SitesBLAST
Comparing 3608603 FitnessBrowser__Dino:3608603 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)
P00944 Xylose isomerase; D-xylulose keto-isomerase; EC 5.3.1.5 from Escherichia coli (strain K12) (see paper)
60% identity, 100% coverage: 1:434/434 of query aligns to 1:437/440 of P00944
1a0eA Xylose isomerase from thermotoga neapolitana
50% identity, 100% coverage: 2:434/434 of query aligns to 1:435/443 of 1a0eA
- active site: H100 (= H99), D103 (= D102), W138 (= W137), E231 (= E230), K233 (= K232), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
- binding cobalt (ii) ion: E231 (= E230), E267 (= E266), E267 (= E266), H270 (= H269), D295 (= D294), D308 (= D307), D338 (= D337)
5nhcA Crystal structure of xylose isomerase from piromyces e2 in complex with two co2+ ions and xylulose (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nhcA
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding cobalt (ii) ion: E232 (= E230), E268 (= E266), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding 4-hydroxyproline: G290 (= G288), L292 (= L290), G328 (≠ A326), G330 (= G328), V332 (≠ D330)
- binding d-xylulose: W49 (= W49), H101 (= H99), W188 (= W186), E232 (= E230), E268 (= E266), H271 (= H269), D339 (= D337)
5nhaA Crystal structure of xylose isomerase from piromyces sp. E2 in complex with two mn2+ ions and sorbitol (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nhaA
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding manganese (ii) ion: E232 (= E230), E268 (= E266), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding sorbitol: W49 (= W49), H101 (= H99), W188 (= W186), E232 (= E230), D339 (= D337)
5nh9A Crystal structure of xylose isomerase from piromyces e2 in complex with two mn2+ ions and xylose (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nh9A
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding manganese (ii) ion: E232 (= E230), E268 (= E266), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding D-xylose: W49 (= W49), H101 (= H99), W188 (= W186), E232 (= E230), E268 (= E266), H271 (= H269), D339 (= D337)
- binding beta-D-xylopyranose: G63 (≠ P63), K65 (≠ F65), S66 (≠ Q66), K203 (≠ G201), K206 (≠ R204), H257 (≠ F255), D288 (≠ E286), A289 (≠ F287)
5nh7A Crystal structure of xylose isomerase from piromyces e2 in complex with two mg2+ ions and xylose (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nh7A
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding magnesium ion: E232 (= E230), E268 (= E266), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding D-xylose: W49 (= W49), H101 (= H99), W188 (= W186), E232 (= E230), E268 (= E266), H271 (= H269), D339 (= D337)
- binding beta-D-xylopyranose: G63 (≠ P63), K65 (≠ F65), S66 (≠ Q66)
- binding alpha-D-xylopyranose: P21 (≠ D21), D40 (= D40), Y97 (≠ F95), K136 (≠ R134), E350 (≠ A348)
5nh6A Crystal structure of xylose isomerase from piromyces e2 complexed with one mg2+ ion and xylitol (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nh6A
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding magnesium ion: E232 (= E230), E268 (= E266), D296 (= D294), D339 (= D337)
- binding Xylitol: W49 (= W49), H101 (= H99), W188 (= W186), E232 (= E230), E268 (= E266), H271 (= H269), D339 (= D337)
5nh5A Crystal structure of native xylose isomerase from piromyces e2 (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nh5A
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding calcium ion: E232 (= E230), E268 (= E266), D296 (= D294), D339 (= D337)
- binding fe (ii) ion: E232 (= E230), E268 (= E266), D296 (= D294), D339 (= D337)
- binding magnesium ion: E232 (= E230), E268 (= E266), D296 (= D294), D339 (= D337)
5nh4A Crystal structure of xylose isomerase from piromyces e2 in complex with one mg2+ ions and glycerol (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 2:435/436 of 5nh4A
- active site: H101 (= H99), D104 (= D102), W139 (= W137), E232 (= E230), K234 (= K232), E268 (= E266), H271 (= H269), D296 (= D294), D307 (= D305), D309 (= D307), D339 (= D337)
- binding magnesium ion: E232 (= E230), E268 (= E266), D296 (= D294), D339 (= D337)
5yn3A Crystal structure of xylose isomerase from piromyces sp. E2 (see paper)
49% identity, 100% coverage: 2:433/434 of query aligns to 1:434/435 of 5yn3A
- active site: H100 (= H99), D103 (= D102), W138 (= W137), E231 (= E230), K233 (= K232), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
- binding glycerol: H100 (= H99), W187 (= W186), E231 (= E230), D295 (= D294)
- binding manganese (ii) ion: E231 (= E230), E267 (= E266), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
1a0dA Xylose isomerase from bacillus stearothermophilus
50% identity, 99% coverage: 4:434/434 of query aligns to 2:433/437 of 1a0dA
- active site: H98 (= H99), D101 (= D102), W136 (= W137), E229 (= E230), K231 (= K232), E265 (= E266), H268 (= H269), D293 (= D294), D304 (= D305), D306 (= D307), D336 (= D337)
- binding manganese (ii) ion: E229 (= E230), E265 (= E266), E265 (= E266), H268 (= H269), D293 (= D294), D304 (= D305), D306 (= D307), D336 (= D337)
1a0cA Xylose isomerase from thermoanaerobacterium thermosulfurigenes
47% identity, 100% coverage: 2:434/434 of query aligns to 1:435/437 of 1a0cA
- active site: H100 (= H99), D103 (= D102), W138 (= W137), E231 (= E230), K233 (= K232), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
- binding cobalt (ii) ion: E231 (= E230), E267 (= E266), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
4xkmA Crystal structure of xylose isomerase from an human intestinal tract microbe bacteroides thetaiotaomicron
51% identity, 100% coverage: 2:433/434 of query aligns to 1:434/435 of 4xkmA
- active site: F23 (= F24), E29 (≠ D30), H100 (= H99), D103 (= D102), W138 (= W137), E231 (= E230), K233 (= K232), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
- binding manganese (ii) ion: E231 (= E230), E267 (= E266), E267 (= E266), H270 (= H269), D295 (= D294), D306 (= D305), D308 (= D307), D338 (= D337)
6intA Xylose isomerase from paenibacillus sp. R4 (see paper)
44% identity, 98% coverage: 4:429/434 of query aligns to 1:402/413 of 6intA
- active site: H74 (= H99), D77 (= D102), W112 (= W137), E205 (= E230), K207 (= K232), E241 (= E266), H244 (= H269), D269 (= D294), D280 (= D305), D282 (= D307), D313 (= D337)
- binding calcium ion: G166 (= G191), E178 (= E203), E205 (= E230), E241 (= E266), E241 (= E266), H244 (= H269), D269 (= D294), D280 (= D305), D282 (= D307), D313 (= D337)
1xycA X-ray crystallographic structures of d-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis (see paper)
30% identity, 69% coverage: 43:342/434 of query aligns to 9:291/386 of 1xycA
- active site: M87 (≠ W137)
- binding 3-o-methylfructose in linear form: W15 (= W49), H53 (= H99), T89 (= T139), W136 (= W186), E180 (= E230), K182 (= K232), H219 (= H269), D286 (= D337)
- binding magnesium ion: E180 (= E230), E216 (= E266), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
1xybA X-ray crystallographic structures of d-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis (see paper)
30% identity, 69% coverage: 43:342/434 of query aligns to 9:291/386 of 1xybA
- active site: M87 (≠ W137)
- binding D-glucose: H53 (= H99), W136 (= W186), E180 (= E230), K182 (= K232), H219 (= H269), D286 (= D337)
- binding magnesium ion: E180 (= E230), E216 (= E266), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
2gyiA Design, synthesis, and characterization of a potent xylose isomerase inhibitor, d-threonohydroxamic acid, and high-resolution x-ray crystallographic structure of the enzyme-inhibitor complex (see paper)
30% identity, 69% coverage: 43:342/434 of query aligns to 8:290/385 of 2gyiA
- active site: H52 (= H99), D55 (= D102), M86 (≠ W137), E179 (= E230), K181 (= K232), E215 (= E266), H218 (= H269), D243 (= D294), D253 (= D307), D255 (vs. gap), D285 (= D337)
- binding 2,3,4,n-tetrahydroxy-butyrimidic acid: H52 (= H99), W135 (= W186), E179 (= E230), K181 (= K232), H218 (= H269), D285 (= D337)
- binding magnesium ion: E179 (= E230), E215 (= E266), E215 (= E266), H218 (= H269), D243 (= D294), D285 (= D337)
1s5mA Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift (see paper)
30% identity, 69% coverage: 43:342/434 of query aligns to 9:291/386 of 1s5mA
- active site: H53 (= H99), D56 (= D102), M87 (≠ W137), E180 (= E230), K182 (= K232), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
- binding alpha-D-glucopyranose: H53 (= H99), F93 (= F143), W136 (= W186), E180 (= E230), D286 (= D337)
- binding manganese (ii) ion: E180 (= E230), E216 (= E266), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
1muwA The 0.86 angstrom structure of xylose isomerase
30% identity, 69% coverage: 43:342/434 of query aligns to 9:291/386 of 1muwA
- active site: H53 (= H99), D56 (= D102), M87 (≠ W137), E180 (= E230), K182 (= K232), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
- binding magnesium ion: P35 (≠ T73), L57 (≠ I103), H70 (≠ M120), D162 (≠ Q212), E206 (≠ G256), R207 (≠ L257), Y211 (≠ V261)
- binding manganese (ii) ion: E180 (= E230), E216 (= E266), E216 (= E266), H219 (= H269), D244 (= D294), D254 (= D307), D256 (vs. gap), D286 (= D337)
4j4kA Crystal structure of glucose isomerase
30% identity, 69% coverage: 43:342/434 of query aligns to 8:290/385 of 4j4kA
- active site: H52 (= H99), D55 (= D102), M86 (≠ W137), E179 (= E230), K181 (= K232), E215 (= E266), H218 (= H269), D243 (= D294), D253 (= D307), D255 (vs. gap), D285 (= D337)
- binding zinc ion: E179 (= E230), E215 (= E266), E215 (= E266), H218 (= H269), D243 (= D294), D253 (= D307), D255 (vs. gap), D285 (= D337)
Query Sequence
>3608603 FitnessBrowser__Dino:3608603
MSDFFAGIPAVTYEGPEARSDFAFRHYNPDEMVMGKRMEDQLRFAVAWWHSFAWEGGDPF
GGPTFQRPWFGDTLDHARAKADAAFEMFRILNVPFYCFHDADIRPEGASFAETTANLEAM
VDYLGQKQEASGKRLLWGTANLFSHRRYMAGAATNPDPDVFAYAAATIKTCMDATHKLGG
ANYVLWGGREGYETLLNTDLGREREQAGRMLQMVVDYKHKIGFEGTILLEPKPQEPTKHQ
YDYDVATVFSFLSEFGLQDEVKMNIEQGHAILAGHSFEHELALAREFGILGSIDMNRNDY
QSGWDTDQFPNNIPEVALAYYEILRAGGFDTGGTNFDSKLRRQSLDPADLIAAHVAAMDV
CAAGLKAAARMLEDGELEQRREDRYAGWRAPSAEAMLNGGKLEDCFAHVMETGLDPQPVS
GGQERLEALVARYL
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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