SitesBLAST
Comparing Pf1N1B4_71 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_71 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)
76% identity, 98% coverage: 10:447/447 of query aligns to 8:446/446 of P0AES2
- Y150 (= Y152) mutation to F: Reduces activity 100-fold.
- K207 (= K209) active site, Proton acceptor; mutation to Q: Reduces activity 1000-fold.; mutation to R: Reduces activity 10000-fold.
- D235 (= D237) binding
- E266 (= E268) binding
- N289 (= N291) binding
- H339 (= H341) 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 (= N343) 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 (= D368) 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)
76% identity, 98% coverage: 10:447/447 of query aligns to 6:444/444 of 1ecqA
- active site: K203 (= K207), K205 (= K209), D233 (= D237), N235 (= N239), E258 (= E262), N287 (= N291), M288 (= M292), D311 (= D315), H337 (= H341), N339 (= N343), I363 (= I367)
- binding 4-deoxyglucarate: N25 (= N29), H30 (= H34), T101 (= T105), Y148 (= Y152), F150 (= F154), K205 (= K209), D233 (= D237), N235 (= N239), N287 (= N291), H337 (= H341), S338 (= S342), N339 (= N343), H366 (= H370), R420 (= R423)
- binding magnesium ion: D233 (= D237), E258 (= E262), N287 (= N291)
1ec9D E. Coli glucarate dehydratase bound to xylarohydroxamate (see paper)
76% identity, 98% coverage: 10:447/447 of query aligns to 6:444/444 of 1ec9D
- active site: K203 (= K207), K205 (= K209), D233 (= D237), N235 (= N239), E258 (= E262), N287 (= N291), M288 (= M292), D311 (= D315), H337 (= H341), N339 (= N343), I363 (= I367)
- binding magnesium ion: D233 (= D237), E258 (= E262), N287 (= N291)
- binding xylarohydroxamate: H30 (= H34), T101 (= T105), Y148 (= Y152), F150 (= F154), K205 (= K209), D233 (= D237), N235 (= N239), N287 (= N291), H337 (= H341), S338 (= S342), N339 (= N343), H366 (= H370), R420 (= R423)
1ec8A E. Coli glucarate dehydratase bound to product 2,3-dihydroxy-5-oxo- hexanedioate (see paper)
76% identity, 98% coverage: 10:447/447 of query aligns to 4:442/442 of 1ec8A
- active site: K201 (= K207), K203 (= K209), D231 (= D237), N233 (= N239), E256 (= E262), N285 (= N291), M286 (= M292), D309 (= D315), H335 (= H341), N337 (= N343), I361 (= I367)
- binding 2,3-dihydroxy-5-oxo-hexanedioate: N23 (= N29), H28 (= H34), T99 (= T105), Y146 (= Y152), K203 (= K209), D231 (= D237), N233 (= N239), N285 (= N291), H335 (= H341), S336 (= S342), N337 (= N343), H364 (= H370), R418 (= R423)
- binding magnesium ion: D231 (= D237), E256 (= E262), N285 (= N291)
1jctA Glucarate dehydratase, n341l mutant orthorhombic form (see paper)
76% identity, 98% coverage: 10:447/447 of query aligns to 5:443/443 of 1jctA
- active site: K202 (= K207), K204 (= K209), D232 (= D237), N234 (= N239), E257 (= E262), N286 (= N291), M287 (= M292), D310 (= D315), H336 (= H341), L338 (≠ N343), I362 (= I367)
- binding d-glucarate: N24 (= N29), H29 (= H34), T100 (= T105), Y147 (= Y152), F149 (= F154), K204 (= K209), D232 (= D237), N286 (= N291), S337 (= S342), R419 (= R423)
- binding magnesium ion: D232 (= D237), E257 (= E262), N286 (= N291)
3p0wB Crystal structure of d-glucarate dehydratase from ralstonia solanacearum complexed with mg and d-glucarate
68% identity, 98% coverage: 10:445/447 of query aligns to 3:428/428 of 3p0wB
- active site: K189 (= K207), K191 (= K209), D219 (= D237), N221 (= N239), E244 (= E262), N273 (= N291), D297 (= D315), H323 (= H341), N325 (= N343)
- binding d-glucarate: H27 (= H34), Y134 (= Y152), K191 (= K209), D219 (= D237), N221 (= N239), N273 (= N291), H323 (= H341), N325 (= N343), H352 (= H370), R406 (= R423)
- binding magnesium ion: D219 (= D237), E244 (= E262), N273 (= N291)
3nxlC Crystal structure of glucarate dehydratase from burkholderia cepacia complexed with magnesium
67% identity, 98% coverage: 10:445/447 of query aligns to 3:424/425 of 3nxlC
3n6hB Crystal structure of mandelate racemase/muconate lactonizing protein from actinobacillus succinogenes 130z complexed with magnesium/sulfate
63% identity, 98% coverage: 9:447/447 of query aligns to 3:430/432 of 3n6hB
- active site: K189 (= K207), K191 (= K209), D219 (= D237), N221 (= N239), E244 (= E262), N273 (= N291), D297 (= D315), H323 (= H341), N325 (= N343)
- binding magnesium ion: D219 (= D237), E244 (= E262), N273 (= N291)
3pfrA Crystal structure of d-glucarate dehydratase related protein from actinobacillus succinogenes complexed with d-glucarate
63% identity, 98% coverage: 9:447/447 of query aligns to 2:426/426 of 3pfrA
- active site: K185 (= K207), K187 (= K209), D215 (= D237), N217 (= N239), E240 (= E262), N269 (= N291), D293 (= D315), H319 (= H341), N321 (= N343)
- binding d-glucarate: N22 (= N29), H27 (= H34), Y130 (= Y152), F132 (= F154), K187 (= K209), D215 (= D237), N217 (= N239), N269 (= N291), H319 (= H341), S320 (= S342), N321 (= N343), H348 (= H370)
- binding magnesium ion: D215 (= D237), E240 (= E262), N269 (= N291)
3nfuA Crystal structure of probable glucarate dehydratase from chromohalobacter salexigens dsm 3043 complexed with magnesium
60% identity, 98% coverage: 10:446/447 of query aligns to 3:440/441 of 3nfuA
- active site: K201 (= K207), K203 (= K209), D231 (= D237), N233 (= N239), E256 (= E262), N285 (= N291), D309 (= D315), H335 (= H341), N337 (= N343)
- binding magnesium ion: D231 (= D237), N233 (= N239), E256 (= E262), D257 (= D263), N285 (= N291)
4it1D Crystal structure of enolase pfl01_3283 (target efi-502286) from pseudomonas fluorescens pf0-1 with bound magnesium, potassium and tartrate
38% identity, 95% coverage: 12:437/447 of query aligns to 6:421/427 of 4it1D
- active site: S51 (≠ V57), D54 (≠ G60), A98 (≠ L103), Y150 (= Y152), K194 (= K207), K196 (= K209), D224 (= D237), N226 (= N239), Y247 (= Y260), E249 (= E262), T271 (= T290), N272 (= N291), M273 (= M292), D296 (= D315), H323 (= H341), S324 (= S342), N325 (= N343), C349 (≠ I367), D350 (= D368)
- binding magnesium ion: D224 (= D237), E249 (= E262), N272 (= N291)
3va8A Crystal structure of enolase fg03645.1 (target efi-502278) from gibberella zeae ph-1 complexed with magnesium, formate and sulfate
34% identity, 98% coverage: 4:443/447 of query aligns to 5:425/427 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: 11:442/447 of query aligns to 3:417/420 of 3vc6A
- active site: D52 (≠ G60), H55 (≠ I63), Y146 (= Y152), K188 (= K207), K190 (= K209), D218 (= D237), N220 (= N239), E243 (= E262), N266 (= N291), M267 (= M292), D290 (= D315), H317 (= H341), S318 (= S342), N319 (= N343), H321 (= H345), C343 (≠ I367), D344 (= D368)
- binding magnesium ion: D218 (= D237), E243 (= E262), N266 (= N291)
2gghC The mutant a68c-d72c-nlq of deinococcus radiodurans nacylamino acid racemase (see paper)
26% identity, 72% coverage: 91:413/447 of query aligns to 80:363/370 of 2gghC
- active site: Y95 (≠ F106), S137 (≠ D163), K163 (= K207), K165 (= K209), R186 (= R233), T188 (= T235), D190 (= D237), N192 (= N239), E215 (= E262), D240 (≠ K287), E241 (≠ T288), S242 (≠ A289), K264 (≠ Q307), C290 (≠ S340), G291 (≠ H341), G292 (≠ S342), M293 (≠ N343), G316 (= G362), D317 (≠ E363), T318 (≠ I364)
- binding magnesium ion: D190 (= D237), E215 (= E262)
- binding n~2~-acetyl-l-glutamine: G292 (≠ S342), M293 (≠ N343), L294 (≠ N344)
Sites not aligning to the query:
3dg6A Crystal structure of muconate lactonizing enzyme from mucobacterium smegmatis complexed with muconolactone (see paper)
28% identity, 66% coverage: 114:409/447 of query aligns to 98:361/366 of 3dg6A
- active site: M134 (≠ E182), K160 (= K207), K162 (= K209), D191 (= D237), N193 (= N239), E217 (= E262), D242 (≠ K287), E243 (≠ T288), S244 (≠ A289), K266 (≠ P312), G292 (≠ N343), N293 (= N344), Q294 (≠ H345), G319 (≠ I367), E320 (≠ D368), L321 (≠ T369)
- binding magnesium ion: D191 (= D237), E217 (= E262), D242 (≠ K287)
- binding [(2S)-5-oxo-2,5-dihydrofuran-2-yl]acetic acid: M134 (≠ E182), K160 (= K207), K162 (= K209), D191 (= D237), N193 (= N239), D242 (≠ K287), K266 (≠ P312), N293 (= N344), Q294 (≠ H345), I295 (≠ F346)
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)
25% identity, 72% coverage: 91:413/447 of query aligns to 85:368/375 of Q9RYA6
- Y100 (≠ F106) mutation to C: Loss of activity; when associated with C-60.
- R120 (≠ Q128) mutation to C: Loss of activity; when associated with C-48.
- G127 (≠ A135) mutation to C: Retains 93% of wild-type activity; when associated with C-313.
- S142 (vs. gap) binding
- E149 (≠ D158) mutation to C: Retains 88% of wild-type activity; when associated with C-182.
- G163 (= G202) mutation to C: Loss of activity; when associated with C-343.
- KLK 168:170 (= KLK 207:209) binding
- A182 (= A224) mutation to C: Retains 88% of wild-type activity; when associated with C-149.
- D195 (= D237) binding
- Y218 (= Y260) mutation to C: Retains 35% of wild-type activity.
- E220 (= E262) binding
- D245 (≠ K287) binding
- V265 (≠ A303) mutation to C: Retains 39% of wild-type activity.
- K269 (≠ Q307) binding
- L299 (≠ N344) binding
- T313 (≠ A358) mutation to C: Retains 93% of wild-type activity; when associated with C-127.
- D343 (= D388) 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.
2ps2A Crystal structure of putative mandelate racemase/muconate lactonizing enzyme from aspergillus oryzae
25% identity, 68% coverage: 114:415/447 of query aligns to 95:361/361 of 2ps2A
- active site: S132 (≠ Y152), Q156 (≠ K204), S157 (≠ D205), V158 (≠ F206), K159 (= K207), D187 (= D237), E213 (= E262), D236 (≠ N291), E237 (≠ M292), K260 (≠ A314), Q287 (≠ H341), E288 (≠ S342), T289 (≠ N343), C313 (≠ I367), I314 (≠ D368), L315 (≠ T369)
- binding magnesium ion: D187 (= D237), E213 (= E262), D236 (≠ N291)
Sites not aligning to the query:
5olcC Crystal structure of the 3,6-anhydro-d-galactonate cycloisomerase from zobellia galactanivorans (see paper)
24% identity, 66% coverage: 114:408/447 of query aligns to 87:345/351 of 5olcC
- active site: K148 (= K207), K150 (= K209), D178 (= D237), N180 (= N239), E204 (= E262), G229 (≠ N291), E230 (≠ A294), D253 (≠ H317), H280 (= H332), E304 (≠ A366), E309 (≠ H370)
- binding magnesium ion: D178 (= D237), E204 (= E262), E230 (≠ A294)
3t8qB Crystal structure of mandelate racemase/muconate lactonizing enzyme family protein from hoeflea phototrophica
25% identity, 68% coverage: 113:414/447 of query aligns to 82:365/369 of 3t8qB
- active site: S120 (≠ R159), K147 (= K207), R149 (≠ K209), D159 (≠ I219), D185 (= D237), N187 (= N239), E211 (= E262), G236 (≠ L286), E237 (≠ K287), D239 (≠ A289), Q258 (≠ D315), D260 (≠ H317), H287 (= H341), A288 (≠ S342), A289 (≠ N343), K310 (≠ T365), E313 (≠ D368)
- binding magnesium ion: D185 (= D237), E211 (= E262), E237 (≠ K287)
3cb3A Crystal structure of l-talarate dehydratase from polaromonas sp. Js666 complexed with mg and l-glucarate
27% identity, 47% coverage: 196:404/447 of query aligns to 160:357/373 of 3cb3A
- active site: K171 (= K207), K173 (= K209), D202 (= D237), N204 (= N239), E228 (= E262), G253 (≠ N291), E254 (≠ M292), M275 (≠ L313), D277 (= D315), H304 (= H341), F305 (≠ I348), A306 (≠ S349), E324 (≠ I367)
- binding l-glucaric acid: K171 (= K207), K173 (= K209), D202 (= D237), E254 (≠ M292), H304 (= H341)
- binding magnesium ion: D202 (= D237), E228 (= E262), A243 (≠ M277), F246 (= F280), E254 (≠ M292)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_71 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_71
MNPQEAAKAPIITSMQVVPVAGHDGMLLNLSGAHGPFFTRNVVILKDNAGHTGVGEVPGG
ERIRQTLEDARALVVGSPIGTYQKILNQVRQTFADRDAGGRGLQTFDLRITIHAVTGLEA
ALLDLLGQHLDVPVAALLGEGQQRDEVKMLGYLFYVGDRNETDLAYRSEPDADNDWFRVR
HEKAMSADAVVRLAEAAHARYGFKDFKLKGGVLSGDEEIEAVTALAERFPDARITLDPNG
AWSLKEAIRLCRDQHHVLAYAEDPCGAENSYSGREVMAEFRRATGLKTATNMIATDWREM
GHAIQLQSVDIPLADPHFWTLQGSVRVAQMCHEWGLTWGSHSNNHFDISLAMFTHVAAAA
PGEITAIDTHWIWQDGQRLTKAPLQIVDGCVQVPTKPGLGVELDMDQLAKAHELYKGMGL
GARDDSVAMQFLIPGWKFDNKRPCLVR
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