SitesBLAST
Comparing Ac3H11_338 FitnessBrowser__acidovorax_3H11:Ac3H11_338 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)
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: 12:454/454 of query aligns to 3:446/446 of P0AES2
- Y150 (= Y159) mutation to F: Reduces activity 100-fold.
- K207 (= K216) active site, Proton acceptor; mutation to Q: Reduces activity 1000-fold.; mutation to R: Reduces activity 10000-fold.
- D235 (= D244) binding
- E266 (= E275) binding
- N289 (= N298) binding
- H339 (= H348) 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 (= N350) 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 (= D375) 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: 12:454/454 of query aligns to 1:444/444 of 1ecqA
- active site: K203 (= K214), K205 (= K216), D233 (= D244), N235 (= N246), E258 (= E269), N287 (= N298), M288 (= M299), D311 (= D322), H337 (= H348), N339 (= N350), I363 (= I374)
- binding 4-deoxyglucarate: N25 (= N36), H30 (= H41), T101 (= T112), Y148 (= Y159), F150 (= F161), K205 (= K216), D233 (= D244), N235 (= N246), N287 (= N298), H337 (= H348), S338 (= S349), N339 (= N350), H366 (= H377), R420 (= R430)
- binding magnesium ion: D233 (= D244), E258 (= E269), N287 (= N298)
1ec9D E. Coli glucarate dehydratase bound to xylarohydroxamate (see paper)
73% identity, 98% coverage: 12:454/454 of query aligns to 1:444/444 of 1ec9D
- active site: K203 (= K214), K205 (= K216), D233 (= D244), N235 (= N246), E258 (= E269), N287 (= N298), M288 (= M299), D311 (= D322), H337 (= H348), N339 (= N350), I363 (= I374)
- binding magnesium ion: D233 (= D244), E258 (= E269), N287 (= N298)
- binding xylarohydroxamate: H30 (= H41), T101 (= T112), Y148 (= Y159), F150 (= F161), K205 (= K216), D233 (= D244), N235 (= N246), N287 (= N298), H337 (= H348), S338 (= S349), N339 (= N350), H366 (= H377), R420 (= R430)
1ec8A E. Coli glucarate dehydratase bound to product 2,3-dihydroxy-5-oxo- hexanedioate (see paper)
73% identity, 97% coverage: 15:454/454 of query aligns to 2:442/442 of 1ec8A
- active site: K201 (= K214), K203 (= K216), D231 (= D244), N233 (= N246), E256 (= E269), N285 (= N298), M286 (= M299), D309 (= D322), H335 (= H348), N337 (= N350), I361 (= I374)
- binding 2,3-dihydroxy-5-oxo-hexanedioate: N23 (= N36), H28 (= H41), T99 (= T112), Y146 (= Y159), K203 (= K216), D231 (= D244), N233 (= N246), N285 (= N298), H335 (= H348), S336 (= S349), N337 (= N350), H364 (= H377), R418 (= R430)
- binding magnesium ion: D231 (= D244), E256 (= E269), N285 (= N298)
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
73% identity, 97% coverage: 15:454/454 of query aligns to 3:443/443 of 1jctA
- active site: K202 (= K214), K204 (= K216), D232 (= D244), N234 (= N246), E257 (= E269), N286 (= N298), M287 (= M299), D310 (= D322), H336 (= H348), L338 (≠ N350), I362 (= I374)
- binding d-glucarate: N24 (= N36), H29 (= H41), T100 (= T112), Y147 (= Y159), F149 (= F161), K204 (= K216), D232 (= D244), N286 (= N298), S337 (= S349), R419 (= R430)
- binding magnesium ion: D232 (= D244), E257 (= E269), N286 (= N298)
3p0wB Crystal structure of d-glucarate dehydratase from ralstonia solanacearum complexed with mg and d-glucarate
64% identity, 96% coverage: 16:452/454 of query aligns to 2:428/428 of 3p0wB
- active site: K189 (= K214), K191 (= K216), D219 (= D244), N221 (= N246), E244 (= E269), N273 (= N298), D297 (= D322), H323 (= H348), N325 (= N350)
- binding d-glucarate: H27 (= H41), Y134 (= Y159), K191 (= K216), D219 (= D244), N221 (= N246), N273 (= N298), H323 (= H348), N325 (= N350), H352 (= H377), R406 (= R430)
- binding magnesium ion: D219 (= D244), E244 (= E269), N273 (= N298)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
63% identity, 96% coverage: 16:450/454 of query aligns to 2:422/425 of 3nxlC
3nfuA Crystal structure of probable glucarate dehydratase from chromohalobacter salexigens dsm 3043 complexed with magnesium
56% identity, 96% coverage: 17:453/454 of query aligns to 3:440/441 of 3nfuA
- active site: K201 (= K214), K203 (= K216), D231 (= D244), N233 (= N246), E256 (= E269), N285 (= N298), D309 (= D322), H335 (= H348), N337 (= N350)
- binding magnesium ion: D231 (= D244), N233 (= N246), E256 (= E269), D257 (= D270), N285 (= N298)
3n6hB Crystal structure of mandelate racemase/muconate lactonizing protein from actinobacillus succinogenes 130z complexed with magnesium/sulfate
58% identity, 97% coverage: 14:454/454 of query aligns to 1:430/432 of 3n6hB
- active site: K189 (= K214), K191 (= K216), D219 (= D244), N221 (= N246), E244 (= E269), N273 (= N298), D297 (= D322), H323 (= H348), N325 (= N350)
- binding magnesium ion: D219 (= D244), E244 (= E269), N273 (= N298)
3pfrA Crystal structure of d-glucarate dehydratase related protein from actinobacillus succinogenes complexed with d-glucarate
58% identity, 97% coverage: 15:454/454 of query aligns to 1:426/426 of 3pfrA
- active site: K185 (= K214), K187 (= K216), D215 (= D244), N217 (= N246), E240 (= E269), N269 (= N298), D293 (= D322), H319 (= H348), N321 (= N350)
- binding d-glucarate: N22 (= N36), H27 (= H41), Y130 (= Y159), F132 (= F161), K187 (= K216), D215 (= D244), N217 (= N246), N269 (= N298), H319 (= H348), S320 (= S349), N321 (= N350), H348 (= H377)
- binding magnesium ion: D215 (= D244), E240 (= E269), N269 (= N298)
4it1D Crystal structure of enolase pfl01_3283 (target efi-502286) from pseudomonas fluorescens pf0-1 with bound magnesium, potassium and tartrate
36% identity, 94% coverage: 19:444/454 of query aligns to 6:421/427 of 4it1D
- active site: S51 (≠ V64), D54 (≠ G67), A98 (≠ L110), Y150 (= Y159), K194 (= K214), K196 (= K216), D224 (= D244), N226 (= N246), Y247 (= Y267), E249 (= E269), T271 (= T297), N272 (= N298), M273 (= M299), D296 (= D322), H323 (= H348), S324 (= S349), N325 (= N350), C349 (≠ I374), D350 (= D375)
- binding magnesium ion: D224 (= D244), E249 (= E269), N272 (= N298)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
34% identity, 97% coverage: 12:450/454 of query aligns to 6:425/427 of 3va8A
3vc6A Crystal structure of enolase tbis_1083(target efi-502310) from thermobispora bispora dsm 43833 complexed with magnesium and formate
33% identity, 94% coverage: 18:444/454 of query aligns to 3:414/420 of 3vc6A
- active site: D52 (≠ G67), H55 (≠ I70), Y146 (= Y159), K188 (= K214), K190 (= K216), D218 (= D244), N220 (= N246), E243 (= E269), N266 (= N298), M267 (= M299), D290 (= D322), H317 (= H348), S318 (= S349), N319 (= N350), H321 (= H352), C343 (≠ I374), D344 (= D375)
- binding magnesium ion: D218 (= D244), E243 (= E269), N266 (= N298)
3dg6A Crystal structure of muconate lactonizing enzyme from mucobacterium smegmatis complexed with muconolactone (see paper)
26% identity, 65% coverage: 121:415/454 of query aligns to 98:360/366 of 3dg6A
- active site: M134 (= M156), K160 (= K214), K162 (= K216), D191 (= D244), N193 (= N246), E217 (= E269), D242 (≠ A290), E243 (≠ T291), S244 (≠ G292), K266 (≠ P319), G292 (= G346), N293 (≠ S347), Q294 (≠ H348), G319 (≠ A373), E320 (≠ I374), L321 (≠ D375)
- binding magnesium ion: D191 (= D244), E217 (= E269), D242 (≠ A290)
- binding [(2S)-5-oxo-2,5-dihydrofuran-2-yl]acetic acid: M134 (= M156), K160 (= K214), K162 (= K216), D191 (= D244), N193 (= N246), D242 (≠ A290), K266 (≠ P319), N293 (≠ S347), Q294 (≠ H348), I295 (≠ S349)
Sites not aligning to the query:
4j1oA Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l- proline betaine (substrate) (see paper)
27% identity, 72% coverage: 84:411/454 of query aligns to 50:357/369 of 4j1oA
- active site: A137 (≠ R174), Q162 (≠ K214), K164 (= K216), D194 (= D244), N196 (= N246), V217 (≠ Y267), E219 (= E269), D242 (vs. gap), E243 (vs. gap), K266 (≠ V300), D293 (≠ T327), D294 (≠ M328), A295 (= A329), E318 (≠ D375), G319 (≠ T376), V320 (≠ H377), W321 (= W378)
- binding magnesium ion: D194 (= D244), E219 (= E269), D242 (vs. gap)
- binding 1,1-dimethyl-prolinium: Y56 (≠ N90), Q162 (≠ K214), K164 (= K216), D194 (= D244), D242 (vs. gap), K266 (≠ V300)
Sites not aligning to the query:
4izgA Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound cis-4oh-d-proline betaine (product) (see paper)
27% identity, 72% coverage: 84:411/454 of query aligns to 50:357/369 of 4izgA
- active site: A137 (≠ R174), Q162 (≠ K214), K164 (= K216), D194 (= D244), N196 (= N246), V217 (≠ Y267), E219 (= E269), D242 (vs. gap), E243 (vs. gap), K266 (≠ V300), D293 (≠ T327), D294 (≠ M328), A295 (= A329), E318 (≠ D375), G319 (≠ T376), V320 (≠ H377), W321 (= W378)
- binding (2S,4S)-2-carboxy-4-hydroxy-1,1-dimethylpyrrolidinium: Y56 (≠ N90), Q162 (≠ K214), K164 (= K216), D194 (= D244), D242 (vs. gap), K266 (≠ V300), A295 (= A329)
- binding magnesium ion: D194 (= D244), E219 (= E269), D242 (vs. gap)
Sites not aligning to the query:
2ps2A Crystal structure of putative mandelate racemase/muconate lactonizing enzyme from aspergillus oryzae
25% identity, 67% coverage: 121:422/454 of query aligns to 95:361/361 of 2ps2A
- active site: S132 (≠ Y159), Q156 (≠ A211), S157 (≠ D212), V158 (≠ F213), K159 (= K214), D187 (= D244), E213 (= E269), D236 (≠ N298), E237 (≠ M299), K260 (≠ P319), Q287 (≠ H348), E288 (≠ S349), T289 (≠ N350), C313 (≠ W378), I314 (= I379), L315 (≠ W380)
- binding magnesium ion: D187 (= D244), E213 (= E269), D236 (≠ N298)
Sites not aligning to the query:
2gghC The mutant a68c-d72c-nlq of deinococcus radiodurans nacylamino acid racemase (see paper)
27% identity, 71% coverage: 100:420/454 of query aligns to 82:369/370 of 2gghC
- active site: Y95 (≠ F113), S137 (≠ D170), K163 (≠ D212), K165 (= K214), R186 (= R240), T188 (= T242), D190 (= D244), N192 (= N246), E215 (= E269), D240 (≠ P294), E241 (≠ T295), S242 (≠ A296), K264 (≠ A321), C290 (vs. gap), G291 (vs. gap), G292 (vs. gap), M293 (vs. gap), G316 (= G369), D317 (≠ R370), T318 (≠ V371)
- binding magnesium ion: D190 (= D244), E215 (= E269)
- binding n~2~-acetyl-l-glutamine: G292 (vs. gap), M293 (vs. gap), L294 (vs. gap)
Sites not aligning to the query:
Q9RYA6 N-succinylamino acid racemase; NSAAR; NSAR; N-acylamino acid racemase; NAAAR; o-succinylbenzoate synthase; OSB synthase; OSBS; EC 5.1.1.-; EC 5.1.1.-; EC 4.2.1.113 from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) (see 2 papers)
26% identity, 71% coverage: 100:420/454 of query aligns to 87:374/375 of Q9RYA6
- Y100 (≠ F113) mutation to C: Loss of activity; when associated with C-60.
- R120 (≠ Q135) mutation to C: Loss of activity; when associated with C-48.
- G127 (≠ A142) mutation to C: Retains 93% of wild-type activity; when associated with C-313.
- S142 (≠ G158) binding
- E149 (≠ D165) mutation to C: Retains 88% of wild-type activity; when associated with C-182.
- G163 (≠ A204) mutation to C: Loss of activity; when associated with C-343.
- KLK 168:170 (≠ DFK 212:214) binding
- A182 (= A231) mutation to C: Retains 88% of wild-type activity; when associated with C-149.
- D195 (= D244) binding
- Y218 (= Y267) mutation to C: Retains 35% of wild-type activity.
- E220 (= E269) binding
- D245 (≠ N298) binding
- V265 (vs. gap) mutation to C: Retains 39% of wild-type activity.
- K269 (≠ A321) binding
- L299 (vs. gap) binding
- T313 (≠ S356) mutation to C: Retains 93% of wild-type activity; when associated with C-127.
- D343 (≠ N395) mutation to C: Loss of activity; when associated with C-163.
Sites not aligning to the query:
- 48 V→C: Loss of activity; when associated with C-120.
- 56 M→C: Loss of activity; when associated with C-65.
- 60 P→C: Loss of activity; when associated with C-100.
- 65 E→C: Loss of activity; when associated with C-56.
- 68 A→C: No change in activity; when associated with C-72.
- 72 D→C: No change in activity; when associated with C-68.
4hpnA Crystal structure of a proposed galactarolactone cycloisomerase from agrobacterium tumefaciens, target efi-500704, with bound ca, ordered loops (see paper)
25% identity, 69% coverage: 103:413/454 of query aligns to 86:368/378 of 4hpnA
- active site: T134 (= T175), K164 (= K214), K166 (= K216), D194 (= D244), N196 (= N246), E220 (= E269), G245 (≠ N298), E246 (≠ M299), T247 (≠ V300), Q267 (≠ D322), D269 (≠ H324), H296 (vs. gap), V297 (≠ T344), W298 (= W345), R320 (= R370), E329 (vs. gap), F330 (vs. gap), H334 (= H377)
- binding calcium ion: D194 (= D244), D209 (≠ R259), E220 (= E269), G237 (≠ A290), E246 (≠ M299)
Sites not aligning to the query:
Query Sequence
>Ac3H11_338 FitnessBrowser__acidovorax_3H11:Ac3H11_338
LLLPTMTTSTPSTSSTPVITELRVVPVAGHDSMLMNLSGAHGPFFTRNLIILRDSAGHTG
VGEVPGGEKIRQTIEDARALIVGCPIGHHNAVLNAMRAQFADRDAGGRGLQTFDLRITIH
AVTAVESAFLDLLGQHLGVPVAALLGEGVQRESVQMLGYLFYVGDRAKTDLAYRTEPGAD
NDWFRLRNEKAMTAEGIVRLAEAAYERYGFADFKLKGGVLRGEEEVEAIRALHQRFPEAR
VTLDPNGGWLLKDAIRITRDLHGVMAYAEDPCGAEGVFSGREVMAEFRRATGLPTATNMV
ATDWREMAHSLALQSVDIPLADPHFWTMAGSVRVAQMCQAFGLTWGSHSNNHFDVSLAMF
THVGAAAPGRVTAIDTHWIWQDGERLTKEPFQIKNGFIDLPKKPGLGVELDMDEVERAHR
LYLQHGLGARDDAIAMQYLIPGWKFNNKSPCMVR
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