SitesBLAST
Comparing Pf1N1B4_5057 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5057 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)
4it1D Crystal structure of enolase pfl01_3283 (target efi-502286) from pseudomonas fluorescens pf0-1 with bound magnesium, potassium and tartrate
93% identity, 100% coverage: 1:424/424 of query aligns to 4:427/427 of 4it1D
- active site: S51 (= S48), D54 (= D51), A98 (= A95), Y150 (= Y147), K194 (= K191), K196 (= K193), D224 (= D221), N226 (= N223), Y247 (= Y244), E249 (= E246), T271 (= T268), N272 (= N269), M273 (= M270), D296 (= D293), H323 (= H320), S324 (= S321), N325 (= N322), C349 (= C346), D350 (= D347)
- binding magnesium ion: D224 (= D221), E249 (= E246), N272 (= N269)
3vc6A Crystal structure of enolase tbis_1083(target efi-502310) from thermobispora bispora dsm 43833 complexed with magnesium and formate
50% identity, 99% coverage: 1:419/424 of query aligns to 2:415/420 of 3vc6A
- active site: D52 (= D51), H55 (≠ A54), Y146 (= Y147), K188 (= K191), K190 (= K193), D218 (= D221), N220 (= N223), E243 (= E246), N266 (= N269), M267 (= M270), D290 (= D293), H317 (= H320), S318 (= S321), N319 (= N322), H321 (= H324), C343 (= C346), D344 (= D347)
- binding magnesium ion: D218 (= D221), E243 (= E246), N266 (= N269)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
50% identity, 100% coverage: 3:424/424 of query aligns to 13:427/427 of 3va8A
3nfuA Crystal structure of probable glucarate dehydratase from chromohalobacter salexigens dsm 3043 complexed with magnesium
36% identity, 98% coverage: 2:418/424 of query aligns to 4:431/441 of 3nfuA
- active site: K201 (= K191), K203 (= K193), D231 (= D221), N233 (= N223), E256 (= E246), N285 (= N269), D309 (= D293), H335 (= H320), N337 (= N322)
- binding magnesium ion: D231 (= D221), N233 (= N223), E256 (= E246), D257 (= D247), N285 (= N269)
P0AES2 Glucarate dehydratase; GDH; GlucD; D-glucarate dehydratase; EC 4.2.1.40 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 98% coverage: 3:417/424 of query aligns to 10:435/446 of P0AES2
- Y150 (= Y147) mutation to F: Reduces activity 100-fold.
- K207 (= K193) active site, Proton acceptor; mutation to Q: Reduces activity 1000-fold.; mutation to R: Reduces activity 10000-fold.
- D235 (= D221) binding
- E266 (vs. gap) binding
- N289 (= N269) binding
- H339 (= H320) 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 (= N322) 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 (= D347) 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)
35% identity, 98% coverage: 3:417/424 of query aligns to 8:433/444 of 1ecqA
- active site: K203 (= K191), K205 (= K193), D233 (= D221), N235 (= N223), E258 (= E246), N287 (= N269), M288 (= M270), D311 (= D293), H337 (= H320), N339 (= N322), I363 (≠ C346)
- binding 4-deoxyglucarate: N25 (= N20), H30 (= H25), T101 (≠ S101), Y148 (= Y147), F150 (= F149), K205 (= K193), D233 (= D221), N235 (= N223), N287 (= N269), H337 (= H320), S338 (= S321), N339 (= N322), H366 (= H349), R420 (= R404)
- binding magnesium ion: D233 (= D221), E258 (= E246), N287 (= N269)
1ec9D E. Coli glucarate dehydratase bound to xylarohydroxamate (see paper)
35% identity, 98% coverage: 3:417/424 of query aligns to 8:433/444 of 1ec9D
- active site: K203 (= K191), K205 (= K193), D233 (= D221), N235 (= N223), E258 (= E246), N287 (= N269), M288 (= M270), D311 (= D293), H337 (= H320), N339 (= N322), I363 (≠ C346)
- binding magnesium ion: D233 (= D221), E258 (= E246), N287 (= N269)
- binding xylarohydroxamate: H30 (= H25), T101 (≠ S101), Y148 (= Y147), F150 (= F149), K205 (= K193), D233 (= D221), N235 (= N223), N287 (= N269), H337 (= H320), S338 (= S321), N339 (= N322), H366 (= H349), R420 (= R404)
1ec8A E. Coli glucarate dehydratase bound to product 2,3-dihydroxy-5-oxo- hexanedioate (see paper)
35% identity, 98% coverage: 3:417/424 of query aligns to 6:431/442 of 1ec8A
- active site: K201 (= K191), K203 (= K193), D231 (= D221), N233 (= N223), E256 (= E246), N285 (= N269), M286 (= M270), D309 (= D293), H335 (= H320), N337 (= N322), I361 (≠ C346)
- binding 2,3-dihydroxy-5-oxo-hexanedioate: N23 (= N20), H28 (= H25), T99 (≠ S101), Y146 (= Y147), K203 (= K193), D231 (= D221), N233 (= N223), N285 (= N269), H335 (= H320), S336 (= S321), N337 (= N322), H364 (= H349), R418 (= R404)
- binding magnesium ion: D231 (= D221), E256 (= E246), N285 (= N269)
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
35% identity, 98% coverage: 3:417/424 of query aligns to 7:432/443 of 1jctA
- active site: K202 (= K191), K204 (= K193), D232 (= D221), N234 (= N223), E257 (= E246), N286 (= N269), M287 (= M270), D310 (= D293), H336 (= H320), L338 (≠ N322), I362 (≠ C346)
- binding d-glucarate: N24 (= N20), H29 (= H25), T100 (≠ S101), Y147 (= Y147), F149 (= F149), K204 (= K193), D232 (= D221), N286 (= N269), S337 (= S321), R419 (= R404)
- binding magnesium ion: D232 (= D221), E257 (= E246), N286 (= N269)
3pfrA Crystal structure of d-glucarate dehydratase related protein from actinobacillus succinogenes complexed with d-glucarate
34% identity, 99% coverage: 3:423/424 of query aligns to 5:421/426 of 3pfrA
- active site: K185 (= K191), K187 (= K193), D215 (= D221), N217 (= N223), E240 (= E246), N269 (= N269), D293 (= D293), H319 (= H320), N321 (= N322)
- binding d-glucarate: N22 (= N20), H27 (= H25), Y130 (= Y147), F132 (= F149), K187 (= K193), D215 (= D221), N217 (= N223), N269 (= N269), H319 (= H320), S320 (= S321), N321 (= N322), H348 (= H349)
- binding magnesium ion: D215 (= D221), E240 (= E246), N269 (= N269)
3n6hB Crystal structure of mandelate racemase/muconate lactonizing protein from actinobacillus succinogenes 130z complexed with magnesium/sulfate
35% identity, 99% coverage: 3:423/424 of query aligns to 6:425/432 of 3n6hB
- active site: K189 (= K191), K191 (= K193), D219 (= D221), N221 (= N223), E244 (= E246), N273 (= N269), D297 (= D293), H323 (= H320), N325 (= N322)
- binding magnesium ion: D219 (= D221), E244 (= E246), N273 (= N269)
3p0wB Crystal structure of d-glucarate dehydratase from ralstonia solanacearum complexed with mg and d-glucarate
34% identity, 100% coverage: 2:423/424 of query aligns to 4:424/428 of 3p0wB
- active site: K189 (= K191), K191 (= K193), D219 (= D221), N221 (= N223), E244 (= E246), N273 (= N269), D297 (= D293), H323 (= H320), N325 (= N322)
- binding d-glucarate: H27 (= H25), Y134 (= Y147), K191 (= K193), D219 (= D221), N221 (= N223), N273 (= N269), H323 (= H320), N325 (= N322), H352 (= H349), R406 (= R404)
- binding magnesium ion: D219 (= D221), E244 (= E246), N273 (= N269)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
34% identity, 100% coverage: 2:423/424 of query aligns to 4:420/425 of 3nxlC
2qq6B Crystal structure of mandelate racemase/muconate lactonizing enzyme- like protein from rubrobacter xylanophilus dsm 9941
32% identity, 81% coverage: 44:387/424 of query aligns to 31:381/396 of 2qq6B
- active site: P37 (≠ G50), G79 (= G91), D124 (vs. gap), K166 (= K191), D168 (≠ K193), D213 (= D221), H215 (≠ N223), E239 (= E246), G264 (≠ T268), E265 (≠ N269), M286 (≠ L291), D288 (= D293), H315 (= H320), N316 (≠ S321), E340 (≠ T348), D345 (≠ Q353)
- binding magnesium ion: D213 (= D221), E239 (= E246), E265 (≠ N269), H315 (= H320)
3i4kA Crystal structure of muconate lactonizing enzyme from corynebacterium glutamicum
27% identity, 66% coverage: 110:389/424 of query aligns to 102:365/370 of 3i4kA
- active site: A139 (≠ Y147), K165 (= K191), K167 (= K193), D196 (= D221), N198 (= N223), E222 (= E246), D247 (≠ N269), E248 (≠ M270), S249 (≠ V271), A269 (≠ L291), K271 (≠ D293), T272 (≠ H294), A298 (≠ H320), T299 (≠ S321), S300 (≠ N322), T324 (≠ C346), E325 (≠ D347), L326 (≠ T348)
- binding magnesium ion: D196 (= D221), E222 (= E246), D247 (≠ N269)
Sites not aligning to the query:
1nu5A Crystal structure of pseudomonas sp. P51 chloromuconate lactonizing enzyme (see paper)
25% identity, 81% coverage: 46:389/424 of query aligns to 56:363/369 of 1nu5A
- active site: T137 (≠ Y147), K163 (= K191), K165 (= K193), E176 (≠ S204), D194 (= D221), N196 (= N223), E220 (= E246), D245 (≠ N269), E246 (≠ M270), S247 (≠ V271), K269 (≠ V290), G296 (≠ H320), T297 (≠ S321), M298 (≠ N322), C322 (= C346), E323 (≠ D347), L324 (≠ T348)
- binding manganese (ii) ion: D194 (= D221), E220 (= E246), T235 (≠ H259), N238 (≠ T262), D245 (≠ N269)
Sites not aligning to the query:
3ck5A Crystal structure of a racemase from streptomyces coelicolor a3(2) with bound magnesium
27% identity, 85% coverage: 34:392/424 of query aligns to 34:355/357 of 3ck5A
- active site: T50 (vs. gap), G137 (≠ Q154), K164 (= K191), K166 (= K193), D195 (= D221), N197 (= N223), I220 (≠ Y245), E221 (= E246), I243 (≠ L266), G246 (≠ N269), E247 (≠ M270), E268 (≠ L291), D270 (= D293), H297 (= H320), G298 (≠ S321), V299 (≠ N322), Y315 (= Y344), E317 (vs. gap)
- binding magnesium ion: D195 (= D221), E221 (= E246), E247 (≠ M270)
Sites not aligning to the query:
Q9RKF7 3,6-anhydro-alpha-L-galactonate cycloisomerase; AHGA cycloisomerase; EC 5.5.1.25 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
27% identity, 85% coverage: 34:392/424 of query aligns to 34:358/361 of Q9RKF7
- D195 (= D221) binding
- E221 (= E246) binding
- E247 (≠ M270) binding
1f9cA Crystal structure of mle d178n variant (see paper)
25% identity, 68% coverage: 104:392/424 of query aligns to 86:358/360 of 1f9cA
- active site: T129 (≠ Y147), K155 (= K191), K157 (= K193), D186 (= D221), N188 (= N223), E212 (= E246), D237 (≠ N269), E238 (≠ M270), S239 (≠ V271), K261 (≠ D293), G288 (≠ H320), T289 (≠ S321), M290 (≠ N322), T314 (≠ C346), E315 (≠ D347), L316 (≠ T348)
- binding manganese (ii) ion: D186 (= D221), E212 (= E246), D237 (≠ N269)
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)
27% identity, 67% coverage: 110:394/424 of query aligns to 106:368/375 of Q9RYA6
- R120 (≠ H124) mutation to C: Loss of activity; when associated with C-48.
- G127 (≠ V131) mutation to C: Retains 93% of wild-type activity; when associated with C-313.
- S142 (= S164) binding
- E149 (= E171) mutation to C: Retains 88% of wild-type activity; when associated with C-182.
- G163 (= G186) mutation to C: Loss of activity; when associated with C-343.
- KLK 168:170 (= KLK 191:193) binding
- A182 (= A208) mutation to C: Retains 88% of wild-type activity; when associated with C-149.
- D195 (= D221) binding
- Y218 (= Y244) mutation to C: Retains 35% of wild-type activity.
- E220 (= E246) binding
- D245 (≠ N269) binding
- V265 (≠ I289) mutation to C: Retains 39% of wild-type activity.
- K269 (≠ D293) binding
- L299 (≠ S323) binding
- T313 (≠ S338) mutation to C: Retains 93% of wild-type activity; when associated with C-127.
- D343 (= D369) 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.
- 100 Y→C: Loss of activity; when associated with C-60.
Query Sequence
>Pf1N1B4_5057 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5057
LKIKRVTVTPIAFRDPPLLNASGIHEPFALRSIIEIESDNGYIGLGESYGDAPALAIQQQ
LQSQLIGLDPFNLNQLRAIVQATVAANKTQGIAGAELAPGSHASKAVSNAYSAFEVAFLD
LQAHSLNVPLVDLLGGAIRDEVPFSAYLFFKYAQHIDSPYKPDSWGEALNEEQIVAQARR
MIEAYGFKSIKLKAGALPPEHEVSCIKALKKAFPGYPLRIDPNGNWSLETSIRMAELLGD
DLQYYEDPTPGLDGMAELHKRTGLPLATNMVVTDFDEFRRSVALNSVQIVLADHHYWGGL
RDTQALAKMCDTFGLGVSMHSNSHLGISLMAMAHVAASVPNLDYACDTHYPWQEPDEEVI
KGGKLSIVDGCVKITRAPGLGLELDHDQLGKLHDQYLSCGIRQRDDVKQMQRYKPEWKTI
KPRF
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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