SitesBLAST
Comparing SM_b20510 FitnessBrowser__Smeli:SM_b20510 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)
Q6BF17 D-galactonate dehydratase; GalD; EC 4.2.1.6 from Escherichia coli (strain K12)
64% identity, 100% coverage: 1:382/382 of query aligns to 1:382/382 of Q6BF17
- H185 (= H185) mutation H->N,Q: Loss of activity.
- H285 (= H285) mutation to N: Loss of activity.
- E310 (= E310) mutation to Q: Loss of activity.
3rraB Crystal structure of enolase prk14017 (target efi-500653) from ralstonia pickettii 12j with magnesium bound
65% identity, 100% coverage: 1:382/382 of query aligns to 2:375/379 of 3rraB
- active site: I35 (≠ V34), R38 (= R37), Y118 (= Y117), K145 (= K144), N147 (= N146), E151 (= E150), D184 (= D183), H186 (= H185), E210 (= E209), G235 (= G234), E236 (= E235), R237 (= R236), Q257 (= Q256), D259 (= D258), H286 (= H285), P288 (= P287), E311 (= E310)
- binding magnesium ion: D184 (= D183), E210 (= E209), E236 (= E235)
4gmeC Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
32% identity, 100% coverage: 1:382/382 of query aligns to 2:403/403 of 4gmeC
- active site: L37 (≠ V34), R40 (= R37), D211 (= D183), H213 (= H185), E237 (= E209), G262 (= G234), E263 (= E235), I264 (≠ R236), T286 (≠ D258), H313 (= H285), A315 (vs. gap), E340 (= E310)
- binding d-mannonic acid: N38 (≠ E35), Y160 (vs. gap), D211 (= D183), H213 (= H185), E237 (= E209), E263 (= E235), H313 (= H285), D317 (≠ P287), E340 (= E310), L390 (≠ N369), W403 (= W382)
- binding magnesium ion: D211 (= D183), E237 (= E209), E263 (= E235)
4gmeA Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
32% identity, 100% coverage: 1:382/382 of query aligns to 2:403/403 of 4gmeA
- active site: L37 (≠ V34), R40 (= R37), T119 (≠ K115), R148 (≠ K144), Q150 (vs. gap), Y160 (vs. gap), D211 (= D183), H213 (= H185), E237 (= E209), G262 (= G234), E263 (= E235), I264 (≠ R236), R284 (≠ Q256), T286 (≠ D258), H313 (= H285), A315 (vs. gap), E340 (= E310), W403 (= W382)
- binding carbonate ion: R148 (≠ K144), Y160 (vs. gap), D211 (= D183), E263 (= E235), E340 (= E310)
- binding magnesium ion: D211 (= D183), E237 (= E209), E263 (= E235)
Q9AAR4 D-mannonate dehydratase CC0532; ManD; EC 4.2.1.8 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
32% identity, 100% coverage: 1:382/382 of query aligns to 2:403/403 of Q9AAR4
- D211 (= D183) binding
- E237 (= E209) binding
- E263 (= E235) binding
4e4fB Crystal structure of enolase pc1_0802 (target efi-502240) from pectobacterium carotovorum subsp. Carotovorum pc1
33% identity, 100% coverage: 1:382/382 of query aligns to 2:381/381 of 4e4fB
- active site: L37 (≠ V34), R40 (= R37), R148 (≠ K144), Q150 (≠ N146), D189 (= D183), H191 (= H185), E215 (= E209), G240 (= G234), E241 (= E235), V242 (≠ R236), R262 (≠ Q256), T264 (≠ D258), H291 (= H285), P293 (= P287), E318 (= E310), W381 (= W382)
- binding magnesium ion: D189 (= D183), E215 (= E209), E241 (= E235)
3rgtA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with d-arabinohydroxamate
32% identity, 100% coverage: 1:382/382 of query aligns to 1:383/383 of 3rgtA
- active site: H122 (≠ W119), R147 (≠ K144), Q149 (≠ N146), D191 (= D183), H193 (= H185), E217 (= E209), G242 (= G234), E243 (= E235), R264 (≠ Q256), P266 (≠ D258), H293 (= H285), G294 (≠ C286), E320 (= E310), W383 (= W382)
- binding cobalt (ii) ion: D191 (= D183), E217 (= E209), E243 (= E235)
- binding (2S,3R,4R)-2,3,4,5-tetrahydroxy-N-oxo-pentanamide: N37 (≠ E35), D191 (= D183), H193 (= H185), E243 (= E235), H293 (= H285), P295 (= P287), D297 (vs. gap), E320 (= E310), W383 (= W382)
3p93C Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
32% identity, 100% coverage: 1:382/382 of query aligns to 1:384/384 of 3p93C
- active site: H122 (≠ W119), R147 (≠ K144), Q149 (vs. gap), D192 (= D183), H194 (= H185), E218 (= E209), G243 (= G234), E244 (= E235), R265 (≠ Q256), P267 (≠ D258), H294 (= H285), G295 (≠ C286), E321 (= E310), W384 (= W382)
- binding 2-keto-3-deoxygluconate: N37 (≠ E35), D192 (= D183), H194 (= H185), E244 (= E235), H294 (= H285), P296 (= P287), D298 (vs. gap), E321 (= E310), W384 (= W382)
- binding magnesium ion: D192 (= D183), E218 (= E209), E244 (= E235)
3p93A Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
32% identity, 100% coverage: 1:382/382 of query aligns to 1:384/384 of 3p93A
- active site: H122 (≠ W119), R147 (≠ K144), Q149 (vs. gap), D192 (= D183), H194 (= H185), E218 (= E209), G243 (= G234), E244 (= E235), R265 (≠ Q256), P267 (≠ D258), H294 (= H285), G295 (≠ C286), E321 (= E310), W384 (= W382)
- binding d-mannonic acid: N37 (≠ E35), D192 (= D183), H194 (= H185), E244 (= E235), H294 (= H285), P296 (= P287), D298 (vs. gap), E321 (= E310)
- binding magnesium ion: D192 (= D183), E218 (= E209), E244 (= E235)
C6D9S0 D-galactonate dehydratase family member PC1_0802; D-mannonate dehydratase; EC 4.2.1.-; EC 4.2.1.8 from Pectobacterium carotovorum subsp. carotovorum (strain PC1) (see paper)
31% identity, 100% coverage: 1:382/382 of query aligns to 1:404/404 of C6D9S0
- D212 (= D183) binding
- E238 (= E209) binding
- E264 (= E235) binding
4kwsA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and glycerol
32% identity, 100% coverage: 1:382/382 of query aligns to 1:397/397 of 4kwsA
- active site: H122 (≠ W119), R147 (≠ K144), Q149 (≠ N146), Y159 (vs. gap), D205 (= D183), H207 (= H185), E231 (= E209), G256 (= G234), E257 (= E235), R278 (≠ Q256), P280 (≠ D258), H307 (= H285), G308 (≠ C286), E334 (= E310), W397 (= W382)
- binding magnesium ion: D205 (= D183), E231 (= E209), E257 (= E235)
3qkeA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate
32% identity, 100% coverage: 1:382/382 of query aligns to 1:397/397 of 3qkeA
- active site: H122 (≠ W119), R147 (≠ K144), Q149 (≠ N146), Y159 (vs. gap), D205 (= D183), H207 (= H185), E231 (= E209), G256 (= G234), E257 (= E235), R278 (≠ Q256), P280 (≠ D258), H307 (= H285), G308 (≠ C286), E334 (= E310), W397 (= W382)
- binding D-gluconic acid: N37 (≠ E35), Y159 (vs. gap), D205 (= D183), H207 (= H185), E257 (= E235), H307 (= H285), P309 (= P287), D311 (vs. gap), E334 (= E310), W397 (= W382)
- binding magnesium ion: D205 (= D183), E231 (= E209), E257 (= E235)
3v3wA Crystal structure of an enolase from the soil bacterium cellvibrio japonicus (target efi-502161) with bound mg and glycerol
31% identity, 100% coverage: 1:382/382 of query aligns to 1:397/397 of 3v3wA
- active site: L36 (≠ V34), R39 (= R37), H122 (≠ W119), K144 (= K141), R147 (≠ K144), Q149 (≠ N146), Y159 (vs. gap), E179 (≠ N157), D205 (= D183), H207 (= H185), E231 (= E209), G256 (= G234), E257 (= E235), V258 (≠ R236), R278 (≠ Q256), T280 (≠ D258), F306 (≠ P284), H307 (= H285), G308 (vs. gap), A309 (vs. gap), E334 (= E310), W397 (= W382)
- binding magnesium ion: D205 (= D183), E231 (= E209), E257 (= E235)
B3PDB1 D-galactonate dehydratase family member RspA; D-mannonate dehydratase; Starvation sensing protein RspA homolog; EC 4.2.1.-; EC 4.2.1.8 from Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) (see paper)
31% identity, 100% coverage: 1:382/382 of query aligns to 1:402/402 of B3PDB1
- D210 (= D183) binding
- E236 (= E209) binding
- E262 (= E235) binding
3t6cA Crystal structure of an enolase from pantoea ananatis (efi target efi- 501676) with bound d-gluconate and mg
33% identity, 99% coverage: 3:379/382 of query aligns to 4:412/415 of 3t6cA
- active site: F39 (≠ V34), R42 (= R37), R150 (≠ K144), Q152 (≠ N146), D162 (≠ E149), D221 (= D183), H223 (= H185), E247 (= E209), G272 (= G234), E273 (= E235), L274 (≠ R236), R294 (≠ Q256), H296 (≠ D258), H323 (= H285), P325 (= P287), E350 (= E310)
- binding D-gluconic acid: Y156 (vs. gap), L166 (≠ I153), D221 (= D183), H223 (= H185), E273 (= E235), H323 (= H285), P325 (= P287), D327 (vs. gap), E350 (= E310)
- binding magnesium ion: D221 (= D183), E247 (= E209), E273 (= E235)
Sites not aligning to the query:
D4GJ14 D-galactonate dehydratase family member RspA; D-gluconate dehydratase; Starvation sensing protein RspA homolog; EC 4.2.1.-; EC 4.2.1.39 from Pantoea ananatis (strain LMG 20103) (see paper)
33% identity, 99% coverage: 3:379/382 of query aligns to 6:414/417 of D4GJ14
- D223 (= D183) binding
- E249 (= E209) binding
- E275 (= E235) binding
4k1wA Crystal structure of the a314p mutant of mannonate dehydratase from novosphingobium aromaticivorans complexed with mg and d-mannonate
33% identity, 100% coverage: 1:382/382 of query aligns to 11:395/395 of 4k1wA
- active site: G131 (≠ S118), R157 (≠ K144), Q159 (vs. gap), D203 (= D183), H205 (= H185), E229 (= E209), G254 (= G234), E255 (= E235), R276 (≠ Q256), T278 (≠ D258), H305 (= H285), E332 (= E310), W395 (= W382)
- binding d-mannonic acid: N47 (≠ E35), D203 (= D183), H205 (= H185), E255 (= E235), H305 (= H285), P307 (= P287), D309 (vs. gap), E332 (= E310), L382 (≠ W367), W395 (= W382)
- binding magnesium ion: D203 (= D183), E229 (= E209), E255 (= E235)
- binding 1,3-propandiol: W174 (vs. gap), H202 (≠ V182), Y208 (≠ V188)
2qjnA Crystal structure of d-mannonate dehydratase from novosphingobium aromaticivorans complexed with mg and 2-keto-3-deoxy-d-gluconate (see paper)
33% identity, 100% coverage: 1:382/382 of query aligns to 1:385/385 of 2qjnA
- active site: G121 (≠ S118), R147 (≠ K144), Q149 (vs. gap), D193 (= D183), H195 (= H185), E219 (= E209), G244 (= G234), E245 (= E235), R266 (≠ Q256), T268 (≠ D258), H295 (= H285), E322 (= E310), W385 (= W382)
- binding 2-keto-3-deoxygluconate: N37 (≠ E35), D193 (= D183), H195 (= H185), E245 (= E235), H295 (= H285), A297 (vs. gap), D299 (≠ P287), E322 (= E310), L372 (≠ W367), W385 (= W382)
- binding magnesium ion: D193 (= D183), E219 (= E209), E245 (= E235)
3sjnA Crystal structure of enolase spea_3858 (target efi-500646) from shewanella pealeana with magnesium bound
34% identity, 90% coverage: 16:357/382 of query aligns to 28:367/373 of 3sjnA
- active site: S46 (≠ G36), L49 (= L39), T139 (≠ S118), K165 (= K144), G167 (≠ N146), M171 (≠ E150), D198 (= D183), A200 (≠ H185), E225 (= E209), I247 (= I231), G250 (= G234), E251 (= E235), S252 (≠ R236), Q272 (= Q256), D274 (= D258), H301 (= H285), G302 (≠ C286), F303 (≠ P287), M325 (≠ I315), E326 (≠ H316), Q329 (≠ E319), S331 (≠ N321)
- binding magnesium ion: D198 (= D183), E225 (= E209), E251 (= E235)
3twbC Crystal structure of gluconate dehydratase (target efi-501679) from salmonella enterica subsp. Enterica serovar enteritidis str. P125109 complexed with magnesium and gluconic acid
32% identity, 100% coverage: 1:381/382 of query aligns to 4:416/417 of 3twbC
- active site: F41 (≠ V34), R44 (= R37), P123 (≠ K115), R152 (≠ K144), Q154 (≠ N146), D164 (≠ E149), D223 (vs. gap), H225 (= H185), E249 (= E209), G274 (= G234), E275 (= E235), L276 (≠ R236), R296 (≠ Q256), H298 (≠ D258), H325 (= H285), P327 (= P287), E352 (= E310)
- binding D-gluconic acid: R152 (≠ K144), Y158 (vs. gap), D223 (vs. gap), H225 (= H185), E275 (= E235), H325 (= H285), D329 (vs. gap), E352 (= E310)
- binding magnesium ion: D223 (vs. gap), E249 (= E209), E275 (= E235)
Sites not aligning to the query:
Query Sequence
>SM_b20510 FitnessBrowser__Smeli:SM_b20510
MKITKLTTYIVPPRWLFLKIETDEGVVGWGEPVVEGRALTVEAAVHELSDYLVGKDPFLI
EDHWNVLYRGGFYRGGAIHMSALAGIDQALWDIKGKALGQPVHSLLGGQCRDRIKVYSWI
GGDRPSDVANNAREVVARGFKAIKLNGCEEMQIVDTNEKIDKAVETIGLIRDAIGPHVGI
GVDFHGRVHRPMAKVLAKELEPFKLMFIEEPVLSENREALREIANHCSTPIALGERLYSR
WDFKSVLSDGFVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVD
AVSYNAFIQEQSLGIHYNEANDILDYISNKEVFAYEDGFVSIPQGPGLGIEVDEAYVMER
AKEGHRWRNPVWRHSDGSVAEW
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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