SitesBLAST
Comparing GFF375 FitnessBrowser__psRCH2:GFF375 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)
P0AES2 Glucarate dehydratase; GDH; GlucD; D-glucarate dehydratase; EC 4.2.1.40 from Escherichia coli (strain K12) (see 3 papers)
73% identity, 98% coverage: 8:446/446 of query aligns to 7:446/446 of P0AES2
- Y150 (= Y151) mutation to F: Reduces activity 100-fold.
- K207 (= K208) active site, Proton acceptor; mutation to Q: Reduces activity 1000-fold.; mutation to R: Reduces activity 10000-fold.
- D235 (= D236) binding
- E266 (= E267) binding
- N289 (= N290) binding
- H339 (= H340) active site, Proton acceptor; mutation to A: Loss of activity.; mutation to N: Reduces activity 10000-fold.; mutation to Q: Reduces activity 1000-fold.
- N341 (= N342) mutation to D: Inactive in the dehydration reaction of D-glucarate, L-idarate, and 4F-Gluc.; mutation to L: Almost no effect on the dehydration reaction of D-glucarate, L-idarate, and 4F-Gluc.
- D366 (= D367) mutation D->A,N: Reduces activity over 100-fold.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ecqA E. Coli glucarate dehydratase bound to 4-deoxyglucarate (see paper)
73% identity, 98% coverage: 8:446/446 of query aligns to 5:444/444 of 1ecqA
- active site: K203 (= K206), K205 (= K208), D233 (= D236), N235 (= N238), E258 (= E261), N287 (= N290), M288 (= M291), D311 (= D314), H337 (= H340), N339 (= N342), I363 (= I366)
- binding 4-deoxyglucarate: N25 (= N28), H30 (= H33), T101 (= T104), Y148 (= Y151), F150 (= F153), K205 (= K208), D233 (= D236), N235 (= N238), N287 (= N290), H337 (= H340), S338 (= S341), N339 (= N342), H366 (= H369), R420 (= R422)
- binding magnesium ion: D233 (= D236), E258 (= E261), N287 (= N290)
1ec9D E. Coli glucarate dehydratase bound to xylarohydroxamate (see paper)
73% identity, 98% coverage: 8:446/446 of query aligns to 5:444/444 of 1ec9D
- active site: K203 (= K206), K205 (= K208), D233 (= D236), N235 (= N238), E258 (= E261), N287 (= N290), M288 (= M291), D311 (= D314), H337 (= H340), N339 (= N342), I363 (= I366)
- binding magnesium ion: D233 (= D236), E258 (= E261), N287 (= N290)
- binding xylarohydroxamate: H30 (= H33), T101 (= T104), Y148 (= Y151), F150 (= F153), K205 (= K208), D233 (= D236), N235 (= N238), N287 (= N290), H337 (= H340), S338 (= S341), N339 (= N342), H366 (= H369), R420 (= R422)
1ec8A E. Coli glucarate dehydratase bound to product 2,3-dihydroxy-5-oxo- hexanedioate (see paper)
73% identity, 98% coverage: 8:446/446 of query aligns to 3:442/442 of 1ec8A
- active site: K201 (= K206), K203 (= K208), D231 (= D236), N233 (= N238), E256 (= E261), N285 (= N290), M286 (= M291), D309 (= D314), H335 (= H340), N337 (= N342), I361 (= I366)
- binding 2,3-dihydroxy-5-oxo-hexanedioate: N23 (= N28), H28 (= H33), T99 (= T104), Y146 (= Y151), K203 (= K208), D231 (= D236), N233 (= N238), N285 (= N290), H335 (= H340), S336 (= S341), N337 (= N342), H364 (= H369), R418 (= R422)
- binding magnesium ion: D231 (= D236), E256 (= E261), N285 (= N290)
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
73% identity, 98% coverage: 8:446/446 of query aligns to 4:443/443 of 1jctA
- active site: K202 (= K206), K204 (= K208), D232 (= D236), N234 (= N238), E257 (= E261), N286 (= N290), M287 (= M291), D310 (= D314), H336 (= H340), L338 (≠ N342), I362 (= I366)
- binding d-glucarate: N24 (= N28), H29 (= H33), T100 (= T104), Y147 (= Y151), F149 (= F153), K204 (= K208), D232 (= D236), N286 (= N290), S337 (= S341), R419 (= R422)
- binding magnesium ion: D232 (= D236), E257 (= E261), N286 (= N290)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
68% identity, 98% coverage: 7:444/446 of query aligns to 1:424/425 of 3nxlC
3p0wB Crystal structure of d-glucarate dehydratase from ralstonia solanacearum complexed with mg and d-glucarate
67% identity, 98% coverage: 8:444/446 of query aligns to 2:428/428 of 3p0wB
- active site: K189 (= K206), K191 (= K208), D219 (= D236), N221 (= N238), E244 (= E261), N273 (= N290), D297 (= D314), H323 (= H340), N325 (= N342)
- binding d-glucarate: H27 (= H33), Y134 (= Y151), K191 (= K208), D219 (= D236), N221 (= N238), N273 (= N290), H323 (= H340), N325 (= N342), H352 (= H369), R406 (= R422)
- binding magnesium ion: D219 (= D236), E244 (= E261), N273 (= N290)
3nfuA Crystal structure of probable glucarate dehydratase from chromohalobacter salexigens dsm 3043 complexed with magnesium
60% identity, 98% coverage: 9:445/446 of query aligns to 3:440/441 of 3nfuA
- active site: K201 (= K206), K203 (= K208), D231 (= D236), N233 (= N238), E256 (= E261), N285 (= N290), D309 (= D314), H335 (= H340), N337 (= N342)
- binding magnesium ion: D231 (= D236), N233 (= N238), E256 (= E261), D257 (= D262), N285 (= N290)
3n6hB Crystal structure of mandelate racemase/muconate lactonizing protein from actinobacillus succinogenes 130z complexed with magnesium/sulfate
57% identity, 98% coverage: 8:446/446 of query aligns to 3:430/432 of 3n6hB
- active site: K189 (= K206), K191 (= K208), D219 (= D236), N221 (= N238), E244 (= E261), N273 (= N290), D297 (= D314), H323 (= H340), N325 (= N342)
- binding magnesium ion: D219 (= D236), E244 (= E261), N273 (= N290)
3pfrA Crystal structure of d-glucarate dehydratase related protein from actinobacillus succinogenes complexed with d-glucarate
57% identity, 98% coverage: 8:446/446 of query aligns to 2:426/426 of 3pfrA
- active site: K185 (= K206), K187 (= K208), D215 (= D236), N217 (= N238), E240 (= E261), N269 (= N290), D293 (= D314), H319 (= H340), N321 (= N342)
- binding d-glucarate: N22 (= N28), H27 (= H33), Y130 (= Y151), F132 (= F153), K187 (= K208), D215 (= D236), N217 (= N238), N269 (= N290), H319 (= H340), S320 (= S341), N321 (= N342), H348 (= H369)
- binding magnesium ion: D215 (= D236), E240 (= E261), N269 (= N290)
4it1D Crystal structure of enolase pfl01_3283 (target efi-502286) from pseudomonas fluorescens pf0-1 with bound magnesium, potassium and tartrate
38% identity, 96% coverage: 10:435/446 of query aligns to 5:420/427 of 4it1D
- active site: S51 (≠ V56), D54 (≠ G59), A98 (≠ R100), Y150 (= Y151), K194 (= K206), K196 (= K208), D224 (= D236), N226 (= N238), Y247 (= Y259), E249 (= E261), T271 (= T289), N272 (= N290), M273 (= M291), D296 (= D314), H323 (= H340), S324 (= S341), N325 (= N342), C349 (≠ I366), D350 (= D367)
- binding magnesium ion: D224 (= D236), E249 (= E261), N272 (= N290)
3vc6A Crystal structure of enolase tbis_1083(target efi-502310) from thermobispora bispora dsm 43833 complexed with magnesium and formate
37% identity, 96% coverage: 11:436/446 of query aligns to 4:414/420 of 3vc6A
- active site: D52 (≠ G59), H55 (≠ I62), Y146 (= Y151), K188 (= K206), K190 (= K208), D218 (= D236), N220 (= N238), E243 (= E261), N266 (= N290), M267 (= M291), D290 (= D314), H317 (= H340), S318 (= S341), N319 (= N342), H321 (= H344), C343 (≠ I366), D344 (= D367)
- binding magnesium ion: D218 (= D236), E243 (= E261), N266 (= N290)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
35% identity, 97% coverage: 11:442/446 of query aligns to 13:425/427 of 3va8A
3dg6A Crystal structure of muconate lactonizing enzyme from mucobacterium smegmatis complexed with muconolactone (see paper)
27% identity, 68% coverage: 113:415/446 of query aligns to 98:364/366 of 3dg6A
- active site: M134 (= M148), K160 (= K206), K162 (= K208), D191 (= D236), N193 (= N238), E217 (= E261), D242 (≠ A282), E243 (≠ T283), S244 (≠ G284), K266 (≠ P311), G292 (= G338), N293 (≠ S339), Q294 (≠ H340), G319 (≠ A365), E320 (≠ I366), L321 (≠ D367)
- binding magnesium ion: D191 (= D236), E217 (= E261), D242 (≠ A282)
- binding [(2S)-5-oxo-2,5-dihydrofuran-2-yl]acetic acid: M134 (= M148), K160 (= K206), K162 (= K208), D191 (= D236), N193 (= N238), D242 (≠ A282), K266 (≠ P311), N293 (≠ S339), Q294 (≠ H340), I295 (≠ S341)
Sites not aligning to the query:
3i6eA Crystal structure of muconate lactonizing enzyme from ruegeria pomeroyi.
27% identity, 76% coverage: 70:409/446 of query aligns to 59:351/356 of 3i6eA
- active site: S124 (≠ Y151), K149 (= K206), K151 (= K208), D179 (= D236), Y180 (≠ P237), N181 (= N238), Q182 (≠ G239), E205 (= E261), D230 (≠ N290), E231 (≠ M291), S232 (≠ I292), K254 (≠ P311), Y279 (≠ H340), G281 (≠ N342), D282 (≠ N343), M283 (≠ H344), C307 (≠ I366), E308 (≠ D367), F309 (≠ T368)
- binding magnesium ion: D179 (= D236), E205 (= E261), D230 (≠ N290)
5olcC Crystal structure of the 3,6-anhydro-d-galactonate cycloisomerase from zobellia galactanivorans (see paper)
26% identity, 85% coverage: 38:417/446 of query aligns to 18:351/351 of 5olcC
- active site: K148 (= K206), K150 (= K208), D178 (= D236), N180 (= N238), E204 (= E261), G229 (≠ N290), E230 (≠ M291), D253 (≠ H316), H280 (vs. gap), E304 (≠ A365), E309 (≠ H369)
- binding magnesium ion: D178 (= D236), E204 (= E261), E230 (≠ M291)
2ps2A Crystal structure of putative mandelate racemase/muconate lactonizing enzyme from aspergillus oryzae
25% identity, 68% coverage: 113:414/446 of query aligns to 95:361/361 of 2ps2A
- active site: S132 (≠ Y151), Q156 (≠ F205), S157 (≠ K206), V158 (≠ L207), K159 (= K208), D187 (= D236), E213 (= E261), D236 (≠ N290), E237 (≠ M291), K260 (≠ A313), Q287 (≠ H340), E288 (≠ S341), T289 (≠ N342), C313 (≠ W370), I314 (= I371), L315 (≠ W372)
- binding magnesium ion: D187 (= D236), E213 (= E261), D236 (≠ N290)
Sites not aligning to the query:
3i6tB Crystal structure of muconate cycloisomerase from jannaschia sp.
26% identity, 83% coverage: 41:409/446 of query aligns to 34:361/364 of 3i6tB
- active site: S136 (≠ Y151), K161 (≠ R191), K163 (≠ R199), D191 (= D236), N193 (= N238), E217 (= E261), D242 (≠ T289), E243 (≠ N290), S262 (≠ D309), K264 (≠ P311), G291 (≠ N342), D292 (≠ N343), M293 (≠ H344), C317 (≠ I366), E318 (≠ D367), F319 (vs. gap)
- binding magnesium ion: D191 (= D236), E217 (= E261), D242 (≠ T289)
Sites not aligning to the query:
2gghC The mutant a68c-d72c-nlq of deinococcus radiodurans nacylamino acid racemase (see paper)
26% identity, 65% coverage: 117:407/446 of query aligns to 105:358/370 of 2gghC
- active site: S137 (vs. gap), K163 (≠ D204), K165 (= K206), R186 (= R232), T188 (= T234), D190 (= D236), N192 (= N238), E215 (= E261), D240 (≠ P286), E241 (≠ T287), S242 (≠ A288), K264 (≠ P311), C290 (≠ S339), G291 (≠ H340), G292 (≠ S341), M293 (≠ N342), G316 (= G361), D317 (≠ R362), T318 (≠ V363)
- binding magnesium ion: D190 (= D236), E215 (= E261)
- binding n~2~-acetyl-l-glutamine: G292 (≠ S341), M293 (≠ N342), L294 (≠ N343)
Sites not aligning to the query:
3ozmA Crystal structure of enolase superfamily member from bordetella bronchiseptica complexed with mg, m-xylarate and l-lyxarate
24% identity, 92% coverage: 10:421/446 of query aligns to 3:382/386 of 3ozmA
- active site: M20 (= M27), G53 (= G58), D56 (vs. gap), S143 (≠ D162), K170 (= K206), K172 (= K208), D200 (= D236), N202 (= N238), E226 (= E261), G252 (= G284), E253 (≠ L285), N254 (≠ P286), Q274 (≠ L312), D276 (= D314), H303 (= H340), T304 (≠ S341), F305 (≠ N342), E328 (vs. gap), I331 (≠ V363), H333 (≠ A365)
- binding D-xylaric acid: S24 (≠ G31), K29 (≠ W36), Y146 (= Y165), K170 (= K206), K172 (= K208), D200 (= D236), N202 (= N238), E253 (≠ L285), H303 (= H340), F305 (≠ N342), E328 (vs. gap)
- binding magnesium ion: D200 (= D236), E226 (= E261), E253 (≠ L285)
Query Sequence
>GFF375 FitnessBrowser__psRCH2:GFF375
MTIAATGTPRITELTVVPVAGQDSMLMNLSGAHGPWFTRNILILKDSAGHVGVGEVPGGE
AIRQTLEDARVLLVGEPIGQYNALLNRARRAFADRDSGGRGLQTFDLRIAIHAVTALESA
LLDLLGQHLEVPVAALLGDGQQRDEVEMLGYLFFIGDRNKTDFGYRDESGADDAWFRLRN
EEAMTPESIVRQAEAAYERYGFKDFKLKGGVLRGEEEVEAIRALAARFPDARVTLDPNGA
WSLDEAIGLCRDLHGVLAYAEDPCGAENGYSGREVMAEFRRATGLPTATNMIATDWRQMS
HTVQLNSVDIPLADPHFWTMAGSVRVAQMCADFGLTWGSHSNNHFDISLAMFTHVAAAAP
GRVTAIDTHWIWQDGQHLTLEPLKIVGGKVAVPQKPGLGVELDWDALQQAHAHYQEKGLG
ARDDAIAMQYLIPDWTFNNKKPCMVR
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