SitesBLAST
Comparing WP_084936388.1 NCBI__GCF_002095475.1:WP_084936388.1 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)
3n6hB Crystal structure of mandelate racemase/muconate lactonizing protein from actinobacillus succinogenes 130z complexed with magnesium/sulfate
69% identity, 99% coverage: 4:446/448 of query aligns to 1:431/432 of 3n6hB
- active site: K189 (= K204), K191 (= K206), D219 (= D234), N221 (= N236), E244 (= E259), N273 (= N288), D297 (= D312), H323 (= H338), N325 (= N340)
- binding magnesium ion: D219 (= D234), E244 (= E259), N273 (= N288)
3pfrA Crystal structure of d-glucarate dehydratase related protein from actinobacillus succinogenes complexed with d-glucarate
69% identity, 98% coverage: 5:445/448 of query aligns to 1:426/426 of 3pfrA
- active site: K185 (= K204), K187 (= K206), D215 (= D234), N217 (= N236), E240 (= E259), N269 (= N288), D293 (= D312), H319 (= H338), N321 (= N340)
- binding d-glucarate: N22 (= N26), H27 (= H31), Y130 (= Y149), F132 (= F151), K187 (= K206), D215 (= D234), N217 (= N236), N269 (= N288), H319 (= H338), S320 (= S339), N321 (= N340), H348 (= H367)
- binding magnesium ion: D215 (= D234), E240 (= E259), N269 (= N288)
P0AES2 Glucarate dehydratase; GDH; GlucD; D-glucarate dehydratase; EC 4.2.1.40 from Escherichia coli (strain K12) (see 3 papers)
65% identity, 99% coverage: 1:445/448 of query aligns to 1:446/446 of P0AES2
- M1 (= M1) modified: Initiator methionine, Removed
- Y150 (= Y149) mutation to F: Reduces activity 100-fold.
- K207 (= K206) active site, Proton acceptor; mutation to Q: Reduces activity 1000-fold.; mutation to R: Reduces activity 10000-fold.
- D235 (= D234) binding Mg(2+)
- E266 (= E265) binding Mg(2+)
- N289 (= N288) binding Mg(2+)
- H339 (= H338) 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 (= N340) 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 (= D365) mutation D->A,N: Reduces activity over 100-fold.
1ecqA E. Coli glucarate dehydratase bound to 4-deoxyglucarate (see paper)
65% identity, 98% coverage: 5:445/448 of query aligns to 4:444/444 of 1ecqA
- active site: K203 (= K204), K205 (= K206), D233 (= D234), N235 (= N236), E258 (= E259), N287 (= N288), M288 (= M289), D311 (= D312), H337 (= H338), N339 (= N340), I363 (= I364)
- binding 4-deoxyglucarate: N25 (= N26), H30 (= H31), T101 (= T104), Y148 (= Y149), F150 (= F151), K205 (= K206), D233 (= D234), N235 (= N236), N287 (= N288), H337 (= H338), S338 (= S339), N339 (= N340), H366 (= H367), R420 (= R421)
- binding magnesium ion: D233 (= D234), E258 (= E259), N287 (= N288)
1ec9D E. Coli glucarate dehydratase bound to xylarohydroxamate (see paper)
65% identity, 98% coverage: 5:445/448 of query aligns to 4:444/444 of 1ec9D
- active site: K203 (= K204), K205 (= K206), D233 (= D234), N235 (= N236), E258 (= E259), N287 (= N288), M288 (= M289), D311 (= D312), H337 (= H338), N339 (= N340), I363 (= I364)
- binding magnesium ion: D233 (= D234), E258 (= E259), N287 (= N288)
- binding xylarohydroxamate: H30 (= H31), T101 (= T104), Y148 (= Y149), F150 (= F151), K205 (= K206), D233 (= D234), N235 (= N236), N287 (= N288), H337 (= H338), S338 (= S339), N339 (= N340), H366 (= H367), R420 (= R421)
1ec8A E. Coli glucarate dehydratase bound to product 2,3-dihydroxy-5-oxo- hexanedioate (see paper)
65% identity, 98% coverage: 5:445/448 of query aligns to 2:442/442 of 1ec8A
- active site: K201 (= K204), K203 (= K206), D231 (= D234), N233 (= N236), E256 (= E259), N285 (= N288), M286 (= M289), D309 (= D312), H335 (= H338), N337 (= N340), I361 (= I364)
- binding 2,3-dihydroxy-5-oxo-hexanedioate: N23 (= N26), H28 (= H31), T99 (= T104), Y146 (= Y149), K203 (= K206), D231 (= D234), N233 (= N236), N285 (= N288), H335 (= H338), S336 (= S339), N337 (= N340), H364 (= H367), R418 (= R421)
- binding magnesium ion: D231 (= D234), E256 (= E259), N285 (= N288)
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
65% identity, 98% coverage: 5:445/448 of query aligns to 3:443/443 of 1jctA
- active site: K202 (= K204), K204 (= K206), D232 (= D234), N234 (= N236), E257 (= E259), N286 (= N288), M287 (= M289), D310 (= D312), H336 (= H338), L338 (≠ N340), I362 (= I364)
- binding d-glucarate: N24 (= N26), H29 (= H31), T100 (= T104), Y147 (= Y149), F149 (= F151), K204 (= K206), D232 (= D234), N286 (= N288), S337 (= S339), R419 (= R421)
- binding magnesium ion: D232 (= D234), E257 (= E259), N286 (= N288)
3p0wB Crystal structure of d-glucarate dehydratase from ralstonia solanacearum complexed with mg and d-glucarate
64% identity, 98% coverage: 6:443/448 of query aligns to 2:428/428 of 3p0wB
- active site: K189 (= K204), K191 (= K206), D219 (= D234), N221 (= N236), E244 (= E259), N273 (= N288), D297 (= D312), H323 (= H338), N325 (= N340)
- binding d-glucarate: H27 (= H31), Y134 (= Y149), K191 (= K206), D219 (= D234), N221 (= N236), N273 (= N288), H323 (= H338), N325 (= N340), H352 (= H367), R406 (= R421)
- binding magnesium ion: D219 (= D234), E244 (= E259), N273 (= N288)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
63% identity, 98% coverage: 6:444/448 of query aligns to 2:425/425 of 3nxlC
3nfuA Crystal structure of probable glucarate dehydratase from chromohalobacter salexigens dsm 3043 complexed with magnesium
58% identity, 98% coverage: 7:443/448 of query aligns to 3:439/441 of 3nfuA
- active site: K201 (= K204), K203 (= K206), D231 (= D234), N233 (= N236), E256 (= E259), N285 (= N288), D309 (= D312), H335 (= H338), N337 (= N340)
- binding magnesium ion: D231 (= D234), N233 (= N236), E256 (= E259), D257 (= D260), N285 (= N288)
4it1D Crystal structure of enolase pfl01_3283 (target efi-502286) from pseudomonas fluorescens pf0-1 with bound magnesium, potassium and tartrate
37% identity, 96% coverage: 9:440/448 of query aligns to 6:426/427 of 4it1D
- active site: S51 (≠ A54), D54 (≠ G57), A98 (vs. gap), Y150 (= Y149), K194 (= K204), K196 (= K206), D224 (= D234), N226 (= N236), Y247 (= Y257), E249 (= E259), T271 (= T287), N272 (= N288), M273 (= M289), D296 (= D312), H323 (= H338), S324 (= S339), N325 (= N340), C349 (≠ I364), D350 (= D365)
- binding magnesium ion: D224 (= D234), E249 (= E259), N272 (= N288)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
34% identity, 96% coverage: 8:435/448 of query aligns to 12:421/427 of 3va8A
3vc6A Crystal structure of enolase tbis_1083(target efi-502310) from thermobispora bispora dsm 43833 complexed with magnesium and formate
35% identity, 97% coverage: 6:438/448 of query aligns to 1:417/420 of 3vc6A
- active site: D52 (≠ G57), H55 (≠ I60), Y146 (= Y149), K188 (= K204), K190 (= K206), D218 (= D234), N220 (= N236), E243 (= E259), N266 (= N288), M267 (= M289), D290 (= D312), H317 (= H338), S318 (= S339), N319 (= N340), H321 (= H342), C343 (≠ I364), D344 (= D365)
- binding magnesium ion: D218 (= D234), E243 (= E259), N266 (= N288)
3dg6A Crystal structure of muconate lactonizing enzyme from mucobacterium smegmatis complexed with muconolactone (see paper)
25% identity, 66% coverage: 110:406/448 of query aligns to 97:360/366 of 3dg6A
- active site: M134 (≠ L150), K160 (= K204), K162 (= K206), D191 (= D234), N193 (= N236), E217 (= E259), D242 (≠ N288), E243 (≠ M289), S244 (≠ I290), K266 (≠ P309), G292 (≠ H338), N293 (≠ S339), Q294 (≠ N340), G319 (≠ D365), E320 (≠ T366), L321 (≠ H367)
- binding magnesium ion: D191 (= D234), E217 (= E259), D242 (≠ N288)
- binding [(2S)-5-oxo-2,5-dihydrofuran-2-yl]acetic acid: M134 (≠ L150), K160 (= K204), K162 (= K206), D191 (= D234), N193 (= N236), D242 (≠ N288), K266 (≠ P309), N293 (≠ S339), Q294 (≠ N340), I295 (≠ N341)
Sites not aligning to the query:
5olcC Crystal structure of the 3,6-anhydro-d-galactonate cycloisomerase from zobellia galactanivorans (see paper)
23% identity, 85% coverage: 30:408/448 of query aligns to 12:347/351 of 5olcC
- active site: K148 (= K204), K150 (= K206), D178 (= D234), N180 (= N236), E204 (= E259), G229 (≠ N288), E230 (≠ A291), D253 (≠ H314), H280 (vs. gap), E304 (≠ A363), E309 (= E372)
- binding magnesium ion: D178 (= D234), E204 (= E259), E230 (≠ A291)
2ps2A Crystal structure of putative mandelate racemase/muconate lactonizing enzyme from aspergillus oryzae
23% identity, 90% coverage: 11:413/448 of query aligns to 1:361/361 of 2ps2A
- active site: Y21 (≠ H31), S132 (≠ G166), Q156 (≠ K201), S157 (≠ D202), V158 (≠ F203), K159 (= K204), D187 (= D234), E213 (= E259), D236 (≠ N288), E237 (≠ M289), K260 (≠ P309), Q287 (≠ H338), E288 (≠ S339), T289 (≠ N340), C313 (≠ W368), I314 (= I369), L315 (≠ W370)
- binding magnesium ion: D187 (= D234), E213 (= E259), D236 (≠ N288)
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, 66% coverage: 111:406/448 of query aligns to 106:363/375 of Q9RYA6
- R120 (≠ Q125) mutation to C: Loss of activity; when associated with C-48.
- G127 (≠ A132) mutation to C: Retains 93% of wild-type activity; when associated with C-313.
- S142 (≠ D160) binding N-acetyl-L-glutamine
- E149 (= E167) mutation to C: Retains 88% of wild-type activity; when associated with C-182.
- G163 (= G199) mutation to C: Loss of activity; when associated with C-343.
- KLK 168:170 (= KLK 204:206) binding N-acetyl-L-glutamine
- A182 (= A221) mutation to C: Retains 88% of wild-type activity; when associated with C-149.
- D195 (= D234) binding Mg(2+)
- Y218 (= Y257) mutation to C: Retains 35% of wild-type activity.
- E220 (= E259) binding Mg(2+)
- D245 (≠ N288) binding Mg(2+)
- V265 (vs. gap) mutation to C: Retains 39% of wild-type activity.
- K269 (≠ A311) binding N-acetyl-L-glutamine
- L299 (≠ N341) binding N-acetyl-L-glutamine
- T313 (≠ A355) mutation to C: Retains 93% of wild-type activity; when associated with C-127.
- D343 (≠ N386) 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.
2gghC The mutant a68c-d72c-nlq of deinococcus radiodurans nacylamino acid racemase (see paper)
27% identity, 66% coverage: 111:406/448 of query aligns to 101:358/370 of 2gghC
- active site: S137 (≠ D160), K163 (= K204), K165 (= K206), R186 (= R230), T188 (= T232), D190 (= D234), N192 (= N236), E215 (= E259), D240 (≠ N288), E241 (≠ M289), S242 (≠ I290), K264 (≠ A311), C290 (= C337), G291 (≠ H338), G292 (≠ S339), M293 (≠ N340), G316 (= G359), D317 (≠ K360), T318 (≠ P361)
- binding magnesium ion: D190 (= D234), E215 (= E259)
- binding n~2~-acetyl-l-glutamine: G292 (≠ S339), M293 (≠ N340), L294 (≠ N341)
Sites not aligning to the query:
Q8ZL58 L-talarate/galactarate dehydratase; TalrD/GalrD; StTGD; EC 4.2.1.156; EC 4.2.1.42 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
24% identity, 81% coverage: 39:401/448 of query aligns to 64:380/398 of Q8ZL58
- KR 82:83 (≠ EA 53:54) binding substrate
- K195 (= K204) binding substrate
- K197 (= K206) active site, Proton acceptor; mutation to A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- D226 (= D234) binding Mg(2+)
- N228 (= N236) binding substrate
- E252 (= E259) binding Mg(2+)
- E278 (≠ M289) binding Mg(2+)
- H328 (= H338) active site, Proton donor/acceptor; mutation H->N,A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity.
- E348 (≠ I364) binding substrate
Sites not aligning to the query:
2pp1A Crystal structure of l-talarate/galactarate dehydratase from salmonella typhimurium lt2 liganded with mg and l-lyxarohydroxamate (see paper)
24% identity, 81% coverage: 39:401/448 of query aligns to 61:377/395 of 2pp1A
- active site: S78 (vs. gap), K192 (= K204), K194 (= K206), D223 (= D234), N225 (= N236), E249 (= E259), G274 (≠ N288), E275 (≠ M289), D298 (= D312), H325 (= H338), E345 (≠ I364)
- binding (2r,3s,4r)-2,3,4-trihydroxy-5-(hydroxyamino)-5-oxopentanoic acid: K79 (≠ E53), F168 (≠ A169), K194 (= K206), E275 (≠ M289), H325 (= H338), E345 (≠ I364)
- binding magnesium ion: D223 (= D234), E249 (= E259), E275 (≠ M289)
Sites not aligning to the query:
Query Sequence
>WP_084936388.1 NCBI__GCF_002095475.1:WP_084936388.1
MNTQSSPVITDMQVIPVAGYDSMLLNIGGAHSACFTRNIVVLTDSDGHTGVGEAPGGETI
YQTLVEAIPQVKGQQVARMNRLVQQVHKGNQSADFDTFGKGAWTFELRVNAVAALEAALL
DLLGQCLGVPVAELLGPGQQRDEVTVLGYLFYLGDRRKTDLPYLTGEGASHDWYHLRHQE
ALTPEAVVRLAEAAQDKYGFKDFKLKGGVLPGEQEIESAAALKKRFPDARITVDPNGAWT
LDEAIRLCKGMGDVLTYAEDPCGAEQGYSGREVMAEFRRATGLPVATNMIATNWREMNHA
VMLNSVDIPLADPHFWTPSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGK
PTAIDTHWIWQEGDQRLTKEPLQIRNGKIAVPDKPGLGVELDWDRLHQANALYKSLPAGS
RNDATAMQYLVPGWSFDRKRPAFGRRHA
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