SitesBLAST
Comparing Pf6N2E2_389 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_389 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)
34% identity, 97% coverage: 7:510/521 of query aligns to 3:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G15), G13 (= G17), S14 (≠ T18), A15 (= A19), E35 (= E39), A36 (= A40), W47 (= W65), P65 (≠ N83), G67 (= G85), V180 (= V227), A214 (≠ M261), G215 (= G262), A218 (≠ N265), T270 (≠ V317), Y391 (≠ W451), A424 (= A484), I435 (≠ T495), N436 (≠ M496)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
33% identity, 96% coverage: 8:507/521 of query aligns to 1:501/508 of 4ha6A
- active site: F360 (≠ A367), G361 (= G368), H444 (≠ Y450), H446 (= H452), G487 (= G493), P488 (≠ N494)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), S11 (≠ T18), A12 (= A19), E32 (= E39), A33 (= A40), W58 (= W65), R77 (≠ M84), G78 (= G85), G83 (= G90), S84 (≠ G91), L87 (≠ I94), H88 (≠ N95), A89 (≠ V96), M90 (= M97), G91 (≠ V98), V218 (= V227), A251 (≠ M261), G252 (= G262), E255 (≠ N265), H445 (≠ W451), A478 (= A484), P488 (≠ N494), I489 (≠ T495), H490 (≠ M496)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ V96), S314 (≠ C322), H444 (≠ Y450), H446 (= H452)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
33% identity, 96% coverage: 8:507/521 of query aligns to 1:501/509 of 3t37A
- active site: F360 (≠ A367), G361 (= G368), H444 (≠ Y450), H446 (= H452), G487 (= G493), P488 (≠ N494)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), S11 (≠ T18), A12 (= A19), E32 (= E39), A33 (= A40), W58 (= W65), R77 (≠ M84), G78 (= G85), R79 (≠ K86), G83 (= G90), S84 (≠ G91), H88 (≠ N95), A89 (≠ V96), G91 (≠ V98), R217 (≠ L226), V218 (= V227), A251 (≠ M261), E255 (≠ N265), H445 (≠ W451), A478 (= A484), P488 (≠ N494), I489 (≠ T495), H490 (≠ M496)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
34% identity, 98% coverage: 6:515/521 of query aligns to 11:531/532 of 4mjwA
- active site: I333 (vs. gap), P377 (≠ A367), N378 (≠ G368), V464 (≠ Y450), H466 (= H452), V509 (≠ G493), N510 (= N494)
- binding flavin-adenine dinucleotide: G20 (= G15), G22 (= G17), S23 (≠ T18), E44 (= E39), A45 (= A40), W71 (= W65), R89 (vs. gap), A90 (≠ G85), G95 (= G90), C96 (≠ G91), H99 (≠ I94), N100 (= N95), S101 (≠ V96), I103 (≠ V98), R231 (≠ L226), A232 (≠ V227), T269 (≠ M261), G270 (= G262), D273 (≠ N265), Y465 (≠ W451), H466 (= H452), A500 (= A484), N510 (= N494), P511 (≠ T495), N512 (≠ M496), V515 (≠ C499)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 98% coverage: 6:514/521 of query aligns to 11:530/530 of 3ljpA
- active site: I333 (vs. gap), P377 (≠ A367), N378 (≠ G368), A464 (≠ Y450), H466 (= H452), V509 (≠ G493), N510 (= N494)
- binding dihydroflavine-adenine dinucleotide: G22 (= G17), S23 (≠ T18), E44 (= E39), A45 (= A40), W71 (= W65), R89 (vs. gap), A90 (≠ G85), G95 (= G90), C96 (≠ G91), H99 (≠ I94), N100 (= N95), S101 (≠ V96), I103 (≠ V98), A232 (≠ V227), T269 (≠ M261), D273 (≠ N265), Y465 (≠ W451), H466 (= H452), D499 (= D483), A500 (= A484), N510 (= N494), P511 (≠ T495), N512 (≠ M496), V515 (≠ C499)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
34% identity, 97% coverage: 6:510/521 of query aligns to 11:526/527 of 2jbvA
- active site: I333 (vs. gap), P377 (≠ A367), N378 (≠ G368), V464 (≠ Y450), H466 (= H452), V509 (≠ G493), N510 (= N494)
- 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 (= G17), S23 (≠ T18), E44 (= E39), A45 (= A40), W71 (= W65), A90 (≠ G85), G95 (= G90), C96 (≠ G91), H99 (≠ I94), N100 (= N95), S101 (≠ V96), I103 (≠ V98), R231 (≠ L226), A232 (≠ V227), T269 (≠ M261), G270 (= G262), D273 (≠ N265), V464 (≠ Y450), Y465 (≠ W451), H466 (= H452), D499 (= D483), A500 (= A484), N510 (= N494), P511 (≠ T495), N512 (≠ M496), V515 (≠ C499)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
32% identity, 98% coverage: 7:516/521 of query aligns to 22:575/578 of 5nccA
- active site: R347 (≠ Q315), L420 (≠ A367), I421 (≠ G368), S507 (≠ Y450), A509 (≠ H452), G552 (= G493), Q553 (≠ N494)
- binding flavin-adenine dinucleotide: G30 (= G15), G32 (= G17), T33 (= T18), A34 (= A19), L53 (≠ I38), E54 (= E39), A55 (= A40), F74 (≠ L59), W80 (= W65), A98 (≠ N83), G100 (= G85), G105 (= G90), S106 (≠ G91), N110 (= N95), A111 (≠ V96), T112 (≠ M97), L113 (≠ V98), V238 (= V227), A278 (≠ M261), H282 (≠ N265), L286 (≠ V269), N508 (≠ W451), Q553 (≠ N494), T554 (= T495), G555 (≠ M496), V558 (≠ C499)
6yrvAAA structure of fap after illumination at 100k (see paper)
31% identity, 98% coverage: 7:516/521 of query aligns to 6:566/573 of 6yrvAAA
- binding carbon dioxide: R375 (vs. gap), N499 (≠ W451)
- binding flavin-adenine dinucleotide: G14 (= G15), G16 (= G17), T17 (= T18), A18 (= A19), L37 (≠ I38), E38 (= E39), A39 (= A40), F58 (≠ L59), W64 (= W65), A82 (≠ N83), G89 (= G90), S90 (≠ G91), N94 (= N95), A95 (≠ V96), T96 (≠ M97), L97 (≠ V98), M191 (≠ R196), V222 (= V227), C264 (≠ S260), A265 (≠ M261), G266 (= G262), H269 (≠ N265), N499 (≠ W451), A534 (= A484), Q544 (≠ N494), T545 (= T495), G546 (≠ M496)
- binding heptadecane: V377 (vs. gap), G379 (vs. gap), M380 (vs. gap), G386 (≠ L339), T389 (≠ C342), Y390 (≠ Q343), F393 (= F346), T408 (= T364), Q410 (≠ F366)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
31% identity, 98% coverage: 7:516/521 of query aligns to 82:642/654 of A0A248QE08
- TA 93:94 (= TA 18:19) binding
- E114 (= E39) binding
- L162 (≠ G87) binding
- S166 (≠ G91) binding
- NATL 170:173 (≠ NVMV 95:98) binding
- V298 (= V227) binding
- C432 (= C322) binding
- R451 (vs. gap) binding
- Y466 (≠ Q343) binding
- Q486 (≠ F366) binding
- G622 (≠ M496) binding
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
30% identity, 97% coverage: 8:514/521 of query aligns to 1:565/565 of 5oc1A
- active site: V339 (vs. gap), N413 (vs. gap), A414 (≠ G368), I499 (≠ Y450), H501 (= H452), A544 (≠ G493), H545 (≠ N494)
- binding 4-methoxybenzoic acid: Y91 (≠ V96), I356 (≠ L340), I390 (vs. gap), F396 (vs. gap), T412 (vs. gap), I499 (≠ Y450), H501 (= H452), H545 (≠ N494)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), N11 (≠ T18), A12 (= A19), E32 (= E39), A33 (= A40), W60 (= W65), P78 (≠ N83), G80 (= G85), G85 (= G90), S86 (≠ G91), H90 (≠ N95), Y91 (≠ V96), V93 (= V98), V230 (= V227), S270 (= S260), A271 (≠ M261), G272 (= G262), F500 (≠ W451), H545 (≠ N494), T546 (= T495), Q547 (≠ M496), I550 (≠ C499)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
30% identity, 97% coverage: 8:514/521 of query aligns to 1:565/565 of 3fimB
- active site: V339 (vs. gap), N413 (vs. gap), A414 (≠ G368), I499 (≠ Y450), H501 (= H452), A544 (≠ G493), H545 (≠ N494)
- binding flavin-adenine dinucleotide: G8 (= G15), N11 (≠ T18), A12 (= A19), E32 (= E39), A33 (= A40), W60 (= W65), P78 (≠ N83), G80 (= G85), G85 (= G90), S86 (≠ G91), H90 (≠ N95), Y91 (≠ V96), V93 (= V98), V230 (= V227), S270 (= S260), A271 (≠ M261), F500 (≠ W451), H501 (= H452), H545 (≠ N494), T546 (= T495), Q547 (≠ M496), I550 (≠ C499)
3q9tA Crystal structure analysis of formate oxidase (see paper)
29% identity, 98% coverage: 8:515/521 of query aligns to 6:574/577 of 3q9tA
- active site: A335 (vs. gap), D422 (≠ G368), A508 (≠ Y450), H510 (= H452), C552 (≠ G493), R553 (≠ N494)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl(2R,3S,4S)-5-(8-formyl-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-2,3,4-trihydroxypentyl dihydrogendiphosphate: G15 (= G17), T16 (= T18), E37 (= E39), A38 (= A40), W65 (= W65), T85 (≠ N83), R86 (≠ M84), G87 (= G85), G92 (= G90), S93 (≠ G91), N97 (= N95), Y98 (≠ V96), F99 (≠ M97), T100 (≠ V98), S229 (≠ V227), S265 (= S260), Q266 (≠ M261), E270 (≠ N265), F509 (≠ W451), D542 (= D483), A543 (= A484), R553 (≠ N494), I554 (≠ T495), Q555 (≠ M496), V558 (≠ C499)
5zu2A Effect of mutation (r554a) on fad modification in aspergillus oryzae rib40formate oxidase (see paper)
29% identity, 98% coverage: 8:515/521 of query aligns to 6:574/577 of 5zu2A
- binding flavin-adenine dinucleotide: G15 (= G17), T16 (= T18), E37 (= E39), A38 (= A40), W65 (= W65), T85 (≠ N83), R86 (≠ M84), G87 (= G85), G92 (= G90), S93 (≠ G91), N97 (= N95), Y98 (≠ V96), T100 (≠ V98), S229 (≠ V227), S265 (= S260), Q266 (≠ M261), E270 (≠ N265), F509 (≠ W451), D542 (= D483), A543 (= A484), A553 (≠ N494), I554 (≠ T495), Q555 (≠ M496), V558 (≠ C499)
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)
30% identity, 97% coverage: 6:511/521 of query aligns to 3:528/531 of E4QP00
- V101 (≠ I94) mutation to H: Abolishes activity.
- M103 (≠ V96) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ F366) 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 (≠ G368) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ Y450) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (= W451) 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 (= H452) mutation to A: Abolishes activity.
- N511 (= N494) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
30% identity, 97% coverage: 9:511/521 of query aligns to 2:524/525 of 4udqA
- active site: L331 (= L326), F364 (≠ A367), W365 (≠ G368), V461 (≠ Y450), H463 (= H452), A506 (≠ G493), N507 (= N494)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), T11 (= T18), A12 (= A19), E32 (= E39), A33 (= A40), W64 (= W55), G88 (= G85), G93 (= G90), G94 (= G91), N98 (= N95), M99 (≠ V96), V101 (= V98), V229 (= V227), T261 (≠ S260), A262 (≠ M261), W462 (= W451), H463 (= H452), A497 (= A484), N507 (= N494), T508 (= T495), N509 (≠ M496), T512 (≠ C499)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
27% identity, 96% coverage: 9:510/521 of query aligns to 5:563/570 of 4yntA
- active site: V342 (= V317), F413 (≠ G362), W414 (= W363), N502 (≠ Y450), H504 (= H452), G546 (= G493), H547 (≠ N494)
- binding dihydroflavine-adenine dinucleotide: G13 (= G17), T14 (= T18), S15 (≠ A19), E35 (= E39), A36 (= A40), F56 (≠ L59), W62 (= W65), R80 (≠ N83), G82 (= G85), G87 (= G90), T88 (≠ G91), N92 (= N95), G93 (≠ V96), M94 (= M97), A95 (≠ V98), A234 (≠ V227), A274 (≠ M261), R278 (≠ N265), F503 (≠ W451), A537 (= A484), H547 (≠ N494), L548 (≠ T495), V549 (≠ M496), L552 (≠ C499)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
27% identity, 96% coverage: 9:510/521 of query aligns to 4:562/569 of 4ynuA
- active site: V341 (= V317), F412 (≠ G362), W413 (= W363), N501 (≠ Y450), H503 (= H452), G545 (= G493), H546 (≠ N494)
- binding flavin-adenine dinucleotide: G12 (= G17), T13 (= T18), S14 (≠ A19), E34 (= E39), A35 (= A40), Y51 (≠ W55), F55 (≠ L59), W61 (= W65), R79 (≠ N83), G81 (= G85), G86 (= G90), T87 (≠ G91), N91 (= N95), G92 (≠ V96), T232 (≠ L226), A233 (≠ V227), A273 (≠ M261), G274 (= G262), R277 (≠ N265), F502 (≠ W451), A536 (= A484), H546 (≠ N494), L547 (≠ T495), V548 (≠ M496), L551 (≠ C499)
- binding D-glucono-1,5-lactone: Y51 (≠ W55), E411 (≠ Q361), A496 (≠ N445), N497 (≠ S446), R499 (≠ V448), R499 (≠ V448), N501 (≠ Y450), H503 (= H452), H546 (≠ N494)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
27% identity, 96% coverage: 9:510/521 of query aligns to 4:562/566 of 7vzsA
- binding D-glucal: Y6 (≠ F11), L22 (= L27), N25 (≠ Q30), Y51 (≠ W55), I349 (≠ T325), Q356 (vs. gap), E411 (≠ Q361), E444 (≠ P399), W445 (≠ E400), K448 (≠ A403), R499 (≠ V448), N501 (≠ Y450), H546 (≠ N494)
- binding flavin-adenine dinucleotide: G10 (= G15), G12 (= G17), T13 (= T18), S14 (≠ A19), E34 (= E39), A35 (= A40), Y51 (≠ W55), F55 (≠ L59), W61 (= W65), R79 (≠ N83), G81 (= G85), G86 (= G90), T87 (≠ G91), N91 (= N95), G92 (≠ V96), M93 (= M97), A94 (≠ V98), T232 (≠ L226), A233 (≠ V227), A273 (≠ M261), G274 (= G262), R277 (≠ N265), F502 (≠ W451), A536 (= A484), H546 (≠ N494), L547 (≠ T495), V548 (≠ M496), L551 (≠ C499)
Sites not aligning to the query:
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
30% identity, 97% coverage: 8:510/521 of query aligns to 15:572/577 of 4h7uA
- active site: A343 (vs. gap), V426 (vs. gap), Y510 (= Y450), H512 (= H452), A555 (≠ G493), H556 (≠ N494)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-2,3,4-trihydroxy-5-[(4aR)-4a-hydroxy-7,8-dimethyl-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]pentyl dihydrogen diphosphate (non-preferred name): G22 (= G15), G24 (= G17), T25 (= T18), A26 (= A19), E46 (= E39), A47 (= A40), W74 (= W65), G99 (= G90), C100 (≠ G91), H103 (≠ I94), N104 (= N95), G105 (≠ V96), V107 (= V98), L242 (= L226), V243 (= V227), G282 (≠ M261), G283 (= G262), A286 (≠ N265), H512 (= H452), A546 (= A484), H556 (≠ N494), T557 (= T495), Q558 (≠ M496), V561 (≠ C499)
Q3L245 Pyranose dehydrogenase 1; PDH 1; Pyranose:quinone oxidoreductase 1; EC 1.1.99.29 from Leucoagaricus meleagris (Western flat-topped agaric) (Agaricus meleagris) (see 2 papers)
30% identity, 97% coverage: 8:510/521 of query aligns to 40:597/602 of Q3L245
- N100 (≠ A66) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I94) modified: Tele-8alpha-FAD histidine
- N344 (= N298) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H452) active site, Proton acceptor
- H581 (≠ N494) active site
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_389 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_389
MNHRRDRNYDFIVCGAGTAGCVVAARLAQQDNARVLLIEAGNEYAGPEVAEPAQWPLNLG
SERDWAFAGQSNPHLNGRRLSLNMGKGLGGGSSINVMVWARGHRSDWDHFAAESGDCAWG
YDSVLDYYRRIENWHGSPDAARRGSGGPVHVEQPASPQPLAWATLEAASRLGIPRYDSPN
GAMMEGPGGAAITDLRINQGRRESVYDSYVRPRLHQPNLTVLTGALVSRVLLRGTRAVGV
EVIIEGQRHCFYAEAEVVLSMGAVNTPKVLMQSGIGPESELRTHGIVPASHLPGVGQNLQ
DHVAFGCTWEYLQPQAVGGGGCETTLYWKSDSRLDAPDLLHCQLEFAVPSPAEVGIQPPQ
QGWTMFAGLARPVSRGRLRLSGAGPSDAPLIEPNSLSAPEDMAAAFASIDLCRALGNSET
FNDLVKREVVPGPKAHRAMEQFIRNSAVSYWHPSCTAKMGRDEMSVVDHQLRVYGIEKLR
IADASVMPRITVGNTMAPCVVIGERAADLVLAAQSVITLAS
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