SitesBLAST
Comparing H281DRAFT_01518 FitnessBrowser__Burk376:H281DRAFT_01518 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
78% identity, 100% coverage: 1:402/402 of query aligns to 12:415/415 of Q8FHC7
- D223 (= D210) binding
- E249 (= E236) binding
- D250 (= D237) binding
- E275 (= E262) binding
4il2B Crystal structure of d-mannonate dehydratase (rspa) from e. Coli cft073 (efi target efi-501585)
78% identity, 100% coverage: 1:402/402 of query aligns to 1:404/404 of 4il2B
- active site: L36 (= L36), G38 (= G38), W76 (= W76), R147 (= R147), Q149 (= Q149), Y159 (= Y159), D212 (= D210), H214 (= H212), E238 (= E236), G263 (= G261), E264 (= E262), R285 (= R283), T287 (= T285), H314 (= H312), E341 (= E339), W404 (= W402)
- binding magnesium ion: D212 (= D210), E238 (= E236), D239 (= D237), E264 (= E262)
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)
78% identity, 100% coverage: 1:402/402 of query aligns to 1:404/404 of C6D9S0
- D212 (= D210) binding
- E238 (= E236) binding
- E264 (= E262) binding
4e4fB Crystal structure of enolase pc1_0802 (target efi-502240) from pectobacterium carotovorum subsp. Carotovorum pc1
75% identity, 100% coverage: 1:402/402 of query aligns to 2:381/381 of 4e4fB
- active site: L37 (= L36), R40 (= R39), R148 (= R147), Q150 (= Q149), D189 (= D210), H191 (= H212), E215 (= E236), G240 (= G261), E241 (= E262), V242 (= V263), R262 (= R283), T264 (= T285), H291 (= H312), P293 (= P314), E318 (= E339), W381 (= W402)
- binding magnesium ion: D189 (= D210), E215 (= E236), E241 (= E262)
3thuA Crystal structure of an enolase from sphingomonas sp. Ska58 (efi target efi-501683) with bound mg
70% identity, 100% coverage: 2:402/402 of query aligns to 5:405/405 of 3thuA
- active site: L39 (= L36), E43 (= E40), W79 (= W76), G124 (= G121), R150 (= R147), Q152 (= Q149), Y162 (= Y159), D213 (= D210), H215 (= H212), E239 (= E236), G264 (= G261), E265 (= E262), R286 (= R283), T288 (= T285), H315 (= H312), E342 (= E339), W405 (= W402)
- binding magnesium ion: D213 (= D210), E239 (= E236), E265 (= E262)
Q1NAJ2 D-mannonate dehydratase; ManD; EC 4.2.1.8 from Sphingomonas sp. (strain SKA58) (see paper)
70% identity, 100% coverage: 2:402/402 of query aligns to 3:403/403 of Q1NAJ2
- D211 (= D210) binding
- E237 (= E236) binding
- E263 (= E262) 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)
69% identity, 100% coverage: 1:402/402 of query aligns to 1:403/403 of Q1QT89
- D211 (= D210) binding
- E237 (= E236) binding
- E263 (= E262) binding
- H313 (= H312) 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 (= P314) 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
68% identity, 100% coverage: 1:402/402 of query aligns to 1:397/397 of 4kwsA
- active site: H122 (= H122), R147 (= R147), Q149 (= Q149), Y159 (= Y159), D205 (= D210), H207 (= H212), E231 (= E236), G256 (= G261), E257 (= E262), R278 (= R283), P280 (≠ T285), H307 (= H312), G308 (= G313), E334 (= E339), W397 (= W402)
- binding magnesium ion: D205 (= D210), E231 (= E236), E257 (= E262)
3qkeA Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate
68% identity, 100% coverage: 1:402/402 of query aligns to 1:397/397 of 3qkeA
- active site: H122 (= H122), R147 (= R147), Q149 (= Q149), Y159 (= Y159), D205 (= D210), H207 (= H212), E231 (= E236), G256 (= G261), E257 (= E262), R278 (= R283), P280 (≠ T285), H307 (= H312), G308 (= G313), E334 (= E339), W397 (= W402)
- binding D-gluconic acid: N37 (= N37), Y159 (= Y159), D205 (= D210), H207 (= H212), E257 (= E262), H307 (= H312), P309 (= P314), D311 (= D316), E334 (= E339), W397 (= W402)
- binding magnesium ion: D205 (= D210), E231 (= E236), E257 (= E262)
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: 1:402/402 of query aligns to 1:402/402 of B3PDB1
- D210 (= D210) binding
- E236 (= E236) binding
- E262 (= E262) binding
4fi4A Crystal structure of mannonate dehydratase prk15072 (target efi- 502214) from caulobacter sp. K31
67% identity, 100% coverage: 1:402/402 of query aligns to 6:407/407 of 4fi4A
- active site: L41 (= L36), R44 (= R39), H127 (= H122), R152 (= R147), Q154 (= Q149), Y164 (= Y159), S187 (= S182), D215 (= D210), H217 (= H212), E241 (= E236), G266 (= G261), E267 (= E262), I268 (≠ V263), R288 (= R283), T290 (= T285), C316 (= C311), H317 (= H312), G318 (= G313), A319 (≠ P314), E344 (= E339), W407 (= W402)
- binding magnesium ion: D215 (= D210), E241 (= E236), E267 (= E262)
B0T0B1 D-mannonate dehydratase Caul1427; ManD; EC 4.2.1.8 from Caulobacter sp. (strain K31) (see paper)
67% identity, 100% coverage: 1:402/402 of query aligns to 2:403/403 of B0T0B1
- D211 (= D210) binding
- E237 (= E236) binding
- E263 (= E262) binding
3v3wA Crystal structure of an enolase from the soil bacterium cellvibrio japonicus (target efi-502161) with bound mg and glycerol
66% identity, 100% coverage: 1:402/402 of query aligns to 1:397/397 of 3v3wA
- active site: L36 (= L36), R39 (= R39), H122 (= H122), K144 (≠ Q144), R147 (= R147), Q149 (= Q149), Y159 (= Y159), E179 (= E184), D205 (= D210), H207 (= H212), E231 (= E236), G256 (= G261), E257 (= E262), V258 (= V263), R278 (= R283), T280 (= T285), F306 (≠ C311), H307 (= H312), G308 (= G313), A309 (≠ P314), E334 (= E339), W397 (= W402)
- binding magnesium ion: D205 (= D210), E231 (= E236), E257 (= E262)
4gmeC Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
65% identity, 100% coverage: 1:402/402 of query aligns to 2:403/403 of 4gmeC
- active site: L37 (= L36), R40 (= R39), D211 (= D210), H213 (= H212), E237 (= E236), G262 (= G261), E263 (= E262), I264 (≠ V263), T286 (= T285), H313 (= H312), A315 (≠ P314), E340 (= E339)
- binding d-mannonic acid: N38 (= N37), Y160 (= Y159), D211 (= D210), H213 (= H212), E237 (= E236), E263 (= E262), H313 (= H312), D317 (= D316), E340 (= E339), L390 (= L389), W403 (= W402)
- binding magnesium ion: D211 (= D210), E237 (= E236), E263 (= E262)
4gmeA Crystal structure of mannonate dehydratase (target efi-502209) from caulobacter crescentus cb15 complexed with magnesium and d-mannonate
65% identity, 100% coverage: 1:402/402 of query aligns to 2:403/403 of 4gmeA
- active site: L37 (= L36), R40 (= R39), T119 (≠ M118), R148 (= R147), Q150 (= Q149), Y160 (= Y159), D211 (= D210), H213 (= H212), E237 (= E236), G262 (= G261), E263 (= E262), I264 (≠ V263), R284 (= R283), T286 (= T285), H313 (= H312), A315 (≠ P314), E340 (= E339), W403 (= W402)
- binding carbonate ion: R148 (= R147), Y160 (= Y159), D211 (= D210), E263 (= E262), E340 (= E339)
- binding magnesium ion: D211 (= D210), E237 (= E236), E263 (= E262)
Q9AAR4 D-mannonate dehydratase CC0532; ManD; EC 4.2.1.8 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
65% identity, 100% coverage: 1:402/402 of query aligns to 2:403/403 of Q9AAR4
- D211 (= D210) binding
- E237 (= E236) binding
- E263 (= E262) binding
2qjjA Crystal structure of d-mannonate dehydratase from novosphingobium aromaticivorans (see paper)
67% identity, 100% coverage: 1:402/402 of query aligns to 1:402/402 of 2qjjA
- active site: G121 (= G121), R147 (= R147), Q149 (= Q149), Y159 (= Y159), D210 (= D210), H212 (= H212), E236 (= E236), G261 (= G261), E262 (= E262), R283 (= R283), T285 (= T285), H312 (= H312), E339 (= E339), W402 (= W402)
- binding magnesium ion: D210 (= D210), E236 (= E236), E262 (= E262)
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)
67% identity, 100% coverage: 1:402/402 of query aligns to 1:402/402 of A4XF23
- R147 (= R147) mutation to A: Abolishes catalytic activity.; mutation to K: Decreases catalytic activity.
- Y159 (= Y159) mutation to F: Abolishes catalytic activity.
- 161:169 (vs. 161:169, 44% identical) mutation to AGAGGAGAG: Abolishes catalytic activity.
- D210 (= D210) binding
- H212 (= H212) mutation to N: Abolishes catalytic activity.
- E236 (= E236) binding
- E262 (= E262) binding
- K271 (= K271) mutation to E: No effect on catalytic activity.
- R283 (= R283) mutation to A: Abolishes catalytic activity.
- H312 (= H312) mutation to N: Abolishes catalytic activity.
- A314 (≠ P314) mutation to P: Decreases catalytic activity.
- E339 (= E339) mutation to Q: Abolishes catalytic activity.
3p93C Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
67% identity, 100% coverage: 1:402/402 of query aligns to 1:384/384 of 3p93C
- active site: H122 (= H122), R147 (= R147), Q149 (= Q149), D192 (= D210), H194 (= H212), E218 (= E236), G243 (= G261), E244 (= E262), R265 (= R283), P267 (≠ T285), H294 (= H312), G295 (= G313), E321 (= E339), W384 (= W402)
- binding 2-keto-3-deoxygluconate: N37 (= N37), D192 (= D210), H194 (= H212), E244 (= E262), H294 (= H312), P296 (= P314), D298 (= D316), E321 (= E339), W384 (= W402)
- binding magnesium ion: D192 (= D210), E218 (= E236), E244 (= E262)
3p93A Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg,d-mannonate and 2-keto-3-deoxy-d- gluconate
67% identity, 100% coverage: 1:402/402 of query aligns to 1:384/384 of 3p93A
- active site: H122 (= H122), R147 (= R147), Q149 (= Q149), D192 (= D210), H194 (= H212), E218 (= E236), G243 (= G261), E244 (= E262), R265 (= R283), P267 (≠ T285), H294 (= H312), G295 (= G313), E321 (= E339), W384 (= W402)
- binding d-mannonic acid: N37 (= N37), D192 (= D210), H194 (= H212), E244 (= E262), H294 (= H312), P296 (= P314), D298 (= D316), E321 (= E339)
- binding magnesium ion: D192 (= D210), E218 (= E236), E244 (= E262)
Query Sequence
>H281DRAFT_01518 FitnessBrowser__Burk376:H281DRAFT_01518
MKIVRADVIVTCPGRNFVTLKIVTDEGVHGIGDATLNGRELAVASYLKDHVCPLLIGRDP
GRIEDTWQYLYKGAYWRRGPVTMTAIAAVDMALWDILGKVTGMPLYKLLGGASREGVMVY
GHATGRDIPEALDRYAEHIEAGYQAIRIQCGVPNMRSVYGVSKGSGMYEPATKGAVEEQS
WSSEKYLDFVPKLFEAVREKFGFDTHLLHDVHHRLTPIEAARLGKSVEPYRLFWMEDPTP
AENQAGFRLIREHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRATLTHAGGISHLRRIAD
FASLYQVRTGCHGPSDLSPVCMGAALHFDLWVPNFGVQEYMGFPEEALEVFPHAWRFDHG
MMHPGDAPGHGVDIDEAAAARFPYDPAYLPVARLEDGTLWSW
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