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Comparing Echvi_1876 FitnessBrowser__Cola:Echvi_1876 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)
4xkmA Crystal structure of xylose isomerase from an human intestinal tract microbe bacteroides thetaiotaomicron
69% identity, 100% coverage: 3:437/437 of query aligns to 1:435/435 of 4xkmA
- active site: F23 (= F25), E29 (≠ N31), H100 (= H102), D103 (= D105), W138 (= W140), E231 (= E233), K233 (= K235), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
- binding manganese (ii) ion: E231 (= E233), E267 (= E269), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
5nhcA Crystal structure of xylose isomerase from piromyces e2 in complex with two co2+ ions and xylulose (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nhcA
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding cobalt (ii) ion: E232 (= E233), E268 (= E269), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding 4-hydroxyproline: G290 (= G291), L292 (= L293), G328 (≠ A329), G330 (= G331), V332 (≠ Q333)
- binding d-xylulose: W49 (= W50), H101 (= H102), W188 (= W189), E232 (= E233), E268 (= E269), H271 (= H272), D339 (= D340)
5nhaA Crystal structure of xylose isomerase from piromyces sp. E2 in complex with two mn2+ ions and sorbitol (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nhaA
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding manganese (ii) ion: E232 (= E233), E268 (= E269), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding sorbitol: W49 (= W50), H101 (= H102), W188 (= W189), E232 (= E233), D339 (= D340)
5nh9A Crystal structure of xylose isomerase from piromyces e2 in complex with two mn2+ ions and xylose (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nh9A
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding manganese (ii) ion: E232 (= E233), E268 (= E269), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding D-xylose: W49 (= W50), H101 (= H102), W188 (= W189), E232 (= E233), E268 (= E269), H271 (= H272), D339 (= D340)
- binding beta-D-xylopyranose: G63 (= G64), K65 (= K66), S66 (≠ T67), K203 (= K204), K206 (≠ T207), H257 (≠ Y258), D288 (= D289), A289 (= A290)
5nh7A Crystal structure of xylose isomerase from piromyces e2 in complex with two mg2+ ions and xylose (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nh7A
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding magnesium ion: E232 (= E233), E268 (= E269), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding D-xylose: W49 (= W50), H101 (= H102), W188 (= W189), E232 (= E233), E268 (= E269), H271 (= H272), D339 (= D340)
- binding beta-D-xylopyranose: G63 (= G64), K65 (= K66), S66 (≠ T67)
- binding alpha-D-xylopyranose: P21 (= P22), D40 (≠ E41), Y97 (= Y98), K136 (= K137), E350 (≠ D351)
5nh6A Crystal structure of xylose isomerase from piromyces e2 complexed with one mg2+ ion and xylitol (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nh6A
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding magnesium ion: E232 (= E233), E268 (= E269), D296 (= D297), D339 (= D340)
- binding Xylitol: W49 (= W50), H101 (= H102), W188 (= W189), E232 (= E233), E268 (= E269), H271 (= H272), D339 (= D340)
5nh5A Crystal structure of native xylose isomerase from piromyces e2 (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nh5A
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding calcium ion: E232 (= E233), E268 (= E269), D296 (= D297), D339 (= D340)
- binding fe (ii) ion: E232 (= E233), E268 (= E269), D296 (= D297), D339 (= D340)
- binding magnesium ion: E232 (= E233), E268 (= E269), D296 (= D297), D339 (= D340)
5nh4A Crystal structure of xylose isomerase from piromyces e2 in complex with one mg2+ ions and glycerol (see paper)
65% identity, 100% coverage: 2:436/437 of query aligns to 1:435/436 of 5nh4A
- active site: H101 (= H102), D104 (= D105), W139 (= W140), E232 (= E233), K234 (= K235), E268 (= E269), H271 (= H272), D296 (= D297), D307 (= D308), D309 (= D310), D339 (= D340)
- binding magnesium ion: E232 (= E233), E268 (= E269), D296 (= D297), D339 (= D340)
5yn3A Crystal structure of xylose isomerase from piromyces sp. E2 (see paper)
65% identity, 99% coverage: 3:436/437 of query aligns to 1:434/435 of 5yn3A
- active site: H100 (= H102), D103 (= D105), W138 (= W140), E231 (= E233), K233 (= K235), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
- binding glycerol: H100 (= H102), W187 (= W189), E231 (= E233), D295 (= D297)
- binding manganese (ii) ion: E231 (= E233), E267 (= E269), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
P00944 Xylose isomerase; D-xylulose keto-isomerase; EC 5.3.1.5 from Escherichia coli (strain K12) (see paper)
51% identity, 100% coverage: 3:437/437 of query aligns to 2:437/440 of P00944
- H101 (= H102) active site
1a0cA Xylose isomerase from thermoanaerobacterium thermosulfurigenes
50% identity, 99% coverage: 5:437/437 of query aligns to 3:435/437 of 1a0cA
- active site: H100 (= H102), D103 (= D105), W138 (= W140), E231 (= E233), K233 (= K235), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
- binding cobalt (ii) ion: E231 (= E233), E267 (= E269), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
1a0eA Xylose isomerase from thermotoga neapolitana
50% identity, 99% coverage: 5:437/437 of query aligns to 3:435/443 of 1a0eA
- active site: H100 (= H102), D103 (= D105), W138 (= W140), E231 (= E233), K233 (= K235), E267 (= E269), H270 (= H272), D295 (= D297), D306 (= D308), D308 (= D310), D338 (= D340)
- binding cobalt (ii) ion: E231 (= E233), E267 (= E269), E267 (= E269), H270 (= H272), D295 (= D297), D308 (= D310), D338 (= D340)
1a0dA Xylose isomerase from bacillus stearothermophilus
50% identity, 99% coverage: 5:437/437 of query aligns to 2:433/437 of 1a0dA
- active site: H98 (= H102), D101 (= D105), W136 (= W140), E229 (= E233), K231 (= K235), E265 (= E269), H268 (= H272), D293 (= D297), D304 (= D308), D306 (= D310), D336 (= D340)
- binding manganese (ii) ion: E229 (= E233), E265 (= E269), E265 (= E269), H268 (= H272), D293 (= D297), D304 (= D308), D306 (= D310), D336 (= D340)
6intA Xylose isomerase from paenibacillus sp. R4 (see paper)
46% identity, 99% coverage: 5:437/437 of query aligns to 1:410/413 of 6intA
- active site: H74 (= H102), D77 (= D105), W112 (= W140), E205 (= E233), K207 (= K235), E241 (= E269), H244 (= H272), D269 (= D297), D280 (= D308), D282 (= D310), D313 (= D340)
- binding calcium ion: G166 (= G194), E178 (= E206), E205 (= E233), E241 (= E269), E241 (= E269), H244 (= H272), D269 (= D297), D280 (= D308), D282 (= D310), D313 (= D340)
1gw9A Tri-iodide derivative of xylose isomerase from streptomyces rubiginosus (see paper)
31% identity, 73% coverage: 44:361/437 of query aligns to 8:305/384 of 1gw9A
- active site: H52 (= H102), D55 (= D105), M86 (≠ W140), E179 (= E233), K181 (= K235), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding calcium ion: E179 (= E233), E215 (= E269), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding beta-L-xylopyranose: H52 (= H102), F92 (= F146), W135 (= W189), E179 (= E233), D285 (= D340)
1xiiA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
31% identity, 73% coverage: 44:361/437 of query aligns to 8:305/385 of 1xiiA
- active site: H52 (= H102), D55 (= D105), M86 (≠ W140), E179 (= E233), K181 (= K235), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding manganese (ii) ion: E179 (= E233), E215 (= E269), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding d-xylulose: W14 (= W50), H52 (= H102), W135 (= W189), E179 (= E233), H218 (= H272), D285 (= D340)
1xihA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
31% identity, 73% coverage: 44:361/437 of query aligns to 8:305/385 of 1xihA
- active site: H52 (= H102), D55 (= D105), M86 (≠ W140), E179 (= E233), K181 (= K235), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding manganese (ii) ion: E179 (= E233), E215 (= E269), D243 (= D297), D285 (= D340)
- binding sorbitol: H52 (= H102), T88 (= T142), V133 (= V187), W135 (= W189), E179 (= E233), K181 (= K235), E215 (= E269), H218 (= H272), D285 (= D340)
1xicA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
31% identity, 73% coverage: 44:361/437 of query aligns to 8:305/385 of 1xicA
- active site: H52 (= H102), D55 (= D105), M86 (≠ W140), E179 (= E233), K181 (= K235), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding manganese (ii) ion: E179 (= E233), E215 (= E269), E215 (= E269), H218 (= H272), D243 (= D297), D253 (= D310), D255 (vs. gap), D285 (= D340)
- binding D-xylose: W14 (= W50), H52 (= H102), W135 (= W189), E179 (= E233), H218 (= H272), D285 (= D340)
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)
31% identity, 73% coverage: 44:361/437 of query aligns to 10:307/387 of 9xiaA
- active site: H54 (= H102), D57 (= D105), M88 (≠ W140), E181 (= E233), K183 (= K235), E217 (= E269), H220 (= H272), D245 (= D297), D255 (= D310), D257 (vs. gap), D287 (= D340)
- binding 3-deoxy-3-methyl-beta-D-fructofuranose: W16 (= W50), H54 (= H102), M88 (≠ W140), T90 (= T142), V135 (= V187), W137 (= W189), E181 (= E233), D245 (= D297), D287 (= D340)
- binding manganese (ii) ion: E181 (= E233), E217 (= E269), E217 (= E269), H220 (= H272), D245 (= D297), D255 (= D310), D257 (vs. gap), D287 (= D340)
1xieA Modes of binding substrates and their analogues to the enzyme d-xylose isomerase (see paper)
31% identity, 73% coverage: 44:361/437 of query aligns to 10:307/387 of 1xieA
- active site: H54 (= H102), D57 (= D105), M88 (≠ W140), E181 (= E233), K183 (= K235), E217 (= E269), H220 (= H272), D245 (= D297), D255 (= D310), D257 (vs. gap), D287 (= D340)
- binding 1,5-anhydro-D-glucitol: H54 (= H102), W137 (= W189), E181 (= E233), D287 (= D340)
- binding manganese (ii) ion: E181 (= E233), E217 (= E269), E217 (= E269), H220 (= H272), D245 (= D297), D255 (= D310), D257 (vs. gap), D287 (= D340)
Query Sequence
>Echvi_1876 FitnessBrowser__Cola:Echvi_1876
MSKTYFPGIEKIKYEGRDSKNPFAFKFYDENKVVAGKTMKEHFKFAIAYWHSFNATGDDP
FGPGTKTFVWDQAEDALQRAKDKMDAAFEFITKIGAPYYCFHDVDLIDEGSTIEEYESRM
KAITEYAKQKQVETGVKLLWGTANVFSNPRYMNGASTNPDFDVVSWAATQVKNSIDATIA
LGGENYVFWGGREGYMSLLNTDMKRETEHLAKFLTMARDYGRKQGFKGNFLIEPKPMEPT
KHQYDYDSATVVGFLRHYGLDKDFKLNIEVNHATLAGHTFQHELQVAADAGLLGSIDANR
GDYQNGWDTDQFALNLQELTESLLVILEAGGLQGGGVNFDAKLRRNSTDLDDLFHAHIGS
MDAFARALLIANDILEQSEYKALRKKRYASFDGGKGKEFEEGKLTLEDLREHAIATGEPA
STSGKQEMYENIINQYI
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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