SitesBLAST
Comparing HSERO_RS05730 FitnessBrowser__HerbieS:HSERO_RS05730 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
84% 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)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
47% identity, 100% coverage: 3:424/424 of query aligns to 13:427/427 of 3va8A
3vc6A Crystal structure of enolase tbis_1083(target efi-502310) from thermobispora bispora dsm 43833 complexed with magnesium and formate
48% identity, 99% coverage: 1:421/424 of query aligns to 2:417/420 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)
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)
1ecqA E. Coli glucarate dehydratase bound to 4-deoxyglucarate (see paper)
36% 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)
36% 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)
36% 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)
P0AES2 Glucarate dehydratase; GDH; GlucD; D-glucarate dehydratase; EC 4.2.1.40 from Escherichia coli (strain K12) (see 3 papers)
36% 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
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
36% 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
33% 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)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
36% identity, 100% coverage: 2:423/424 of query aligns to 4:420/425 of 3nxlC
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)
3i4kA Crystal structure of muconate lactonizing enzyme from corynebacterium glutamicum
30% 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:
2qq6B Crystal structure of mandelate racemase/muconate lactonizing enzyme- like protein from rubrobacter xylanophilus dsm 9941
31% identity, 81% coverage: 44:387/424 of query aligns to 31:381/396 of 2qq6B
- active site: P37 (≠ G50), G79 (≠ S101), D124 (vs. gap), K166 (= K191), D168 (≠ K193), D213 (= D221), H215 (≠ N223), E239 (= E246), G264 (≠ T268), E265 (≠ N269), M286 (≠ L291), D288 (= D293), H315 (= H320), N316 (= N322), E340 (vs. gap), D345 (= D347)
- binding magnesium ion: D213 (= D221), E239 (= E246), E265 (≠ N269), H315 (= H320)
1nu5A Crystal structure of pseudomonas sp. P51 chloromuconate lactonizing enzyme (see paper)
28% identity, 67% coverage: 109:390/424 of query aligns to 99:364/369 of 1nu5A
- active site: T137 (≠ Y147), K163 (= K191), K165 (= K193), E176 (≠ A204), 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:
2p8cA Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 complexed with n-succinyl arg. (see paper)
24% identity, 85% coverage: 33:392/424 of query aligns to 33:361/369 of 2p8cA
- active site: A50 (≠ G50), H53 (vs. gap), V136 (≠ I156), F160 (≠ I190), K161 (= K191), M162 (≠ L192), K163 (= K193), D191 (= D221), N193 (= N223), E218 (= E246), D243 (≠ N269), E244 (≠ M270), G245 (≠ V271), N265 (≠ L291), K267 (≠ D293), G294 (≠ H320), S295 (= S321), M296 (≠ N322), V319 (≠ Y350), E320 (≠ P351), L321 (≠ W352)
- binding magnesium ion: D191 (= D221), E218 (= E246), D243 (≠ N269)
- binding n~2~-(3-carboxypropanoyl)-l-arginine: D51 (= D51), K163 (= K193), D191 (= D221), D243 (≠ N269), K267 (≠ D293), S295 (= S321), M296 (≠ N322), E320 (≠ P351), L321 (≠ W352), T322 (≠ Q353)
Sites not aligning to the query:
2p8bA Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 complexed with n-succinyl lys. (see paper)
24% identity, 85% coverage: 33:392/424 of query aligns to 33:361/369 of 2p8bA
- active site: A50 (≠ G50), H53 (vs. gap), V136 (≠ I156), F160 (≠ I190), K161 (= K191), M162 (≠ L192), K163 (= K193), D191 (= D221), N193 (= N223), E218 (= E246), D243 (≠ N269), E244 (≠ M270), G245 (≠ V271), N265 (≠ L291), K267 (≠ D293), G294 (≠ H320), S295 (= S321), M296 (≠ N322), V319 (≠ Y350), E320 (≠ P351), L321 (≠ W352)
- binding magnesium ion: D191 (= D221), E218 (= E246), D243 (≠ N269)
- binding n-succinyl lysine: D51 (= D51), V136 (≠ I156), K161 (= K191), K163 (= K193), D243 (≠ N269), K267 (≠ D293), S295 (= S321), M296 (≠ N322), E320 (≠ P351), L321 (≠ W352), T322 (≠ Q353)
Sites not aligning to the query:
2p88A Crystal structure of n-succinyl arg/lys racemase from bacillus cereus atcc 14579 (see paper)
24% identity, 85% coverage: 33:392/424 of query aligns to 33:361/369 of 2p88A
- active site: A50 (≠ G50), H53 (vs. gap), V136 (≠ I156), F160 (≠ I190), K161 (= K191), M162 (≠ L192), K163 (= K193), D191 (= D221), N193 (= N223), E218 (= E246), D243 (≠ N269), E244 (≠ M270), G245 (≠ V271), N265 (≠ L291), K267 (≠ D293), G294 (≠ H320), S295 (= S321), M296 (≠ N322), V319 (≠ Y350), E320 (≠ P351), L321 (≠ W352)
- binding magnesium ion: D191 (= D221), E218 (= E246), D243 (≠ N269)
Sites not aligning to the query:
Q81IL5 N-succinyl-L-Arg/Lys racemase; N-succinyl amino acid racemase; NSAR; EC 5.1.1.- from Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) (see paper)
24% identity, 85% coverage: 33:392/424 of query aligns to 33:361/369 of Q81IL5
- D191 (= D221) binding
- E218 (= E246) binding
- D243 (≠ N269) binding
Query Sequence
>HSERO_RS05730 FitnessBrowser__HerbieS:HSERO_RS05730
MKITRVTVTPIAFKDGPLLNASGIHEPYALRSIIEIETDNGYIGLGESYGDAPALKILDL
VKERLVGLDPFNLNGLRAIVRGVVAAMAPASNAGAELAPGSHASKAVSNAYSAFEVACLD
AQARYLNVPLVDLLGGAVRKEIPFSAYLFFKYAQHIDSPYAPDAWGEALSEEQIVAQARK
MIEENGFQSIKLKAGALAPEHEVACIKALRKAFPDAPLRIDPNGNWSLQTAIRMAELLGD
DLQYYEDPTPGLEGMAELHRRTGLPLATNMVVTDFDELRRSVALDSVQIVLADHHYWGGL
RDTQQLAKMCDVFGLGVSMHSNSHLGISLMAMSHVAAAVENLSYACDTHYPWQEPDEEVI
QGGKLPIRNGCVQITDAPGLGVEVDQDQLRKLHQLYLECGIRQRDDVGQMRKYQPDWKTV
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