SitesBLAST
Comparing GFF3501 FitnessBrowser__Phaeo:GFF3501 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)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
38% identity, 98% coverage: 4:532/538 of query aligns to 6:451/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G9), G13 (= G11), S14 (= S12), A15 (= A13), E35 (= E33), A36 (= A34), W47 (= W62), P65 (= P80), G67 (= G82), V180 (≠ A224), A214 (≠ G258), G215 (= G259), A218 (≠ N262), T270 (= T341), Y391 (= Y472), A424 (= A505), I435 (≠ T516), N436 (= N517)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
38% identity, 99% coverage: 4:533/538 of query aligns to 25:571/578 of 5nccA
- active site: R347 (vs. gap), L420 (≠ I387), I421 (≠ C388), S507 (≠ I471), A509 (≠ H473), G552 (= G514), Q553 (≠ N515)
- binding flavin-adenine dinucleotide: G30 (= G9), G32 (= G11), T33 (≠ S12), A34 (= A13), L53 (= L32), E54 (= E33), A55 (= A34), F74 (≠ L53), W80 (= W62), A98 (≠ P80), G100 (= G82), G105 (= G87), S106 (= S88), N110 (= N92), A111 (= A93), T112 (≠ M94), L113 (= L95), V238 (≠ A224), A278 (≠ G258), H282 (≠ N262), L286 (= L266), N508 (≠ Y472), Q553 (≠ N515), T554 (= T516), G555 (≠ N517), V558 (≠ T520)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
38% identity, 99% coverage: 4:533/538 of query aligns to 85:638/654 of A0A248QE08
- TA 93:94 (≠ SA 12:13) binding
- E114 (= E33) binding
- L162 (≠ G84) binding
- S166 (= S88) binding
- NATL 170:173 (≠ NAML 92:95) binding
- V298 (≠ A224) binding
- C432 (≠ A344) binding
- R451 (≠ H364) binding
- Y466 (vs. gap) binding
- Q486 (≠ H386) binding
- G622 (≠ N517) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
38% identity, 99% coverage: 4:533/538 of query aligns to 9:562/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H364), N499 (≠ Y472)
- binding flavin-adenine dinucleotide: G14 (= G9), G16 (= G11), T17 (≠ S12), A18 (= A13), L37 (= L32), E38 (= E33), A39 (= A34), F58 (≠ L53), W64 (= W62), A82 (≠ P80), G89 (= G87), S90 (= S88), N94 (= N92), A95 (= A93), T96 (≠ M94), L97 (= L95), M191 (≠ T188), V222 (≠ A224), C264 (≠ S257), A265 (≠ G258), G266 (= G259), H269 (≠ N262), N499 (≠ Y472), A534 (= A505), Q544 (≠ N515), T545 (= T516), G546 (≠ N517)
- binding heptadecane: V377 (= V366), G379 (≠ S368), M380 (≠ I369), G386 (vs. gap), T389 (vs. gap), Y390 (vs. gap), F393 (vs. gap), T408 (≠ S384), Q410 (≠ H386)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
33% identity, 99% coverage: 2:533/538 of query aligns to 1:563/565 of 5oc1A
- active site: V339 (≠ R326), N413 (≠ I387), A414 (≠ C388), I499 (= I471), H501 (= H473), A544 (≠ G514), H545 (≠ N515)
- binding 4-methoxybenzoic acid: Y91 (≠ A93), I356 (≠ F343), I390 (≠ H364), F396 (≠ V370), T412 (≠ H386), I499 (= I471), H501 (= H473), H545 (≠ N515)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), N11 (≠ S12), A12 (= A13), E32 (= E33), A33 (= A34), W60 (= W62), P78 (= P80), G80 (= G82), G85 (= G87), S86 (= S88), H90 (≠ N92), Y91 (≠ A93), V93 (≠ L95), V230 (≠ A224), S270 (= S257), A271 (≠ G258), G272 (= G259), F500 (≠ Y472), H545 (≠ N515), T546 (= T516), Q547 (≠ N517), I550 (≠ T520)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 99% coverage: 2:533/538 of query aligns to 1:563/565 of 3fimB
- active site: V339 (≠ R326), N413 (≠ I387), A414 (≠ C388), I499 (= I471), H501 (= H473), A544 (≠ G514), H545 (≠ N515)
- binding flavin-adenine dinucleotide: G8 (= G9), N11 (≠ S12), A12 (= A13), E32 (= E33), A33 (= A34), W60 (= W62), P78 (= P80), G80 (= G82), G85 (= G87), S86 (= S88), H90 (≠ N92), Y91 (≠ A93), V93 (≠ L95), V230 (≠ A224), S270 (= S257), A271 (≠ G258), F500 (≠ Y472), H501 (= H473), H545 (≠ N515), T546 (= T516), Q547 (≠ N517), I550 (≠ T520)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
35% identity, 99% coverage: 2:536/538 of query aligns to 13:531/532 of 4mjwA
- active site: I333 (≠ T334), P377 (≠ I387), N378 (≠ C388), V464 (≠ I471), H466 (= H473), V509 (≠ G514), N510 (= N515)
- binding flavin-adenine dinucleotide: G20 (= G9), G22 (= G11), S23 (= S12), E44 (= E33), A45 (= A34), W71 (= W62), R89 (= R81), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ L95), R231 (≠ Q223), A232 (= A224), T269 (≠ G258), G270 (= G259), D273 (≠ N262), Y465 (= Y472), H466 (= H473), A500 (= A505), N510 (= N515), P511 (≠ T516), N512 (= N517), V515 (≠ T520)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
35% identity, 99% coverage: 2:532/538 of query aligns to 13:527/527 of 2jbvA
- active site: I333 (≠ T334), P377 (≠ I387), N378 (≠ C388), V464 (≠ I471), H466 (= H473), V509 (≠ G514), N510 (= N515)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: G22 (= G11), S23 (= S12), E44 (= E33), A45 (= A34), W71 (= W62), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ L95), R231 (≠ Q223), A232 (= A224), T269 (≠ G258), G270 (= G259), D273 (≠ N262), V464 (≠ I471), Y465 (= Y472), H466 (= H473), D499 (= D504), A500 (= A505), N510 (= N515), P511 (≠ T516), N512 (= N517), V515 (≠ T520)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
35% identity, 99% coverage: 2:534/538 of query aligns to 13:529/530 of 3ljpA
- active site: I333 (≠ T334), P377 (≠ I387), N378 (≠ C388), A464 (≠ I471), H466 (= H473), V509 (≠ G514), N510 (= N515)
- binding dihydroflavine-adenine dinucleotide: G22 (= G11), S23 (= S12), E44 (= E33), A45 (= A34), W71 (= W62), R89 (= R81), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ L95), A232 (= A224), T269 (≠ G258), D273 (≠ N262), Y465 (= Y472), H466 (= H473), D499 (= D504), A500 (= A505), N510 (= N515), P511 (≠ T516), N512 (= N517), V515 (≠ T520)
8bxlB Patulin synthase from penicillium expansum
33% identity, 99% coverage: 4:533/538 of query aligns to 15:588/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G9), G22 (= G11), T23 (≠ S12), A24 (= A13), E44 (= E33), A45 (= A34), W80 (= W62), G100 (= G82), G105 (= G87), S106 (= S88), R109 (≠ I91), N110 (= N92), Y111 (≠ A93), A113 (≠ L95), L253 (≠ Q223), A254 (= A224), A288 (≠ G258), Q292 (≠ N262), F525 (≠ Y472), D559 (= D504), A560 (= A505), H570 (≠ N515), P571 (≠ T516), Q572 (≠ N517), L575 (≠ T520)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
35% identity, 98% coverage: 4:531/538 of query aligns to 3:523/525 of 4udqA
- active site: L331 (≠ W329), F364 (≠ I387), W365 (≠ C388), V461 (≠ I471), H463 (= H473), A506 (≠ G514), N507 (= N515)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), T11 (≠ S12), A12 (= A13), E32 (= E33), A33 (= A34), W64 (= W62), G88 (= G82), G93 (= G87), G94 (≠ S88), N98 (= N92), M99 (≠ A93), V101 (≠ L95), V229 (≠ A224), T261 (≠ S257), A262 (≠ G258), W462 (≠ Y472), H463 (= H473), A497 (= A505), N507 (= N515), T508 (= T516), N509 (= N517), T512 (= T520)
E4QP00 5-(hydroxymethyl)furfural oxidase; 5-hydroxymethylfurfural oxidase; HMFO; Thiol oxidase; EC 1.1.3.47; EC 1.8.3.- from Methylovorus sp. (strain MP688) (see paper)
35% identity, 98% coverage: 4:531/538 of query aligns to 7:527/531 of E4QP00
- V101 (≠ I91) mutation to H: Abolishes activity.
- M103 (≠ A93) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ H386) mutation to K: 1.6-fold reduction in catalytic efficiency on vanillyl alcohol. Shows significantly improved activity on the aldehyde 5-formyl-2-furancarboxylate, which results in a better 5-hydroxymethylfurfural to 2,5-furandicarboxylate conversion.; mutation to R: 1.4-fold reduction in catalytic efficiency on vanillyl alcohol. Shows significantly improved activity on the aldehyde 5-formyl-2-furancarboxylate, which results in a better 5-hydroxymethylfurfural to 2,5-furandicarboxylate conversion. Displays a catalytic efficiency toward 5-formyl-2-furancarboxylate that is over 1000-fold higher than that for wild-type; when associated with F-466.
- W369 (≠ C388) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I471) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ Y472) mutation to A: 39-fold reduction in catalytic efficiency on vanillyl alcohol. In contrast to wild-type, is active on secondary alcohols, such as (S)-1-phenylethanol, and is strictly enantionselective as this mutant has no activity on (R)-1-phenylethanol. Shows increased activity on the aldehyde 5-formyl-2-furancarboxylate.; mutation to F: 3.4-fold reduction in catalytic efficiency on vanillyl alcohol. In contrast to wild-type, is active on secondary alcohols, such as (S)-1-phenylethanol, and is strictly enantionselective as this mutant has no activity on (R)-1-phenylethanol. Shows increased activity on the aldehyde 5-formyl-2-furancarboxylate. Displays a catalytic efficiency toward 5-formyl-2-furancarboxylate that is over 1000-fold higher than that for wild-type; when associated with R-367.
- H467 (= H473) mutation to A: Abolishes activity.
- N511 (= N515) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
36% identity, 98% coverage: 4:528/538 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ I387), G361 (≠ C388), H444 (≠ I471), H446 (= H473), G487 (= G514), P488 (≠ N515)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), S11 (= S12), A12 (= A13), E32 (= E33), A33 (= A34), W58 (= W62), R77 (= R81), G78 (= G82), G83 (= G87), S84 (= S88), L87 (≠ I91), H88 (≠ N92), A89 (= A93), M90 (= M94), G91 (≠ L95), V218 (≠ A224), A251 (≠ G258), G252 (= G259), E255 (≠ N262), H445 (≠ Y472), A478 (= A505), P488 (≠ N515), I489 (≠ T516), H490 (≠ N517)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (= A93), S314 (≠ A344), H444 (≠ I471), H446 (= H473)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
36% identity, 98% coverage: 4:528/538 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ I387), G361 (≠ C388), H444 (≠ I471), H446 (= H473), G487 (= G514), P488 (≠ N515)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), S11 (= S12), A12 (= A13), E32 (= E33), A33 (= A34), W58 (= W62), R77 (= R81), G78 (= G82), R79 (≠ K83), G83 (= G87), S84 (= S88), H88 (≠ N92), A89 (= A93), G91 (≠ L95), R217 (≠ Q223), V218 (≠ A224), A251 (≠ G258), E255 (≠ N262), H445 (≠ Y472), A478 (= A505), P488 (≠ N515), I489 (≠ T516), H490 (≠ N517)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 4:579/584 of 7aa2A
- binding 3-ethyl-2-[(2z)-2-(3-ethyl-6-sulfo-1,3-benzothiazol-2(3h)-ylidene)hydrazino]-6-sulfo-3h-1,3-benzothiazol-1-ium: W52 (≠ M52), A88 (= A93), V90 (≠ L95), L354 (≠ F343), Y431 (≠ C388), N517 (vs. gap), H519 (vs. gap), S562 (≠ N515)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E33), A33 (= A34), W56 (≠ R56), A77 (≠ G82), G82 (= G87), G83 (≠ S88), I86 (= I91), N87 (= N92), A88 (= A93), V90 (≠ L95), L227 (≠ Q223), V228 (≠ A224), A265 (≠ G258), A518 (vs. gap), H519 (vs. gap), D551 (= D504), I552 (≠ A505), S562 (≠ N515), P563 (≠ T516), M564 (≠ N517)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 5:580/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G9), G11 (= G11), I12 (≠ S12), S13 (≠ A13), E33 (= E33), A34 (= A34), W57 (≠ R56), A78 (≠ G82), G83 (= G87), G84 (≠ S88), N88 (= N92), A89 (= A93), V91 (≠ L95), L228 (≠ Q223), V229 (≠ A224), A266 (≠ G258), A519 (vs. gap), H520 (vs. gap), D552 (= D504), I553 (≠ A505), S563 (≠ N515), P564 (≠ T516), M565 (≠ N517)
- binding p-nitrophenol: L93 (≠ I97), V361 (≠ F349), Y432 (≠ C388), L434 (= L390), G562 (= G514), S563 (≠ N515)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 4:579/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P80), L92 (≠ I97), Q306 (≠ H299), V360 (≠ F349), Y431 (≠ C388), L433 (= L390), N514 (≠ H473), S516 (vs. gap), N517 (vs. gap), H519 (vs. gap), G561 (= G514), S562 (≠ N515)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E33), A33 (= A34), W56 (≠ R56), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ L95), L227 (≠ Q223), V228 (≠ A224), A265 (≠ G258), A518 (vs. gap), H519 (vs. gap), D551 (= D504), I552 (≠ A505), S562 (≠ N515), P563 (≠ T516), M564 (≠ N517)
6ze5A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 2-(1h-indol-3-yl)-n-[(1-methyl-1h-pyrrol-2-yl) methyl]ethanamine (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 4:579/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P80), V90 (≠ L95), Y431 (≠ C388), N517 (vs. gap), D576 (= D529)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E33), A33 (= A34), W56 (≠ R56), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ L95), L227 (≠ Q223), V228 (≠ A224), A265 (≠ G258), A518 (vs. gap), H519 (vs. gap), D551 (= D504), I552 (≠ A505), S562 (≠ N515), P563 (≠ T516), M564 (≠ N517)
Sites not aligning to the query:
6ze4A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-oxo-n-[(1s)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl) butanamide (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 4:579/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (= A93), V90 (≠ L95), L354 (≠ F343), H421 (= H378), L429 (≠ H386), Y431 (≠ C388), N517 (vs. gap)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E33), A33 (= A34), W56 (≠ R56), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ L95), L227 (≠ Q223), V228 (≠ A224), A265 (≠ G258), A518 (vs. gap), H519 (vs. gap), D551 (= D504), I552 (≠ A505), S562 (≠ N515), P563 (≠ T516), M564 (≠ N517)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
31% identity, 98% coverage: 5:532/538 of query aligns to 4:579/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (= A93), L354 (≠ F343), Y431 (≠ C388), N517 (vs. gap)
- binding dihydroflavine-adenine dinucleotide: G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E33), A33 (= A34), W56 (≠ R56), G82 (= G87), G83 (≠ S88), I86 (= I91), N87 (= N92), A88 (= A93), V90 (≠ L95), L227 (≠ Q223), V228 (≠ A224), A265 (≠ G258), A518 (vs. gap), H519 (vs. gap), D551 (= D504), I552 (≠ A505), S562 (≠ N515), M564 (≠ N517)
Query Sequence
>GFF3501 FitnessBrowser__Phaeo:GFF3501
MEADYVIVGGGSAGSTLASRLSEDPDVTVCLLEAGGRGDGLLVRAPAAVVAMLPGRPKIN
NWAYETVPQPGLNGRRGYQPRGKGLGGSSAINAMLYIRGHSKDYDEWAALGCEGWDWQSV
LPYFRKSENNERGDDALHGAAGPLQVSNQKSPRPITDAFVKAGRSLQIRHREDFNSGDNE
GIGHYQVTQFHRDDRNGERCSAAAAYLHPVMDRPNLTVITRAQASSVAFEGKRAVGVRYS
QGGRAHMVRARREVILSGGAFNSPQLLQLSGVGRPDDICPHGIDMVHELPGVGQNLQDHL
DFTLAYKSRDRDNFGISLPGSVSLLRHIWNWRKTGRGMIATPFAEGAAFLKTDPNKKRAD
VQLHFVISIVDDHARKLHMGHGFSCHICVLRPKSRGSVGLNSADPKAAPRIDPQFLADPE
DLAVLIKGVRKTRQIMAAEPLAGYVHRELFINGEPDDAALEQHIRARADTIYHPVGTCKM
GTDPLSVVDPSLRVHGLQGLRVVDASVMPRLIGGNTNAPTIMIAEKAADIIRGAWARS
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