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Comparing CCNA_02903 FitnessBrowser__Caulo:CCNA_02903 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)
3thuA Crystal structure of an enolase from sphingomonas sp. Ska58 (efi target efi-501683) with bound mg
80% identity, 100% coverage: 1:403/403 of query aligns to 3:405/405 of 3thuA
- active site: L39 (= L37), E43 (= E41), W79 (= W77), G124 (= G122), R150 (= R148), Q152 (= Q150), Y162 (= Y160), D213 (= D211), H215 (= H213), E239 (= E237), G264 (= G262), E265 (= E263), R286 (= R284), T288 (= T286), H315 (= H313), E342 (= E340), W405 (= W403)
- binding magnesium ion: D213 (= D211), E239 (= E237), E265 (= E263)
Q1NAJ2 D-mannonate dehydratase; ManD; EC 4.2.1.8 from Sphingomonas sp. (strain SKA58) (see paper)
80% identity, 100% coverage: 1:403/403 of query aligns to 1:403/403 of Q1NAJ2
- D211 (= D211) binding
- E237 (= E237) binding
- E263 (= E263) binding
4gmeC Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
79% identity, 100% coverage: 1:403/403 of query aligns to 1:403/403 of 4gmeC
- active site: L37 (= L37), R40 (= R40), D211 (= D211), H213 (= H213), E237 (= E237), G262 (= G262), E263 (= E263), I264 (= I264), T286 (= T286), H313 (= H313), A315 (= A315), E340 (= E340)
- binding d-mannonic acid: N38 (= N38), Y160 (= Y160), D211 (= D211), H213 (= H213), E237 (= E237), E263 (= E263), H313 (= H313), D317 (= D317), E340 (= E340), L390 (= L390), W403 (= W403)
- binding magnesium ion: D211 (= D211), E237 (= E237), E263 (= E263)
4gmeA Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
79% identity, 100% coverage: 1:403/403 of query aligns to 1:403/403 of 4gmeA
- active site: L37 (= L37), R40 (= R40), T119 (≠ M119), R148 (= R148), Q150 (= Q150), Y160 (= Y160), D211 (= D211), H213 (= H213), E237 (= E237), G262 (= G262), E263 (= E263), I264 (= I264), R284 (= R284), T286 (= T286), H313 (= H313), A315 (= A315), E340 (= E340), W403 (= W403)
- binding carbonate ion: R148 (= R148), Y160 (= Y160), D211 (= D211), E263 (= E263), E340 (= E340)
- binding magnesium ion: D211 (= D211), E237 (= E237), E263 (= E263)
Q9AAR4 D-mannonate dehydratase CC0532; ManD; EC 4.2.1.8 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
79% identity, 100% coverage: 1:403/403 of query aligns to 1:403/403 of Q9AAR4
- D211 (= D211) binding
- E237 (= E237) binding
- E263 (= E263) binding
4fi4A Crystal structure of mannonate dehydratase prk15072 (target efi- 502214) from caulobacter sp. K31
78% identity, 100% coverage: 1:403/403 of query aligns to 5:407/407 of 4fi4A
- active site: L41 (= L37), R44 (= R40), H127 (= H123), R152 (= R148), Q154 (= Q150), Y164 (= Y160), S187 (= S183), D215 (= D211), H217 (= H213), E241 (= E237), G266 (= G262), E267 (= E263), I268 (= I264), R288 (= R284), T290 (= T286), C316 (= C312), H317 (= H313), G318 (= G314), A319 (= A315), E344 (= E340), W407 (= W403)
- binding magnesium ion: D215 (= D211), E241 (= E237), E267 (= E263)
B0T0B1 D-mannonate dehydratase Caul1427; ManD; EC 4.2.1.8 from Caulobacter sp. (strain K31) (see paper)
78% identity, 100% coverage: 1:403/403 of query aligns to 1:403/403 of B0T0B1
- D211 (= D211) binding
- E237 (= E237) binding
- E263 (= E263) binding
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)
68% identity, 100% coverage: 3:403/403 of query aligns to 2:404/404 of C6D9S0
- D212 (= D211) binding
- E238 (= E237) binding
- E264 (= E263) binding
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)
66% identity, 100% coverage: 3:403/403 of query aligns to 2:402/402 of B3PDB1
- D210 (= D211) binding
- E236 (= E237) binding
- E262 (= E263) binding
4il2B Crystal structure of d-mannonate dehydratase (rspa) from e. Coli cft073 (efi target efi-501585)
66% identity, 100% coverage: 3:403/403 of query aligns to 2:404/404 of 4il2B
- active site: L36 (= L37), G38 (= G39), W76 (= W77), R147 (= R148), Q149 (= Q150), Y159 (= Y160), D212 (= D211), H214 (= H213), E238 (= E237), G263 (= G262), E264 (= E263), R285 (= R284), T287 (= T286), H314 (= H313), E341 (= E340), W404 (= W403)
- binding magnesium ion: D212 (= D211), E238 (= E237), D239 (= D238), E264 (= E263)
3v3wA Crystal structure of an enolase from the soil bacterium cellvibrio japonicus (target efi-502161) with bound mg and glycerol
66% identity, 100% coverage: 3:403/403 of query aligns to 2:397/397 of 3v3wA
- active site: L36 (= L37), R39 (= R40), H122 (= H123), K144 (= K145), R147 (= R148), Q149 (= Q150), Y159 (= Y160), E179 (= E185), D205 (= D211), H207 (= H213), E231 (= E237), G256 (= G262), E257 (= E263), V258 (≠ I264), R278 (= R284), T280 (= T286), F306 (≠ C312), H307 (= H313), G308 (= G314), A309 (= A315), E334 (= E340), W397 (= W403)
- binding magnesium ion: D205 (= D211), E231 (= E237), E257 (= E263)
Q8FHC7 D-galactonate dehydratase family member RspA; D-mannonate dehydratase; Starvation sensing protein RspA homolog; EC 4.2.1.-; EC 4.2.1.8 from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
66% identity, 100% coverage: 3:403/403 of query aligns to 13:415/415 of Q8FHC7
- D223 (= D211) binding
- E249 (= E237) binding
- D250 (= D238) binding
- E275 (= E263) binding
Q1QT89 D-galactonate dehydratase family member ManD; D-gluconate dehydratase; D-mannonate dehydratase; EC 4.2.1.-; EC 4.2.1.39; EC 4.2.1.8 from Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11) (see paper)
67% identity, 100% coverage: 3:403/403 of query aligns to 2:403/403 of Q1QT89
- D211 (= D211) binding
- E237 (= E237) binding
- E263 (= E263) binding
- H313 (= H313) mutation to N: Abolishes activity with D-gluconate and D-mannonate.; mutation to Q: Abolishes activity with D-gluconate. No effect on activity with D-mannonate.
- P315 (≠ A315) mutation to A: Strongly increases activity with D-mannonate. Slightly decreases activity with D-gluconate.
4kwsA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and glycerol
67% identity, 100% coverage: 3:403/403 of query aligns to 2:397/397 of 4kwsA
- active site: H122 (= H123), R147 (= R148), Q149 (= Q150), Y159 (= Y160), D205 (= D211), H207 (= H213), E231 (= E237), G256 (= G262), E257 (= E263), R278 (= R284), P280 (≠ T286), H307 (= H313), G308 (= G314), E334 (= E340), W397 (= W403)
- binding magnesium ion: D205 (= D211), E231 (= E237), E257 (= E263)
3qkeA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate
67% identity, 100% coverage: 3:403/403 of query aligns to 2:397/397 of 3qkeA
- active site: H122 (= H123), R147 (= R148), Q149 (= Q150), Y159 (= Y160), D205 (= D211), H207 (= H213), E231 (= E237), G256 (= G262), E257 (= E263), R278 (= R284), P280 (≠ T286), H307 (= H313), G308 (= G314), E334 (= E340), W397 (= W403)
- binding D-gluconic acid: N37 (= N38), Y159 (= Y160), D205 (= D211), H207 (= H213), E257 (= E263), H307 (= H313), P309 (≠ A315), D311 (= D317), E334 (= E340), W397 (= W403)
- binding magnesium ion: D205 (= D211), E231 (= E237), E257 (= E263)
2qjjA Crystal structure of d-mannonate dehydratase from novosphingobium aromaticivorans (see paper)
69% identity, 100% coverage: 3:403/403 of query aligns to 2:402/402 of 2qjjA
- active site: G121 (= G122), R147 (= R148), Q149 (= Q150), Y159 (= Y160), D210 (= D211), H212 (= H213), E236 (= E237), G261 (= G262), E262 (= E263), R283 (= R284), T285 (= T286), H312 (= H313), E339 (= E340), W402 (= W403)
- binding magnesium ion: D210 (= D211), E236 (= E237), E262 (= E263)
A4XF23 D-mannonate dehydratase; ManD; RspA homolog; EC 4.2.1.8 from Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199) (see 2 papers)
69% identity, 100% coverage: 3:403/403 of query aligns to 2:402/402 of A4XF23
- R147 (= R148) mutation to A: Abolishes catalytic activity.; mutation to K: Decreases catalytic activity.
- Y159 (= Y160) mutation to F: Abolishes catalytic activity.
- 161:169 (vs. 162:170, 44% identical) mutation to AGAGGAGAG: Abolishes catalytic activity.
- D210 (= D211) binding
- H212 (= H213) mutation to N: Abolishes catalytic activity.
- E236 (= E237) binding
- E262 (= E263) binding
- K271 (= K272) mutation to E: No effect on catalytic activity.
- R283 (= R284) mutation to A: Abolishes catalytic activity.
- H312 (= H313) mutation to N: Abolishes catalytic activity.
- A314 (= A315) mutation to P: Decreases catalytic activity.
- E339 (= E340) mutation to Q: Abolishes catalytic activity.
4e4fB Crystal structure of enolase pc1_0802 (target efi-502240) from pectobacterium carotovorum subsp. Carotovorum pc1
65% identity, 100% coverage: 3:403/403 of query aligns to 3:381/381 of 4e4fB
- active site: L37 (= L37), R40 (= R40), R148 (= R148), Q150 (= Q150), D189 (= D211), H191 (= H213), E215 (= E237), G240 (= G262), E241 (= E263), V242 (≠ I264), R262 (= R284), T264 (= T286), H291 (= H313), P293 (≠ A315), E318 (= E340), W381 (= W403)
- binding magnesium ion: D189 (= D211), E215 (= E237), E241 (= E263)
3p93C Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
64% identity, 100% coverage: 3:403/403 of query aligns to 2:384/384 of 3p93C
- active site: H122 (= H123), R147 (= R148), Q149 (= Q150), D192 (= D211), H194 (= H213), E218 (= E237), G243 (= G262), E244 (= E263), R265 (= R284), P267 (≠ T286), H294 (= H313), G295 (= G314), E321 (= E340), W384 (= W403)
- binding 2-keto-3-deoxygluconate: N37 (= N38), D192 (= D211), H194 (= H213), E244 (= E263), H294 (= H313), P296 (≠ A315), D298 (= D317), E321 (= E340), W384 (= W403)
- binding magnesium ion: D192 (= D211), E218 (= E237), E244 (= E263)
3p93A Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
64% identity, 100% coverage: 3:403/403 of query aligns to 2:384/384 of 3p93A
- active site: H122 (= H123), R147 (= R148), Q149 (= Q150), D192 (= D211), H194 (= H213), E218 (= E237), G243 (= G262), E244 (= E263), R265 (= R284), P267 (≠ T286), H294 (= H313), G295 (= G314), E321 (= E340), W384 (= W403)
- binding d-mannonic acid: N37 (= N38), D192 (= D211), H194 (= H213), E244 (= E263), H294 (= H313), P296 (≠ A315), D298 (= D317), E321 (= E340)
- binding magnesium ion: D192 (= D211), E218 (= E237), E244 (= E263)
Query Sequence
>CCNA_02903 FitnessBrowser__Caulo:CCNA_02903
MPKIIAAKTIVTCPGRNFVTLKIMTDEGVYGLGDATLNGRELAVEAYLTQHVIPCLIGRD
AHQIEDIWQYLYRGCYWRRGPVTMAAIAAVDTALWDIKGKIAGLPVYQLLGGACRVGVMV
YGHANGETIDETLDNAAVYAQQGYKAIRLQTGVPGMSGTYGVSKDKFFYEPADSDLPKET
IWSTERYLRSTPALFEAARERLGDDLHLLHDVHHRLTPIEAARLGKDLEPYRLFWMEDAT
PAENQASFRLIRQHTTTPLAVGEIFNSIWDCKQLIEEQLIDYIRATVVHAGGITHLKKLA
SFADLHHVRTGCHGATDLSPVCMGAALHFDLSIPNFGVQEYMRHTPETDAVFPHAYTFKD
GMLHPGDAPGLGVDIDEDLAAKYPYQRAYLPIARRLDGSMHDW
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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