SitesBLAST
Comparing GFF2991 FitnessBrowser__Phaeo:GFF2991 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)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
37% identity, 98% coverage: 3:523/529 of query aligns to 5:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G9), G13 (= G11), S14 (= S12), A15 (= A13), E35 (= E32), A36 (= A33), W47 (= W59), P65 (= P77), G67 (= G79), V180 (≠ T215), A214 (= A249), G215 (= G250), A218 (≠ N253), T270 (≠ S311), Y391 (≠ F464), A424 (= A497), I435 (≠ T508), N436 (= N509)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
37% identity, 98% coverage: 3:523/529 of query aligns to 24:569/578 of 5nccA
- active site: R347 (≠ K317), L420 (≠ V378), I421 (≠ C379), S507 (≠ T461), A509 (≠ I463), G552 (= G506), Q553 (≠ N507)
- binding flavin-adenine dinucleotide: G30 (= G9), G32 (= G11), T33 (≠ S12), A34 (= A13), L53 (= L31), E54 (= E32), A55 (= A33), F74 (≠ I52), W80 (= W59), A98 (≠ P77), G100 (= G79), G105 (= G84), S106 (≠ C85), N110 (= N89), A111 (≠ G90), T112 (≠ M91), L113 (= L92), V238 (≠ T215), A278 (= A249), H282 (≠ N253), L286 (≠ I257), N508 (≠ T462), Q553 (≠ N507), T554 (= T508), G555 (≠ N509), V558 (≠ T512)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
36% identity, 98% coverage: 3:523/529 of query aligns to 84:636/654 of A0A248QE08
- TA 93:94 (≠ SA 12:13) binding
- E114 (= E32) binding
- L162 (≠ V81) binding
- S166 (≠ C85) binding
- NATL 170:173 (≠ NGML 89:92) binding
- V298 (≠ T215) binding
- C432 (≠ S335) binding
- R451 (≠ H355) binding
- Y466 (vs. gap) binding
- Q486 (≠ S377) binding
- G622 (≠ N509) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
36% identity, 98% coverage: 3:523/529 of query aligns to 8:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H355), N499 (≠ T462)
- binding flavin-adenine dinucleotide: G14 (= G9), G16 (= G11), T17 (≠ S12), A18 (= A13), L37 (= L31), E38 (= E32), A39 (= A33), F58 (≠ I52), W64 (= W59), A82 (≠ P77), G89 (= G84), S90 (≠ C85), N94 (= N89), A95 (≠ G90), T96 (≠ M91), L97 (= L92), M191 (≠ N185), V222 (≠ T215), C264 (≠ S248), A265 (= A249), G266 (= G250), H269 (≠ N253), N499 (≠ T462), A534 (= A497), Q544 (≠ N507), T545 (= T508), G546 (≠ N509)
- binding heptadecane: V377 (≠ Q357), G379 (vs. gap), M380 (≠ L359), G386 (= G365), T389 (vs. gap), Y390 (vs. gap), F393 (vs. gap), T408 (= T375), Q410 (≠ S377)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
31% identity, 99% coverage: 3:527/529 of query aligns to 2:565/565 of 5oc1A
- active site: V339 (≠ K317), N413 (= N380), A414 (vs. gap), I499 (= I463), H501 (= H465), A544 (≠ G506), H545 (≠ N507)
- binding 4-methoxybenzoic acid: Y91 (≠ G90), I356 (vs. gap), I390 (≠ L359), F396 (≠ G365), T412 (≠ C379), I499 (= I463), H501 (= H465), H545 (≠ N507)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), N11 (≠ S12), A12 (= A13), E32 (= E32), A33 (= A33), W60 (= W59), P78 (= P77), G80 (= G79), G85 (= G84), S86 (≠ C85), H90 (≠ N89), Y91 (≠ G90), V93 (≠ L92), V230 (≠ T215), S270 (= S248), A271 (= A249), G272 (= G250), F500 (= F464), H545 (≠ N507), T546 (= T508), Q547 (≠ N509), I550 (≠ T512)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
31% identity, 99% coverage: 3:527/529 of query aligns to 2:565/565 of 3fimB
- active site: V339 (≠ K317), N413 (= N380), A414 (vs. gap), I499 (= I463), H501 (= H465), A544 (≠ G506), H545 (≠ N507)
- binding flavin-adenine dinucleotide: G8 (= G9), N11 (≠ S12), A12 (= A13), E32 (= E32), A33 (= A33), W60 (= W59), P78 (= P77), G80 (= G79), G85 (= G84), S86 (≠ C85), H90 (≠ N89), Y91 (≠ G90), V93 (≠ L92), V230 (≠ T215), S270 (= S248), A271 (= A249), F500 (= F464), H501 (= H465), H545 (≠ N507), T546 (= T508), Q547 (≠ N509), I550 (≠ T512)
8bxlB Patulin synthase from penicillium expansum
31% identity, 98% coverage: 2:520/529 of query aligns to 13:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G9), G22 (= G11), T23 (≠ S12), A24 (= A13), E44 (= E32), A45 (= A33), W80 (= W59), G100 (= G79), G105 (= G84), S106 (≠ C85), R109 (≠ I88), N110 (= N89), Y111 (≠ G90), A113 (≠ L92), L253 (≠ H214), A254 (≠ T215), A288 (= A249), Q292 (≠ N253), F525 (= F464), D559 (= D496), A560 (= A497), H570 (≠ N507), P571 (≠ T508), Q572 (≠ N509), L575 (≠ T512)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
34% identity, 99% coverage: 4:527/529 of query aligns to 3:508/509 of 3t37A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I463), H446 (= H465), G487 (= G506), P488 (≠ N507)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), S11 (= S12), A12 (= A13), E32 (= E32), A33 (= A33), W58 (= W59), R77 (= R78), G78 (= G79), R79 (≠ K80), G83 (= G84), S84 (≠ C85), H88 (≠ N89), A89 (≠ G90), G91 (≠ L92), R217 (≠ H214), V218 (≠ T215), A251 (= A249), E255 (≠ N253), H445 (≠ F464), A478 (= A497), P488 (≠ N507), I489 (≠ T508), H490 (≠ N509)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
34% identity, 99% coverage: 4:527/529 of query aligns to 3:508/508 of 4ha6A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I463), H446 (= H465), G487 (= G506), P488 (≠ N507)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), S11 (= S12), A12 (= A13), E32 (= E32), A33 (= A33), W58 (= W59), R77 (= R78), G78 (= G79), G83 (= G84), S84 (≠ C85), L87 (≠ I88), H88 (≠ N89), A89 (≠ G90), M90 (= M91), G91 (≠ L92), V218 (≠ T215), A251 (= A249), G252 (= G250), E255 (≠ N253), H445 (≠ F464), A478 (= A497), P488 (≠ N507), I489 (≠ T508), H490 (≠ N509)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G90), S314 (= S335), H444 (≠ I463), H446 (= H465)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
30% identity, 100% coverage: 2:528/529 of query aligns to 2:584/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G9), G11 (= G11), I12 (≠ S12), S13 (≠ A13), E33 (= E32), A34 (= A33), W57 (vs. gap), A78 (≠ G79), G83 (= G84), G84 (≠ C85), N88 (= N89), A89 (≠ G90), V91 (≠ L92), L228 (≠ H214), V229 (≠ T215), A266 (= A249), A519 (≠ F464), H520 (= H465), D552 (= D496), I553 (≠ A497), S563 (≠ N507), P564 (≠ T508), M565 (≠ N509)
- binding p-nitrophenol: L93 (= L94), V361 (≠ A339), Y432 (≠ C379), L434 (= L381), G562 (= G506), S563 (≠ N507)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
30% identity, 100% coverage: 2:528/529 of query aligns to 1:583/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P77), L92 (= L94), Q306 (≠ H290), V360 (≠ A339), Y431 (≠ C379), L433 (= L381), N514 (≠ G460), S516 (≠ T462), N517 (≠ I463), H519 (= H465), G561 (= G506), S562 (≠ N507)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E32), A33 (= A33), W56 (vs. gap), A77 (≠ G79), G82 (= G84), G83 (≠ C85), N87 (= N89), A88 (≠ G90), V90 (≠ L92), L227 (≠ H214), V228 (≠ T215), A265 (= A249), A518 (≠ F464), H519 (= H465), D551 (= D496), I552 (≠ A497), S562 (≠ N507), P563 (≠ T508), M564 (≠ N509)
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)
30% identity, 100% coverage: 2:528/529 of query aligns to 1:583/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P77), V90 (≠ L92), Y431 (≠ C379), N517 (≠ I463), D576 (= D521), K580 (≠ S525), R583 (= R528)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E32), A33 (= A33), W56 (vs. gap), A77 (≠ G79), G82 (= G84), G83 (≠ C85), N87 (= N89), A88 (≠ G90), V90 (≠ L92), L227 (≠ H214), V228 (≠ T215), A265 (= A249), A518 (≠ F464), H519 (= H465), D551 (= D496), I552 (≠ A497), S562 (≠ N507), P563 (≠ T508), M564 (≠ N509)
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)
30% identity, 100% coverage: 2:528/529 of query aligns to 1:583/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (≠ G90), V90 (≠ L92), L354 (vs. gap), H421 (= H369), L429 (≠ S377), Y431 (≠ C379), N517 (≠ I463)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E32), A33 (= A33), W56 (vs. gap), A77 (≠ G79), G82 (= G84), G83 (≠ C85), N87 (= N89), A88 (≠ G90), V90 (≠ L92), L227 (≠ H214), V228 (≠ T215), A265 (= A249), A518 (≠ F464), H519 (= H465), D551 (= D496), I552 (≠ A497), S562 (≠ N507), P563 (≠ T508), M564 (≠ N509)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
30% identity, 100% coverage: 2:528/529 of query aligns to 1:583/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (≠ G90), L354 (vs. gap), Y431 (≠ C379), N517 (≠ I463)
- binding dihydroflavine-adenine dinucleotide: G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E32), A33 (= A33), W56 (vs. gap), G82 (= G84), G83 (≠ C85), I86 (= I88), N87 (= N89), A88 (≠ G90), V90 (≠ L92), L227 (≠ H214), V228 (≠ T215), A265 (= A249), A518 (≠ F464), H519 (= H465), D551 (= D496), I552 (≠ A497), S562 (≠ N507), M564 (≠ N509)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
30% identity, 100% coverage: 2:528/529 of query aligns to 1:583/584 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 (= W59), A88 (≠ G90), V90 (≠ L92), L354 (vs. gap), Y431 (≠ C379), N517 (≠ I463), H519 (= H465), S562 (≠ N507)
- binding dihydroflavine-adenine dinucleotide: G8 (= G9), G10 (= G11), I11 (≠ S12), S12 (≠ A13), E32 (= E32), A33 (= A33), W56 (vs. gap), A77 (≠ G79), G82 (= G84), G83 (≠ C85), I86 (= I88), N87 (= N89), A88 (≠ G90), V90 (≠ L92), L227 (≠ H214), V228 (≠ T215), A265 (= A249), A518 (≠ F464), H519 (= H465), D551 (= D496), I552 (≠ A497), S562 (≠ N507), P563 (≠ T508), M564 (≠ N509)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
33% identity, 99% coverage: 2:525/529 of query aligns to 13:528/532 of 4mjwA
- active site: I333 (≠ L337), P377 (≠ A376), N378 (≠ S377), V464 (≠ I463), H466 (= H465), V509 (≠ G506), N510 (= N507)
- binding flavin-adenine dinucleotide: G20 (= G9), G22 (= G11), S23 (= S12), E44 (= E32), A45 (= A33), W71 (= W59), R89 (= R78), A90 (≠ G79), G95 (= G84), C96 (= C85), H99 (≠ I88), N100 (= N89), S101 (≠ G90), I103 (≠ L92), R231 (≠ H214), A232 (≠ T215), T269 (≠ A249), G270 (= G250), D273 (≠ N253), Y465 (≠ F464), H466 (= H465), A500 (= A497), N510 (= N507), P511 (≠ T508), N512 (= N509), V515 (≠ T512)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
33% identity, 99% coverage: 2:523/529 of query aligns to 13:526/527 of 2jbvA
- active site: I333 (≠ L337), P377 (≠ A376), N378 (≠ S377), V464 (≠ I463), H466 (= H465), V509 (≠ G506), N510 (= N507)
- 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 (= E32), A45 (= A33), W71 (= W59), A90 (≠ G79), G95 (= G84), C96 (= C85), H99 (≠ I88), N100 (= N89), S101 (≠ G90), I103 (≠ L92), R231 (≠ H214), A232 (≠ T215), T269 (≠ A249), G270 (= G250), D273 (≠ N253), V464 (≠ I463), Y465 (≠ F464), H466 (= H465), D499 (= D496), A500 (= A497), N510 (= N507), P511 (≠ T508), N512 (= N509), V515 (≠ T512)
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)
33% identity, 99% coverage: 3:525/529 of query aligns to 6:529/531 of E4QP00
- V101 (≠ I88) mutation to H: Abolishes activity.
- M103 (≠ G90) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V378) 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 (≠ N380) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I463) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F464) 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 (= H465) mutation to A: Abolishes activity.
- N511 (= N507) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
33% identity, 99% coverage: 3:525/529 of query aligns to 2:525/525 of 4udqA
- active site: L331 (= L337), F364 (≠ C379), W365 (≠ N380), V461 (≠ I463), H463 (= H465), A506 (≠ G506), N507 (= N507)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), T11 (≠ S12), A12 (= A13), E32 (= E32), A33 (= A33), W64 (= W59), G88 (= G79), G93 (= G84), G94 (≠ C85), N98 (= N89), M99 (≠ G90), V101 (≠ L92), V229 (≠ T215), T261 (≠ S248), A262 (= A249), W462 (≠ F464), H463 (= H465), A497 (= A497), N507 (= N507), T508 (= T508), N509 (= N509), T512 (= T512)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
33% identity, 99% coverage: 2:525/529 of query aligns to 13:528/530 of 3ljpA
- active site: I333 (≠ L337), P377 (≠ A376), N378 (≠ S377), A464 (≠ I463), H466 (= H465), V509 (≠ G506), N510 (= N507)
- binding dihydroflavine-adenine dinucleotide: G22 (= G11), S23 (= S12), E44 (= E32), A45 (= A33), W71 (= W59), R89 (= R78), A90 (≠ G79), G95 (= G84), C96 (= C85), H99 (≠ I88), N100 (= N89), S101 (≠ G90), I103 (≠ L92), A232 (≠ T215), T269 (≠ A249), D273 (≠ N253), Y465 (≠ F464), H466 (= H465), D499 (= D496), A500 (= A497), N510 (= N507), P511 (≠ T508), N512 (= N509), V515 (≠ T512)
Query Sequence
>GFF2991 FitnessBrowser__Phaeo:GFF2991
MSWDYIIVGAGSAGCVLANRLSAAGQRVLLLEAGGKDNYHWVHIPMGYLYCINNPRTDWM
YRTEAEAGLNGRALIYPRGKVLGGCSSINGMLYLRGQAADYDGWRQRGLTGWGWDDVLPY
FKKSEDYVDGSSDMHGVGGEWRVENQRLHWDVLDDWMQAAAEWGLPKVTDFNTGNNEGVG
YFRVNQRSGWRMNTAKAFLRTATGENLKVETGAHTRRILIENGRAVGVEYSQGGAVKTAR
TGGEVLLSAGAINSPQILQLSGLGPEALLRDHGIAVQRDMPEVGQNLQDHLQLRCAWRLK
GAKTLNTLANSLIGKAKIAAEYAMRRSGPMSMAPSQLGAFSRSRPDLATPDLEYHVQPLT
LEAFGQPLHDFPGLTASVCNLRPESRGEVAITSADPMQAPRIAPNYLSTEGDRQVAVAAI
RQARAIMGQEAMQRYAPVEMKPGGGSDEAADLMQAAGAIGTTIFHPTCTLRMGAEEAAPV
DGALRLRGVGGLRVVDASVMPVIPSGNTNAPTIMIAEKAADMILSDHRG
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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