SitesBLAST
Comparing RR42_RS24385 FitnessBrowser__Cup4G11:RR42_RS24385 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, 99% coverage: 9:541/541 of query aligns to 4:456/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G16), G13 (= G18), S14 (= S19), A15 (= A20), E35 (= E40), A36 (= A41), W47 (= W67), P65 (= P85), G67 (= G87), V180 (= V225), A214 (= A259), G215 (= G260), A218 (≠ G263), T270 (≠ I341), Y391 (≠ F476), A424 (= A509), I435 (≠ T520), N436 (= N521)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
38% identity, 98% coverage: 9:539/541 of query aligns to 23:573/578 of 5nccA
- active site: R347 (≠ L326), L420 (≠ S390), I421 (≠ A391), S507 (≠ L475), A509 (≠ H477), G552 (= G518), Q553 (≠ N519)
- binding flavin-adenine dinucleotide: G30 (= G16), G32 (= G18), T33 (≠ S19), A34 (= A20), L53 (= L39), E54 (= E40), A55 (= A41), F74 (= F60), W80 (= W67), A98 (≠ P85), G100 (= G87), G105 (= G92), S106 (= S93), N110 (= N97), A111 (≠ G98), T112 (≠ M99), L113 (≠ V100), V238 (= V225), A278 (= A259), H282 (≠ G263), L286 (= L267), N508 (≠ F476), Q553 (≠ N519), T554 (= T520), G555 (≠ N521), V558 (≠ T524)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
38% identity, 98% coverage: 9:539/541 of query aligns to 83:640/654 of A0A248QE08
- TA 93:94 (≠ SA 19:20) binding
- E114 (= E40) binding
- L162 (≠ I89) binding
- S166 (= S93) binding
- NATL 170:173 (≠ NGMV 97:100) binding
- V298 (= V225) binding
- C432 (≠ S344) binding
- R451 (≠ S364) binding
- Y466 (≠ K377) binding
- Q486 (≠ A389) binding
- G622 (≠ N521) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
38% identity, 98% coverage: 9:539/541 of query aligns to 7:564/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ S364), N499 (≠ F476)
- binding flavin-adenine dinucleotide: G14 (= G16), G16 (= G18), T17 (≠ S19), A18 (= A20), L37 (= L39), E38 (= E40), A39 (= A41), F58 (= F60), W64 (= W67), A82 (≠ P85), G89 (= G92), S90 (= S93), N94 (= N97), A95 (≠ G98), T96 (≠ M99), L97 (≠ V100), M191 (≠ T194), V222 (= V225), C264 (≠ S258), A265 (= A259), G266 (= G260), H269 (≠ G263), N499 (≠ F476), A534 (= A509), Q544 (≠ N519), T545 (= T520), G546 (≠ N521)
- binding heptadecane: V377 (≠ R366), G379 (≠ S369), M380 (≠ F370), G386 (vs. gap), T389 (≠ N376), Y390 (≠ K377), F393 (≠ M380), T408 (≠ Q387), Q410 (≠ A389)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
32% identity, 98% coverage: 9:538/541 of query aligns to 1:564/565 of 5oc1A
- active site: V339 (≠ N327), N413 (≠ S390), A414 (= A391), I499 (≠ L475), H501 (= H477), A544 (≠ G518), H545 (≠ N519)
- binding 4-methoxybenzoic acid: Y91 (≠ G98), I356 (≠ G342), I390 (≠ D373), F396 (vs. gap), T412 (≠ A389), I499 (≠ L475), H501 (= H477), H545 (≠ N519)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), N11 (≠ S19), A12 (= A20), E32 (= E40), A33 (= A41), W60 (= W67), P78 (= P85), G80 (= G87), G85 (= G92), S86 (= S93), H90 (≠ N97), Y91 (≠ G98), V93 (= V100), V230 (= V225), S270 (= S258), A271 (= A259), G272 (= G260), F500 (= F476), H545 (≠ N519), T546 (= T520), Q547 (≠ N521), I550 (≠ T524)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 98% coverage: 9:538/541 of query aligns to 1:564/565 of 3fimB
- active site: V339 (≠ N327), N413 (≠ S390), A414 (= A391), I499 (≠ L475), H501 (= H477), A544 (≠ G518), H545 (≠ N519)
- binding flavin-adenine dinucleotide: G8 (= G16), N11 (≠ S19), A12 (= A20), E32 (= E40), A33 (= A41), W60 (= W67), P78 (= P85), G80 (= G87), G85 (= G92), S86 (= S93), H90 (≠ N97), Y91 (≠ G98), V93 (= V100), V230 (= V225), S270 (= S258), A271 (= A259), F500 (= F476), H501 (= H477), H545 (≠ N519), T546 (= T520), Q547 (≠ N521), I550 (≠ T524)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
33% identity, 98% coverage: 7:535/541 of query aligns to 11:526/532 of 4mjwA
- active site: I333 (= I341), P377 (≠ S390), N378 (≠ A391), V464 (≠ L475), H466 (= H477), V509 (≠ G518), N510 (= N519)
- binding flavin-adenine dinucleotide: G20 (= G16), G22 (= G18), S23 (= S19), E44 (= E40), A45 (= A41), W71 (= W67), R89 (= R86), A90 (≠ G87), G95 (= G92), C96 (≠ S93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (≠ V100), R231 (≠ V224), A232 (≠ V225), T269 (≠ A259), G270 (= G260), D273 (≠ G263), Y465 (≠ F476), H466 (= H477), A500 (= A509), N510 (= N519), P511 (≠ T520), N512 (= N521), V515 (≠ T524)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
33% identity, 98% coverage: 7:535/541 of query aligns to 11:526/527 of 2jbvA
- active site: I333 (= I341), P377 (≠ S390), N378 (≠ A391), V464 (≠ L475), H466 (= H477), V509 (≠ G518), N510 (= N519)
- 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 (= G18), S23 (= S19), E44 (= E40), A45 (= A41), W71 (= W67), A90 (≠ G87), G95 (= G92), C96 (≠ S93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (≠ V100), R231 (≠ V224), A232 (≠ V225), T269 (≠ A259), G270 (= G260), D273 (≠ G263), V464 (≠ L475), Y465 (≠ F476), H466 (= H477), D499 (= D508), A500 (= A509), N510 (= N519), P511 (≠ T520), N512 (= N521), V515 (≠ T524)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
33% identity, 98% coverage: 7:535/541 of query aligns to 11:526/530 of 3ljpA
- active site: I333 (= I341), P377 (≠ S390), N378 (≠ A391), A464 (≠ L475), H466 (= H477), V509 (≠ G518), N510 (= N519)
- binding dihydroflavine-adenine dinucleotide: G22 (= G18), S23 (= S19), E44 (= E40), A45 (= A41), W71 (= W67), R89 (= R86), A90 (≠ G87), G95 (= G92), C96 (≠ S93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (≠ V100), A232 (≠ V225), T269 (≠ A259), D273 (≠ G263), Y465 (≠ F476), H466 (= H477), D499 (= D508), A500 (= A509), N510 (= N519), P511 (≠ T520), N512 (= N521), V515 (≠ T524)
8bxlB Patulin synthase from penicillium expansum
31% identity, 96% coverage: 10:530/541 of query aligns to 14:581/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G16), G22 (= G18), T23 (≠ S19), A24 (= A20), E44 (= E40), A45 (= A41), W80 (= W67), G100 (= G87), G105 (= G92), S106 (= S93), R109 (≠ I96), N110 (= N97), Y111 (≠ G98), A113 (≠ V100), L253 (≠ V224), A254 (≠ V225), A288 (= A259), Q292 (≠ G263), F525 (= F476), D559 (= D508), A560 (= A509), H570 (≠ N519), P571 (≠ T520), Q572 (≠ N521), L575 (≠ T524)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 96% coverage: 11:529/541 of query aligns to 3:498/509 of 3t37A
- active site: F360 (= F388), G361 (≠ A391), H444 (≠ L475), H446 (= H477), G487 (= G518), P488 (≠ N519)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), S11 (= S19), A12 (= A20), E32 (= E40), A33 (= A41), W58 (= W67), R77 (= R86), G78 (= G87), R79 (≠ K88), G83 (= G92), S84 (= S93), H88 (≠ N97), A89 (≠ G98), G91 (≠ V100), R217 (≠ V224), V218 (= V225), A251 (= A259), E255 (≠ G263), H445 (≠ F476), A478 (= A509), P488 (≠ N519), I489 (≠ T520), H490 (≠ N521)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 96% coverage: 11:529/541 of query aligns to 3:498/508 of 4ha6A
- active site: F360 (= F388), G361 (≠ A391), H444 (≠ L475), H446 (= H477), G487 (= G518), P488 (≠ N519)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), S11 (= S19), A12 (= A20), E32 (= E40), A33 (= A41), W58 (= W67), R77 (= R86), G78 (= G87), G83 (= G92), S84 (= S93), L87 (≠ I96), H88 (≠ N97), A89 (≠ G98), M90 (= M99), G91 (≠ V100), V218 (= V225), A251 (= A259), G252 (= G260), E255 (≠ G263), H445 (≠ F476), A478 (= A509), P488 (≠ N519), I489 (≠ T520), H490 (≠ N521)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G98), S314 (= S344), H444 (≠ L475), H446 (= H477)
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)
34% identity, 99% coverage: 7:539/541 of query aligns to 3:531/531 of E4QP00
- V101 (≠ I96) mutation to H: Abolishes activity.
- M103 (≠ G98) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ M392) 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 (≠ L475) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F476) 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 (= H477) mutation to A: Abolishes activity.
- N511 (= N519) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
33% identity, 99% coverage: 6:541/541 of query aligns to 1:569/570 of 4yntA
- active site: V342 (≠ K324), F413 (≠ M392), W414 (vs. gap), N502 (≠ L475), H504 (= H477), G546 (= G518), H547 (≠ N519)
- binding dihydroflavine-adenine dinucleotide: G13 (= G18), T14 (≠ S19), S15 (≠ A20), E35 (= E40), A36 (= A41), F56 (= F61), W62 (= W67), R80 (≠ P85), G82 (= G87), G87 (= G92), T88 (≠ S93), N92 (= N97), G93 (= G98), M94 (= M99), A95 (≠ V100), A234 (≠ V225), A274 (= A259), R278 (≠ G263), F503 (= F476), A537 (= A509), H547 (≠ N519), L548 (≠ T520), V549 (≠ N521), L552 (≠ T524)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
33% identity, 99% coverage: 8:541/541 of query aligns to 2:568/569 of 4ynuA
- active site: V341 (≠ K324), F412 (≠ M392), W413 (vs. gap), N501 (≠ L475), H503 (= H477), G545 (= G518), H546 (≠ N519)
- binding flavin-adenine dinucleotide: G12 (= G18), T13 (≠ S19), S14 (≠ A20), E34 (= E40), A35 (= A41), Y51 (≠ G57), F55 (= F61), W61 (= W67), R79 (≠ P85), G81 (= G87), G86 (= G92), T87 (≠ S93), N91 (= N97), G92 (= G98), T232 (≠ V224), A233 (≠ V225), A273 (= A259), G274 (= G260), R277 (≠ G263), F502 (= F476), A536 (= A509), H546 (≠ N519), L547 (≠ T520), V548 (≠ N521), L551 (≠ T524)
- binding D-glucono-1,5-lactone: Y51 (≠ G57), E411 (≠ A391), A496 (≠ R470), N497 (≠ S471), R499 (≠ Q473), R499 (≠ Q473), N501 (≠ L475), H503 (= H477), H546 (≠ N519)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
34% identity, 97% coverage: 10:536/541 of query aligns to 2:524/525 of 4udqA
- active site: L331 (= L339), F364 (≠ L393), W365 (vs. gap), V461 (≠ L475), H463 (= H477), A506 (≠ G518), N507 (= N519)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), T11 (≠ S19), A12 (= A20), E32 (= E40), A33 (= A41), W64 (≠ N62), G88 (= G87), G93 (= G92), G94 (≠ S93), N98 (= N97), M99 (≠ G98), V101 (= V100), V229 (= V225), T261 (≠ S258), A262 (= A259), W462 (≠ F476), H463 (= H477), A497 (= A509), N507 (= N519), T508 (= T520), N509 (= N521), T512 (= T524)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
33% identity, 98% coverage: 8:539/541 of query aligns to 2:566/566 of 7vzsA
- binding D-glucal: Y6 (= Y12), L22 (= L28), N25 (≠ S31), Y51 (≠ G57), I349 (≠ L332), Q356 (≠ P338), E411 (≠ A391), E444 (≠ P422), W445 (≠ D423), K448 (≠ R426), R499 (≠ Q473), N501 (≠ L475), H546 (≠ N519), K563 (≠ L536), A566 (= A539)
- binding flavin-adenine dinucleotide: G10 (= G16), G12 (= G18), T13 (≠ S19), S14 (≠ A20), E34 (= E40), A35 (= A41), Y51 (≠ G57), F55 (= F61), W61 (= W67), R79 (≠ P85), G81 (= G87), G86 (= G92), T87 (≠ S93), N91 (= N97), G92 (= G98), M93 (= M99), A94 (≠ V100), T232 (≠ V224), A233 (≠ V225), A273 (= A259), G274 (= G260), R277 (≠ G263), F502 (= F476), A536 (= A509), H546 (≠ N519), L547 (≠ T520), V548 (≠ N521), L551 (≠ T524)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
30% identity, 99% coverage: 8:540/541 of query aligns to 1:584/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G16), G11 (= G18), I12 (≠ S19), S13 (≠ A20), E33 (= E40), A34 (= A41), W57 (= W67), A78 (≠ G87), G83 (= G92), G84 (≠ S93), N88 (= N97), A89 (≠ G98), V91 (= V100), L228 (≠ V224), V229 (= V225), A266 (= A259), A519 (vs. gap), H520 (vs. gap), D552 (= D508), I553 (≠ A509), S563 (≠ N519), P564 (≠ T520), M565 (≠ N521)
- binding p-nitrophenol: L93 (≠ V102), V361 (vs. gap), Y432 (≠ A391), L434 (= L393), G562 (= G518), S563 (≠ N519)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
30% identity, 98% coverage: 9:540/541 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 (vs. gap), A88 (≠ G98), V90 (= V100), L354 (≠ V329), Y431 (≠ A391), N517 (≠ G480), H519 (vs. gap), S562 (≠ N519)
- binding dihydroflavine-adenine dinucleotide: G8 (= G16), G10 (= G18), I11 (≠ S19), S12 (≠ A20), E32 (= E40), A33 (= A41), W56 (= W67), A77 (≠ G87), G82 (= G92), G83 (≠ S93), I86 (= I96), N87 (= N97), A88 (≠ G98), V90 (= V100), L227 (≠ V224), V228 (= V225), A265 (= A259), A518 (vs. gap), H519 (vs. gap), D551 (= D508), I552 (≠ A509), S562 (≠ N519), P563 (≠ T520), M564 (≠ N521)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
30% identity, 98% coverage: 9:540/541 of query aligns to 1:583/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P85), L92 (≠ V102), Q306 (≠ H300), V360 (vs. gap), Y431 (≠ A391), L433 (= L393), N514 (≠ H477), S516 (≠ A479), N517 (≠ G480), H519 (vs. gap), G561 (= G518), S562 (≠ N519)
- binding dihydroflavine-adenine dinucleotide: G8 (= G16), G10 (= G18), I11 (≠ S19), S12 (≠ A20), E32 (= E40), A33 (= A41), W56 (= W67), A77 (≠ G87), G82 (= G92), G83 (≠ S93), N87 (= N97), A88 (≠ G98), V90 (= V100), L227 (≠ V224), V228 (= V225), A265 (= A259), A518 (vs. gap), H519 (vs. gap), D551 (= D508), I552 (≠ A509), S562 (≠ N519), P563 (≠ T520), M564 (≠ N521)
Query Sequence
>RR42_RS24385 FitnessBrowser__Cup4G11:RR42_RS24385
MNSSTHDTEFDYIVVGAGSAGCVLANRLSASPNVSVLLLEAGKDAEPFWVRTPAGVGNLF
FNERLNWKFFTEPEANLGDRQVYWPRGKILGGSSSINGMVYVRGFASDYDRWQAQGNPGW
AWSDVLPYFKRAEHNDYGASESRGVGGPLHVSFPHRQHPTTEAFVRAGAAVGLTRHDDVV
AGGDAEGVGYLQHTIGEGRRWSSAHAYVRPVRQRTNLAIESEAVVTRLHLDGRCVVGVEY
IRRGQSRTIRARREVILSAGAIGSPHLLMLSGIGPPDHLQEMGVRVRHALPGVGCNLQDH
LAINACYEVRKDASLNAALSGWHKYLNGVDYLLHRRGPLAIGASHAVAFVCSSTSIKVPD
IQLSFRPLSFAFDSKNKLRMHTFAGVQFASAMLRPRSRGQILLRSPNPFDAPVIHANYLT
DPDDMRVMVATLEWTRRLAATAPLADMVVREYLPGENVRSASEVVEFIRRSSQTLFHPAG
TCKMGSDSLAVVDERLRVRGIENLRVVDASVMPTIVSGNTNAPTIMIAEKASDMILEDAR
S
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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