288/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (= M64), G134 (= G126), A135 (= A127), G136 (= G128), G137 (= G129), A138 (= A130), N158 (= N149), R159 (= R150), D161 (vs. gap), F163 (vs. gap), T207 (= T185), V209 (≠ A187), M211 (vs. gap), F214 (= F189), V235 (≠ A210), Y237 (≠ F212), M261 (= M236), M262 (= M237)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N68 (= N61), S70 (= S63), K74 (= K67), N95 (= N88), D110 (= D103), Q265 (= Q240)
Sites not aligning to the query:
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
34% identity, 93% coverage: 12:263/271 of query aligns to 6:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A127), G127 (= G128), G128 (= G129), A129 (= A130), R150 (= R150), F154 (vs. gap), K199 (≠ A186), V200 (≠ A187), M202 (≠ F189), C226 (≠ A210), Y228 (≠ F212), M252 (= M236), L253 (≠ M237)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
38% identity, 89% coverage: 11:250/271 of query aligns to 5:245/263 of 2ev9B
- active site: K64 (= K67), D100 (= D103)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (≠ N20), S16 (≠ K22), N58 (= N61), T60 (≠ S63), K64 (= K67), N85 (= N88), D100 (= D103), Q235 (= Q240)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
38% identity, 89% coverage: 11:250/271 of query aligns to 5:245/263 of Q5SJF8
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
34% identity, 93% coverage: 12:263/271 of query aligns to 12:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A127), G133 (= G128), G134 (= G129), A135 (= A130), N155 (= N149), R156 (= R150), D158 (≠ A152), F160 (vs. gap), T204 (= T185), K205 (≠ A186), V206 (≠ A187), M208 (≠ F189), C232 (≠ A210), M258 (= M236), L259 (≠ M237)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 93% coverage: 12:263/271 of query aligns to 12:284/288 of P0A6D5
- S22 (≠ N20) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (≠ F37) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (= S63) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K67) 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 (= N88) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T102) 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 (= D103) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 127:130) binding
- NRRD 155:158 (≠ NRTA 149:152) binding
- K205 (≠ A186) binding
- CVYN 232:235 (≠ AAFI 210:213) binding
- G255 (= G233) binding
- Q262 (= Q240) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
38% identity, 89% coverage: 11:250/271 of query aligns to 5:245/262 of 2cy0A
- active site: K64 (= K67), D100 (= D103)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G126), G126 (= G129), A127 (= A130), N146 (= N149), R147 (= R150), T148 (= T151), R151 (≠ K154), T179 (= T185), R180 (≠ A186), V181 (≠ A187), L205 (≠ A210), L232 (≠ M237)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
37% identity, 88% coverage: 12:250/271 of query aligns to 239:474/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (= I12), S247 (≠ N20), S249 (≠ K22), T292 (≠ S63), K296 (= K67), N317 (= N88), D334 (= D103), Y436 (≠ F212), Q464 (= Q240), Q468 (= Q244)
Sites not aligning to the query:
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
37% identity, 88% coverage: 12:250/271 of query aligns to 239:474/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (≠ N20), S249 (≠ K22), C291 (≠ V62), K296 (= K67), N317 (= N88), D334 (= D103), Y436 (≠ F212), Q464 (= Q240)
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
38% identity, 88% coverage: 12:250/271 of query aligns to 239:476/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (= I12), S247 (≠ N20), S249 (≠ K22), T292 (≠ S63), K296 (= K67), N317 (= N88), D334 (= D103), Y438 (≠ F212), Q466 (= Q240), Q470 (= Q244)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ M64), P294 (= P65), K296 (= K67), D334 (= D103), G354 (= G128), G355 (= G129), A356 (= A130), N374 (= N149), R375 (= R150), T376 (= T151), R379 (≠ K154), T409 (= T185), S410 (≠ A186), M411 (≠ A187), A436 (= A210), M462 (= M236), F463 (≠ M237)
Sites not aligning to the query:
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
29% identity, 95% coverage: 11:268/271 of query aligns to 4:266/269 of Q5HNV1
- SLS 13:15 (≠ NVK 20:22) binding
- T60 (≠ S63) binding
- N85 (= N88) binding
- D100 (= D103) binding
- Y211 (≠ F212) 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 (= Q240) binding
Query Sequence
>WP_029000245.1 NCBI__GCF_000430725.1:WP_029000245.1
MPRSIPTLCGSIMGSPFTFNVKVHNAAYAALGLDYTFVCFGVEDVPGAIAAIRTLGIRGM
NVSMPHKQAVIAHLDALDETARAIGAVNTINHVDGKLTGYNTDCIGAVRALEEITTLPGQ
RIALLGAGGAARAIAYGLREAGARVTVFNRTAQKAQALAQDFGLEFGGTLENFEAERFDG
VVNATAAGFKAPDVNPIAGRLAPHLFVMDAAFIPVRSRLIRDAEALGCRTSDGTRMMLHQ
ARGQVELYTGGQQAPLEAMSAALLAEIERVG
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