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Comparing BPHYT_RS32825 FitnessBrowser__BFirm:BPHYT_RS32825 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)
67% identity, 99% coverage: 2:437/440 of query aligns to 3:438/440 of P00944
- H101 (= H100) active site
1a0cA Xylose isomerase from thermoanaerobacterium thermosulfurigenes
50% identity, 99% coverage: 2:438/440 of query aligns to 2:437/437 of 1a0cA
- active site: H100 (= H100), D103 (= D103), W138 (= W138), E231 (= E231), K233 (= K233), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
- binding cobalt (ii) ion: E231 (= E231), E267 (= E267), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
1a0eA Xylose isomerase from thermotoga neapolitana
51% identity, 99% coverage: 3:436/440 of query aligns to 3:435/443 of 1a0eA
- active site: H100 (= H100), D103 (= D103), W138 (= W138), E231 (= E231), K233 (= K233), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
- binding cobalt (ii) ion: E231 (= E231), E267 (= E267), E267 (= E267), H270 (= H270), D295 (= D295), D308 (= D308), D338 (= D338)
5yn3A Crystal structure of xylose isomerase from piromyces sp. E2 (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 3:431/435 of 5yn3A
- active site: H100 (= H100), D103 (= D103), W138 (= W138), E231 (= E231), K233 (= K233), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
- binding glycerol: H100 (= H100), W187 (= W187), E231 (= E231), D295 (= D295)
- binding manganese (ii) ion: E231 (= E231), E267 (= E267), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
5nhcA Crystal structure of xylose isomerase from piromyces e2 in complex with two co2+ ions and xylulose (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nhcA
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding cobalt (ii) ion: E232 (= E231), E268 (= E267), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding 4-hydroxyproline: G290 (= G289), L292 (≠ F291), G328 (≠ H327), G330 (= G329), V332 (≠ T331)
- binding d-xylulose: W49 (= W48), H101 (= H100), W188 (= W187), E232 (= E231), E268 (= E267), H271 (= H270), D339 (= D338)
5nhaA Crystal structure of xylose isomerase from piromyces sp. E2 in complex with two mn2+ ions and sorbitol (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nhaA
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding manganese (ii) ion: E232 (= E231), E268 (= E267), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding sorbitol: W49 (= W48), H101 (= H100), W188 (= W187), E232 (= E231), D339 (= D338)
5nh9A Crystal structure of xylose isomerase from piromyces e2 in complex with two mn2+ ions and xylose (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nh9A
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding manganese (ii) ion: E232 (= E231), E268 (= E267), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding D-xylose: W49 (= W48), H101 (= H100), W188 (= W187), E232 (= E231), E268 (= E267), H271 (= H270), D339 (= D338)
- binding beta-D-xylopyranose: G63 (= G62), K65 (≠ F64), S66 (≠ R65), K203 (≠ V202), K206 (≠ R205), H257 (= H256), D288 (≠ A287), A289 (≠ L288)
5nh7A Crystal structure of xylose isomerase from piromyces e2 in complex with two mg2+ ions and xylose (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nh7A
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding magnesium ion: E232 (= E231), E268 (= E267), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding D-xylose: W49 (= W48), H101 (= H100), W188 (= W187), E232 (= E231), E268 (= E267), H271 (= H270), D339 (= D338)
- binding beta-D-xylopyranose: G63 (= G62), K65 (≠ F64), S66 (≠ R65)
- binding alpha-D-xylopyranose: P21 (= P20), D40 (≠ E39), Y97 (= Y96), K136 (= K135), E350 (= E349)
5nh6A Crystal structure of xylose isomerase from piromyces e2 complexed with one mg2+ ion and xylitol (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nh6A
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding magnesium ion: E232 (= E231), E268 (= E267), D296 (= D295), D339 (= D338)
- binding Xylitol: W49 (= W48), H101 (= H100), W188 (= W187), E232 (= E231), E268 (= E267), H271 (= H270), D339 (= D338)
5nh5A Crystal structure of native xylose isomerase from piromyces e2 (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nh5A
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding calcium ion: E232 (= E231), E268 (= E267), D296 (= D295), D339 (= D338)
- binding fe (ii) ion: E232 (= E231), E268 (= E267), D296 (= D295), D339 (= D338)
- binding magnesium ion: E232 (= E231), E268 (= E267), D296 (= D295), D339 (= D338)
5nh4A Crystal structure of xylose isomerase from piromyces e2 in complex with one mg2+ ions and glycerol (see paper)
51% identity, 98% coverage: 3:432/440 of query aligns to 4:432/436 of 5nh4A
- active site: H101 (= H100), D104 (= D103), W139 (= W138), E232 (= E231), K234 (= K233), E268 (= E267), H271 (= H270), D296 (= D295), D307 (= D306), D309 (= D308), D339 (= D338)
- binding magnesium ion: E232 (= E231), E268 (= E267), D296 (= D295), D339 (= D338)
1a0dA Xylose isomerase from bacillus stearothermophilus
52% identity, 99% coverage: 3:436/440 of query aligns to 2:433/437 of 1a0dA
- active site: H98 (= H100), D101 (= D103), W136 (= W138), E229 (= E231), K231 (= K233), E265 (= E267), H268 (= H270), D293 (= D295), D304 (= D306), D306 (= D308), D336 (= D338)
- binding manganese (ii) ion: E229 (= E231), E265 (= E267), E265 (= E267), H268 (= H270), D293 (= D295), D304 (= D306), D306 (= D308), D336 (= D338)
4xkmA Crystal structure of xylose isomerase from an human intestinal tract microbe bacteroides thetaiotaomicron
51% identity, 98% coverage: 3:433/440 of query aligns to 3:432/435 of 4xkmA
- active site: F23 (≠ Y23), E29 (≠ S29), H100 (= H100), D103 (= D103), W138 (= W138), E231 (= E231), K233 (= K233), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
- binding manganese (ii) ion: E231 (= E231), E267 (= E267), E267 (= E267), H270 (= H270), D295 (= D295), D306 (= D306), D308 (= D308), D338 (= D338)
6intA Xylose isomerase from paenibacillus sp. R4 (see paper)
45% identity, 99% coverage: 3:436/440 of query aligns to 1:410/413 of 6intA
- active site: H74 (= H100), D77 (= D103), W112 (= W138), E205 (= E231), K207 (= K233), E241 (= E267), H244 (= H270), D269 (= D295), D280 (= D306), D282 (= D308), D313 (= D338)
- binding calcium ion: G166 (= G192), E178 (= E204), E205 (= E231), E241 (= E267), E241 (= E267), H244 (= H270), D269 (= D295), D280 (= D306), D282 (= D308), D313 (= D338)
9xiaA X-ray analysis of d-xylose isomerase at 1.9 angstroms: native enzyme in complex with substrate and with a mechanism-designed inactivator (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 10:371/387 of 9xiaA
- active site: H54 (= H100), D57 (= D103), M88 (≠ W138), E181 (= E231), K183 (= K233), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
- binding 3-deoxy-3-methyl-beta-D-fructofuranose: W16 (= W48), H54 (= H100), M88 (≠ W138), T90 (= T140), V135 (= V185), W137 (= W187), E181 (= E231), D245 (= D295), D287 (= D338)
- binding manganese (ii) ion: E181 (= E231), E217 (= E267), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
1xieA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 10:371/387 of 1xieA
- active site: H54 (= H100), D57 (= D103), M88 (≠ W138), E181 (= E231), K183 (= K233), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
- binding 1,5-anhydro-D-glucitol: H54 (= H100), W137 (= W187), E181 (= E231), D287 (= D338)
- binding manganese (ii) ion: E181 (= E231), E217 (= E267), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
1xidA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 10:371/387 of 1xidA
- active site: H54 (= H100), D57 (= D103), M88 (≠ W138), E181 (= E231), K183 (= K233), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
- binding ascorbic acid: W16 (= W48), H54 (= H100), W137 (= W187), E181 (= E231), D287 (= D338), K289 (= K340)
- binding manganese (ii) ion: E181 (= E231), E217 (= E267), E217 (= E267), H220 (= H270), D245 (= D295), D255 (= D308), D257 (vs. gap), D287 (= D338)
1xiiA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 8:369/385 of 1xiiA
- active site: H52 (= H100), D55 (= D103), M86 (≠ W138), E179 (= E231), K181 (= K233), E215 (= E267), H218 (= H270), D243 (= D295), D253 (= D308), D255 (vs. gap), D285 (= D338)
- binding manganese (ii) ion: E179 (= E231), E215 (= E267), E215 (= E267), H218 (= H270), D243 (= D295), D253 (= D308), D255 (vs. gap), D285 (= D338)
- binding d-xylulose: W14 (= W48), H52 (= H100), W135 (= W187), E179 (= E231), H218 (= H270), D285 (= D338)
1xihA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 8:369/385 of 1xihA
- active site: H52 (= H100), D55 (= D103), M86 (≠ W138), E179 (= E231), K181 (= K233), E215 (= E267), H218 (= H270), D243 (= D295), D253 (= D308), D255 (vs. gap), D285 (= D338)
- binding manganese (ii) ion: E179 (= E231), E215 (= E267), D243 (= D295), D285 (= D338)
- binding sorbitol: H52 (= H100), T88 (= T140), V133 (= V185), W135 (= W187), E179 (= E231), K181 (= K233), E215 (= E267), H218 (= H270), D285 (= D338)
1xicA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
29% identity, 85% coverage: 42:413/440 of query aligns to 8:369/385 of 1xicA
- active site: H52 (= H100), D55 (= D103), M86 (≠ W138), E179 (= E231), K181 (= K233), E215 (= E267), H218 (= H270), D243 (= D295), D253 (= D308), D255 (vs. gap), D285 (= D338)
- binding manganese (ii) ion: E179 (= E231), E215 (= E267), E215 (= E267), H218 (= H270), D243 (= D295), D253 (= D308), D255 (vs. gap), D285 (= D338)
- binding D-xylose: W14 (= W48), H52 (= H100), W135 (= W187), E179 (= E231), H218 (= H270), D285 (= D338)
Query Sequence
>BPHYT_RS32825 FitnessBrowser__BFirm:BPHYT_RS32825
MSYFEHIPEIRYEGPQSDNPLAYRHYDKSKKVLGKTLEEHLRIAVCYWHTFVWPGVDIFG
QGTFRRPWQQAGDAMERAQQKADSAFEFFSKLGTPYYTFHDTDVSPEGSNLKEYSENFLR
ITDYLARKQESTGIKLLWGTANLFSHPRYAAGAATSPDPEVFAFAATQVRHALDATQRLG
GDNYVLWGGREGYDTLLNTDLVRERDQLARFLHMVVDHAHKIGFKGSLLIEPKPQEPTKH
QYDYDVATVHGFLLQHGLDKEIRVNIEANHATLAGHSFHHEIATAYALGIFGSVDANRGD
PQNGWDTDQFPNSVEELTLAFYEILKHGGFTTGGMNFDSKVRRQSVDPEDLFYGHIGAID
NLALAVERAAVLIENDRLDQFKRQRYSGWDAEFGRKISSGDYSLSALAEEAMARGLNPQH
ASGHQELMENIVNQAIYSGR
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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