SitesBLAST
Comparing 3608021 FitnessBrowser__Dino:3608021 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)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 89% coverage: 47:532/544 of query aligns to 3:496/508 of 4ha6A
- active site: F360 (≠ S398), G361 (= G399), H444 (≠ Y484), H446 (= H486), G487 (≠ S523), P488 (≠ N524)
- binding flavin-adenine dinucleotide: G8 (= G52), G10 (= G54), S11 (= S55), A12 (= A56), E32 (= E75), A33 (= A76), W58 (≠ K101), R77 (= R120), G78 (= G121), G83 (= G126), S84 (≠ T127), L87 (= L130), H88 (≠ N131), A89 (= A132), M90 (= M133), G91 (≠ V134), V218 (= V259), A251 (= A293), G252 (= G294), E255 (≠ D297), H445 (≠ F485), A478 (= A514), P488 (≠ N524), I489 (≠ T525), H490 (≠ N526)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (= A132), S314 (= S355), H444 (≠ Y484), H446 (= H486)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 89% coverage: 47:532/544 of query aligns to 3:496/509 of 3t37A
- active site: F360 (≠ S398), G361 (= G399), H444 (≠ Y484), H446 (= H486), G487 (≠ S523), P488 (≠ N524)
- binding flavin-adenine dinucleotide: G8 (= G52), G10 (= G54), S11 (= S55), A12 (= A56), E32 (= E75), A33 (= A76), W58 (≠ K101), R77 (= R120), G78 (= G121), R79 (≠ N122), G83 (= G126), S84 (≠ T127), H88 (≠ N131), A89 (= A132), G91 (≠ V134), R217 (≠ P258), V218 (= V259), A251 (= A293), E255 (≠ D297), H445 (≠ F485), A478 (= A514), P488 (≠ N524), I489 (≠ T525), H490 (≠ N526)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
37% identity, 92% coverage: 43:543/544 of query aligns to 11:529/532 of 4mjwA
- active site: I333 (≠ V357), P377 (≠ S398), N378 (≠ G399), V464 (≠ Y484), H466 (= H486), V509 (≠ S523), N510 (= N524)
- binding flavin-adenine dinucleotide: G20 (= G52), G22 (= G54), S23 (= S55), E44 (= E75), A45 (= A76), W71 (≠ K101), R89 (= R120), A90 (≠ G121), G95 (= G126), C96 (≠ T127), H99 (≠ L130), N100 (= N131), S101 (≠ A132), I103 (≠ V134), R231 (≠ P258), A232 (≠ V259), T269 (≠ A293), G270 (= G294), D273 (= D297), Y465 (≠ F485), H466 (= H486), A500 (= A514), N510 (= N524), P511 (≠ T525), N512 (= N526), V515 (≠ T529)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
37% identity, 92% coverage: 43:543/544 of query aligns to 11:529/530 of 3ljpA
- active site: I333 (≠ V357), P377 (≠ S398), N378 (≠ G399), A464 (≠ Y484), H466 (= H486), V509 (≠ S523), N510 (= N524)
- binding dihydroflavine-adenine dinucleotide: G22 (= G54), S23 (= S55), E44 (= E75), A45 (= A76), W71 (≠ K101), R89 (= R120), A90 (≠ G121), G95 (= G126), C96 (≠ T127), H99 (≠ L130), N100 (= N131), S101 (≠ A132), I103 (≠ V134), A232 (≠ V259), T269 (≠ A293), D273 (= D297), Y465 (≠ F485), H466 (= H486), D499 (= D513), A500 (= A514), N510 (= N524), P511 (≠ T525), N512 (= N526), V515 (≠ T529)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
37% identity, 92% coverage: 43:540/544 of query aligns to 11:526/527 of 2jbvA
- active site: I333 (≠ V357), P377 (≠ S398), N378 (≠ G399), V464 (≠ Y484), H466 (= H486), V509 (≠ S523), N510 (= N524)
- 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 (= G54), S23 (= S55), E44 (= E75), A45 (= A76), W71 (≠ K101), A90 (≠ G121), G95 (= G126), C96 (≠ T127), H99 (≠ L130), N100 (= N131), S101 (≠ A132), I103 (≠ V134), R231 (≠ P258), A232 (≠ V259), T269 (≠ A293), G270 (= G294), D273 (= D297), V464 (≠ Y484), Y465 (≠ F485), H466 (= H486), D499 (= D513), A500 (= A514), N510 (= N524), P511 (≠ T525), N512 (= N526), V515 (≠ T529)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
33% identity, 92% coverage: 45:542/544 of query aligns to 4:452/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G52), G13 (= G54), S14 (= S55), A15 (= A56), E35 (= E75), A36 (= A76), W47 (≠ T105), P65 (= P119), G67 (= G121), V180 (= V259), A214 (= A293), G215 (= G294), A218 (≠ D297), T270 (≠ S350), Y391 (≠ F485), A424 (= A514), I435 (≠ T525), N436 (= N526)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
28% identity, 91% coverage: 45:540/544 of query aligns to 1:561/565 of 5oc1A
- active site: V339 (vs. gap), N413 (≠ S398), A414 (≠ G399), I499 (≠ Y484), H501 (= H486), A544 (≠ S523), H545 (≠ N524)
- binding 4-methoxybenzoic acid: Y91 (≠ A132), I356 (vs. gap), I390 (vs. gap), F396 (vs. gap), T412 (≠ L397), I499 (≠ Y484), H501 (= H486), H545 (≠ N524)
- binding flavin-adenine dinucleotide: G8 (= G52), G10 (= G54), N11 (≠ S55), A12 (= A56), E32 (= E75), A33 (= A76), W60 (= W102), P78 (= P119), G80 (= G121), G85 (= G126), S86 (≠ T127), H90 (≠ N131), Y91 (≠ A132), V93 (= V134), V230 (= V259), S270 (= S292), A271 (= A293), G272 (= G294), F500 (= F485), H545 (≠ N524), T546 (= T525), Q547 (≠ N526), I550 (≠ T529)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
28% identity, 91% coverage: 45:540/544 of query aligns to 1:561/565 of 3fimB
- active site: V339 (vs. gap), N413 (≠ S398), A414 (≠ G399), I499 (≠ Y484), H501 (= H486), A544 (≠ S523), H545 (≠ N524)
- binding flavin-adenine dinucleotide: G8 (= G52), N11 (≠ S55), A12 (= A56), E32 (= E75), A33 (= A76), W60 (= W102), P78 (= P119), G80 (= G121), G85 (= G126), S86 (≠ T127), H90 (≠ N131), Y91 (≠ A132), V93 (= V134), V230 (= V259), S270 (= S292), A271 (= A293), F500 (= F485), H501 (= H486), H545 (≠ N524), T546 (= T525), Q547 (≠ N526), I550 (≠ T529)
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, 92% coverage: 43:540/544 of query aligns to 3:527/531 of E4QP00
- V101 (≠ L130) mutation to H: Abolishes activity.
- M103 (≠ A132) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (vs. gap) 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 (vs. gap) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ Y484) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F485) 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 (= H486) mutation to A: Abolishes activity.
- N511 (= N524) 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, 91% coverage: 46:540/544 of query aligns to 2:523/525 of 4udqA
- active site: L331 (≠ P365), F364 (vs. gap), W365 (vs. gap), V461 (≠ Y484), H463 (= H486), A506 (≠ S523), N507 (= N524)
- binding flavin-adenine dinucleotide: G8 (= G52), G10 (= G54), T11 (≠ S55), A12 (= A56), E32 (= E75), A33 (= A76), W64 (≠ E104), G88 (= G121), G93 (= G126), G94 (≠ T127), N98 (= N131), M99 (≠ A132), V101 (= V134), V229 (= V259), T261 (≠ S292), A262 (= A293), W462 (≠ F485), H463 (= H486), A497 (= A514), N507 (= N524), T508 (= T525), N509 (= N526), T512 (= T529)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
30% identity, 94% coverage: 35:544/544 of query aligns to 13:574/578 of 5nccA
- active site: R347 (≠ Y358), L420 (≠ S398), I421 (≠ G399), S507 (≠ Y484), A509 (≠ H486), G552 (≠ S523), Q553 (≠ N524)
- binding flavin-adenine dinucleotide: G30 (= G52), G32 (= G54), T33 (≠ S55), A34 (= A56), L53 (= L74), E54 (= E75), A55 (= A76), F74 (≠ W91), W80 (= W102), A98 (≠ P119), G100 (= G121), G105 (= G126), S106 (≠ T127), N110 (= N131), A111 (= A132), T112 (≠ M133), L113 (≠ V134), V238 (= V259), A278 (= A293), H282 (≠ D297), L286 (= L301), N508 (≠ F485), Q553 (≠ N524), T554 (= T525), G555 (≠ N526), V558 (≠ T529)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
29% identity, 94% coverage: 35:544/544 of query aligns to 73:641/654 of A0A248QE08
- TA 93:94 (≠ SA 55:56) binding
- E114 (= E75) binding
- L162 (≠ V123) binding
- S166 (≠ T127) binding
- NATL 170:173 (≠ NAMV 131:134) binding
- V298 (= V259) binding
- C432 (vs. gap) binding
- R451 (vs. gap) binding
- Y466 (= Y376) binding
- Q486 (≠ L397) binding
- G622 (≠ N526) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
29% identity, 93% coverage: 39:544/544 of query aligns to 1:565/573 of 6yrvAAA
- binding carbon dioxide: R375 (vs. gap), N499 (≠ F485)
- binding flavin-adenine dinucleotide: G14 (= G52), G16 (= G54), T17 (≠ S55), A18 (= A56), L37 (= L74), E38 (= E75), A39 (= A76), F58 (≠ W91), W64 (= W102), A82 (≠ P119), G89 (= G126), S90 (≠ T127), N94 (= N131), A95 (= A132), T96 (≠ M133), L97 (≠ V134), M191 (≠ K230), V222 (= V259), C264 (≠ S292), A265 (= A293), G266 (= G294), H269 (≠ D297), N499 (≠ F485), A534 (= A514), Q544 (≠ N524), T545 (= T525), G546 (≠ N526)
- binding heptadecane: V377 (vs. gap), G379 (= G366), M380 (≠ L367), G386 (≠ M372), T389 (≠ L375), Y390 (= Y376), F393 (≠ V379), T408 (≠ C395), Q410 (≠ L397)
8bxlB Patulin synthase from penicillium expansum
29% identity, 87% coverage: 46:518/544 of query aligns to 14:564/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G52), G22 (= G54), T23 (≠ S55), A24 (= A56), E44 (= E75), A45 (= A76), W80 (vs. gap), G100 (= G121), G105 (= G126), S106 (≠ T127), R109 (≠ L130), N110 (= N131), Y111 (≠ A132), A113 (≠ V134), L253 (≠ P258), A254 (≠ V259), A288 (= A293), Q292 (≠ D297), F525 (= F485), D559 (= D513), A560 (= A514)
Sites not aligning to the query:
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)
27% identity, 96% coverage: 23:543/544 of query aligns to 13:600/602 of Q3L245
- N100 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ L130) modified: Tele-8alpha-FAD histidine
- N344 (≠ G329) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H486) active site, Proton acceptor
- H581 (≠ N524) active site
Sites not aligning to the query:
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
27% identity, 91% coverage: 46:542/544 of query aligns to 4:564/569 of 4ynuA
- active site: V341 (= V357), F412 (vs. gap), W413 (vs. gap), N501 (≠ Y484), H503 (= H486), G545 (≠ S523), H546 (≠ N524)
- binding flavin-adenine dinucleotide: G12 (= G54), T13 (≠ S55), S14 (≠ A56), E34 (= E75), A35 (= A76), Y51 (≠ W91), F55 (≠ L95), W61 (≠ K101), R79 (≠ P119), G81 (= G121), G86 (= G126), T87 (= T127), N91 (= N131), G92 (≠ A132), T232 (≠ P258), A233 (≠ V259), A273 (= A293), G274 (= G294), R277 (≠ D297), F502 (= F485), A536 (= A514), H546 (≠ N524), L547 (≠ T525), V548 (≠ N526), L551 (≠ T529)
- binding D-glucono-1,5-lactone: Y51 (≠ W91), E411 (vs. gap), A496 (= A479), N497 (≠ S480), R499 (≠ N482), R499 (≠ N482), N501 (≠ Y484), H503 (= H486), H546 (≠ N524)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
27% identity, 91% coverage: 46:542/544 of query aligns to 4:564/566 of 7vzsA
- binding D-glucal: Y6 (≠ F48), L22 (= L64), N25 (≠ T67), Y51 (≠ W91), I349 (vs. gap), Q356 (vs. gap), E411 (vs. gap), E444 (= E430), W445 (≠ Q431), K448 (= K434), R499 (≠ N482), N501 (≠ Y484), H546 (≠ N524), K563 (≠ S541)
- binding flavin-adenine dinucleotide: G10 (= G52), G12 (= G54), T13 (≠ S55), S14 (≠ A56), E34 (= E75), A35 (= A76), Y51 (≠ W91), F55 (≠ L95), W61 (≠ K101), R79 (≠ P119), G81 (= G121), G86 (= G126), T87 (= T127), N91 (= N131), G92 (≠ A132), M93 (= M133), A94 (≠ V134), T232 (≠ P258), A233 (≠ V259), A273 (= A293), G274 (= G294), R277 (≠ D297), F502 (= F485), A536 (= A514), H546 (≠ N524), L547 (≠ T525), V548 (≠ N526), L551 (≠ T529)
Sites not aligning to the query:
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
27% identity, 91% coverage: 46:542/544 of query aligns to 5:565/570 of 4yntA
- active site: V342 (= V357), F413 (vs. gap), W414 (vs. gap), N502 (≠ Y484), H504 (= H486), G546 (≠ S523), H547 (≠ N524)
- binding dihydroflavine-adenine dinucleotide: G13 (= G54), T14 (≠ S55), S15 (≠ A56), E35 (= E75), A36 (= A76), F56 (≠ L95), W62 (≠ K101), R80 (≠ P119), G82 (= G121), G87 (= G126), T88 (= T127), N92 (= N131), G93 (≠ A132), M94 (= M133), A95 (≠ V134), A234 (≠ V259), A274 (= A293), R278 (≠ D297), F503 (= F485), A537 (= A514), H547 (≠ N524), L548 (≠ T525), V549 (≠ N526), L552 (≠ T529)
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
27% identity, 92% coverage: 45:543/544 of query aligns to 15:575/577 of 4h7uA
- active site: A343 (≠ S355), V426 (≠ P403), Y510 (= Y484), H512 (= H486), A555 (≠ S523), H556 (≠ N524)
- 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 (= G52), G24 (= G54), T25 (≠ S55), A26 (= A56), E46 (= E75), A47 (= A76), W74 (= W102), G99 (= G126), C100 (≠ T127), H103 (≠ L130), N104 (= N131), G105 (≠ A132), V107 (= V134), L242 (= L253), V243 (≠ L254), G282 (≠ A293), G283 (= G294), A286 (≠ D297), H512 (= H486), A546 (= A514), H556 (≠ N524), T557 (= T525), Q558 (≠ N526), V561 (≠ T529)
3q9tA Crystal structure analysis of formate oxidase (see paper)
27% identity, 91% coverage: 46:541/544 of query aligns to 7:570/577 of 3q9tA
- active site: A335 (≠ V347), D422 (≠ S398), A508 (≠ Y484), H510 (= H486), C552 (≠ S523), R553 (≠ N524)
- 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 (= G54), T16 (≠ S55), E37 (= E75), A38 (= A76), W65 (= W102), T85 (vs. gap), R86 (= R120), G87 (= G121), G92 (= G126), S93 (≠ T127), N97 (= N131), Y98 (≠ A132), F99 (≠ M133), T100 (≠ V134), S229 (≠ V259), S265 (= S292), Q266 (≠ A293), E270 (≠ D297), F509 (= F485), D542 (= D513), A543 (= A514), R553 (≠ N524), I554 (≠ T525), Q555 (≠ N526), V558 (≠ T529)
Query Sequence
>3608021 FitnessBrowser__Dino:3608021
MSRRDFLRRAMALGATAGMAGALATAWSGTAIAQSSTTAPQPDGEYDFIVIGTGSAGAAC
VYQLAQTGARILVLEAGRNDDLEEVHDSRLWAASLGTDATKWFETLPSSHTDGRNHMWPR
GNVLGGTSALNAMVYARGHRTDFDVWETMGATGWSYEDVLPHFMAMESYEPGGENRGTSG
PIFVSQPQDPHRHEGAVAFMDAAAGLGYKETPSFNSDRMSGQAWIDFNIKDQRRQSSAVA
FLRPAIENGNITLLTDAPVQKLTLEGTKCTGVTYLHNGAPVSVRAANEVILSAGAIDSPR
LLMLSGIGIASDLRQVGIDAVVDLPVGVGLQDHILGAGVNYEAKGPVPVSHYNHSEVYMW
ERSDPGLRSPDMIALYVSVPFASTGHKLDYEHGYCILSGVATPQSRGYVKLASDDIADAP
IIETNYLAEEQDWKSYRAATELCRELGASDAYAEFRKRESLPQKDGELTDAEWRDFLSAS
VNTYFHPTSTCQIGKVVEPDLRVKGIEGLRVADASVMPQITTSNTNAPTMMIGWRAGDMI
SKAT
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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