SitesBLAST
Comparing RR42_RS29710 FitnessBrowser__Cup4G11:RR42_RS29710 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)
38% identity, 99% coverage: 2:529/531 of query aligns to 3:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), S14 (= S13), A15 (= A14), E35 (= E34), A36 (= A35), W47 (= W61), P65 (= P79), G67 (= G81), V180 (≠ A218), A214 (= A252), G215 (= G253), A218 (≠ Q256), T270 (= T308), Y391 (≠ F468), A424 (≠ C503), I435 (≠ T514), N436 (= N515)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
39% identity, 99% coverage: 2:529/531 of query aligns to 22:569/578 of 5nccA
- active site: R347 (= R318), L420 (≠ I382), I421 (≠ C383), S507 (≠ I467), A509 (≠ H469), G552 (= G512), Q553 (≠ N513)
- binding flavin-adenine dinucleotide: G30 (= G10), G32 (= G12), T33 (≠ S13), A34 (= A14), L53 (= L33), E54 (= E34), A55 (= A35), F74 (≠ M54), W80 (= W61), A98 (≠ P79), G100 (= G81), G105 (= G86), S106 (= S87), N110 (= N91), A111 (≠ G92), T112 (≠ L93), L113 (≠ I94), V238 (≠ A218), A278 (= A252), H282 (≠ Q256), L286 (= L260), N508 (≠ F468), Q553 (≠ N513), T554 (= T514), G555 (≠ N515), V558 (≠ T518)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
38% identity, 99% coverage: 2:529/531 of query aligns to 82:636/654 of A0A248QE08
- TA 93:94 (≠ SA 13:14) binding
- E114 (= E34) binding
- L162 (≠ T83) binding
- S166 (= S87) binding
- NATL 170:173 (≠ NGLI 91:94) binding
- V298 (≠ A218) binding
- C432 (≠ I337) binding
- R451 (≠ H359) binding
- Y466 (≠ E371) binding
- Q486 (≠ S381) binding
- G622 (≠ N515) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
38% identity, 99% coverage: 2:529/531 of query aligns to 6:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H359), N499 (≠ F468)
- binding flavin-adenine dinucleotide: G14 (= G10), G16 (= G12), T17 (≠ S13), A18 (= A14), L37 (= L33), E38 (= E34), A39 (= A35), F58 (≠ M54), W64 (= W61), A82 (≠ P79), G89 (= G86), S90 (= S87), N94 (= N91), A95 (≠ G92), T96 (≠ L93), L97 (≠ I94), M191 (≠ S187), V222 (≠ A218), C264 (= C251), A265 (= A252), G266 (= G253), H269 (≠ Q256), N499 (≠ F468), A534 (≠ C503), Q544 (≠ N513), T545 (= T514), G546 (≠ N515)
- binding heptadecane: V377 (≠ A361), G379 (vs. gap), M380 (vs. gap), G386 (≠ S367), T389 (≠ G370), Y390 (≠ E371), F393 (vs. gap), T408 (= T379), Q410 (≠ S381)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
36% identity, 99% coverage: 4:529/531 of query aligns to 14:526/532 of 4mjwA
- active site: I333 (≠ L327), P377 (≠ I382), N378 (≠ C383), V464 (≠ I467), H466 (= H469), V509 (≠ G512), N510 (= N513)
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ Q217), A232 (= A218), T269 (≠ A252), G270 (= G253), D273 (≠ Q256), Y465 (≠ F468), H466 (= H469), A500 (≠ C503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (≠ T518)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
36% identity, 99% coverage: 4:529/531 of query aligns to 14:526/527 of 2jbvA
- active site: I333 (≠ L327), P377 (≠ I382), N378 (≠ C383), V464 (≠ I467), H466 (= H469), V509 (≠ G512), N510 (= N513)
- 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 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ Q217), A232 (= A218), T269 (≠ A252), G270 (= G253), D273 (≠ Q256), V464 (≠ I467), Y465 (≠ F468), H466 (= H469), D499 (= D502), A500 (≠ C503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (≠ T518)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
36% identity, 99% coverage: 4:529/531 of query aligns to 14:526/530 of 3ljpA
- active site: I333 (≠ L327), P377 (≠ I382), N378 (≠ C383), A464 (≠ I467), H466 (= H469), V509 (≠ G512), N510 (= N513)
- binding dihydroflavine-adenine dinucleotide: G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), A232 (= A218), T269 (≠ A252), D273 (≠ Q256), Y465 (≠ F468), H466 (= H469), D499 (= D502), A500 (≠ C503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (≠ T518)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
36% identity, 99% coverage: 4:530/531 of query aligns to 2:524/525 of 4udqA
- active site: L331 (≠ W325), F364 (≠ I382), W365 (≠ C383), V461 (≠ I467), H463 (= H469), A506 (≠ G512), N507 (= N513)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), T11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W64 (= W61), G88 (= G81), G93 (= G86), G94 (≠ S87), N98 (= N91), M99 (≠ G92), V101 (≠ I94), V229 (≠ A218), T261 (≠ C251), A262 (= A252), W462 (≠ F468), H463 (= H469), A497 (≠ C503), N507 (= N513), T508 (= T514), N509 (= N515), T512 (= T518)
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)
36% identity, 99% coverage: 4:530/531 of query aligns to 6:528/531 of E4QP00
- V101 (≠ I90) mutation to H: Abolishes activity.
- M103 (≠ G92) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V372) 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 (≠ C383) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I467) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F468) 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 (= H469) mutation to A: Abolishes activity.
- N511 (= N513) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
31% identity, 99% coverage: 4:529/531 of query aligns to 2:561/565 of 5oc1A
- active site: V339 (≠ K320), N413 (≠ Q384), A414 (vs. gap), I499 (= I467), H501 (= H469), A544 (≠ G512), H545 (≠ N513)
- binding 4-methoxybenzoic acid: Y91 (≠ G92), I356 (= I337), I390 (≠ L363), F396 (≠ A369), T412 (≠ C383), I499 (= I467), H501 (= H469), H545 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), N11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (= S87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (≠ A218), S270 (≠ C251), A271 (= A252), G272 (= G253), F500 (= F468), H545 (≠ N513), T546 (= T514), Q547 (≠ N515), I550 (≠ T518)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
31% identity, 99% coverage: 4:529/531 of query aligns to 2:561/565 of 3fimB
- active site: V339 (≠ K320), N413 (≠ Q384), A414 (vs. gap), I499 (= I467), H501 (= H469), A544 (≠ G512), H545 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G10), N11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (= S87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (≠ A218), S270 (≠ C251), A271 (= A252), F500 (= F468), H501 (= H469), H545 (≠ N513), T546 (= T514), Q547 (≠ N515), I550 (≠ T518)
8bxlB Patulin synthase from penicillium expansum
32% identity, 99% coverage: 2:526/531 of query aligns to 12:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), T23 (≠ S13), A24 (= A14), E44 (= E34), A45 (= A35), W80 (= W61), G100 (= G81), G105 (= G86), S106 (= S87), R109 (≠ I90), N110 (= N91), Y111 (≠ G92), A113 (≠ I94), L253 (≠ Q217), A254 (= A218), A288 (= A252), Q292 (= Q256), F525 (= F468), D559 (= D502), A560 (≠ C503), H570 (≠ N513), P571 (≠ T514), Q572 (≠ N515), L575 (≠ T518)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
34% identity, 98% coverage: 5:526/531 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I467), H446 (= H469), G487 (= G512), P488 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), G83 (= G86), S84 (= S87), L87 (≠ I90), H88 (≠ N91), A89 (≠ G92), M90 (≠ L93), G91 (≠ I94), V218 (≠ A218), A251 (= A252), G252 (= G253), E255 (≠ Q256), H445 (≠ F468), A478 (≠ C503), P488 (≠ N513), I489 (≠ T514), H490 (≠ N515)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G92), S314 (= S314), H444 (≠ I467), H446 (= H469)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
34% identity, 98% coverage: 5:526/531 of query aligns to 3:501/509 of 3t37A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I467), H446 (= H469), G487 (= G512), P488 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), R79 (= R82), G83 (= G86), S84 (= S87), H88 (≠ N91), A89 (≠ G92), G91 (≠ I94), R217 (≠ Q217), V218 (≠ A218), A251 (= A252), E255 (≠ Q256), H445 (≠ F468), A478 (≠ C503), P488 (≠ N513), I489 (≠ T514), H490 (≠ N515)
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
28% identity, 99% coverage: 4:531/531 of query aligns to 16:574/577 of 4h7uA
- active site: A343 (≠ R313), V426 (≠ C383), Y510 (≠ I467), H512 (= H469), A555 (≠ G512), H556 (≠ N513)
- 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 (= G10), G24 (= G12), T25 (≠ S13), A26 (= A14), E46 (= E34), A47 (= A35), W74 (= W61), G99 (= G86), C100 (≠ S87), H103 (≠ I90), N104 (= N91), G105 (= G92), V107 (≠ I94), L242 (= L215), V243 (≠ A216), G282 (≠ A252), G283 (= G253), A286 (≠ Q256), H512 (= H469), A546 (≠ C503), H556 (≠ N513), T557 (= T514), Q558 (≠ N515), V561 (≠ T518)
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)
28% identity, 99% coverage: 4:531/531 of query aligns to 41:599/602 of Q3L245
- N100 (≠ R62) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I90) modified: Tele-8alpha-FAD histidine
- N344 (= N289) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H469) active site, Proton acceptor
- H581 (≠ N513) active site
Sites not aligning to the query:
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
30% identity, 99% coverage: 4:531/531 of query aligns to 2:580/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P79), L92 (≠ I96), Q306 (≠ H293), V360 (≠ G341), Y431 (≠ C383), L433 (= L385), N514 (≠ H469), S516 (= S471), N517 (≠ G472), H519 (≠ A474), G561 (= G512), S562 (≠ N513)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (≠ A14), E32 (= E34), A33 (= A35), W56 (= W61), A77 (≠ G81), G82 (= G86), G83 (≠ S87), N87 (= N91), A88 (≠ G92), V90 (≠ I94), L227 (≠ Q217), V228 (≠ A218), A265 (= A252), A518 (≠ T473), H519 (≠ A474), D551 (= D502), I552 (≠ C503), S562 (≠ N513), P563 (≠ T514), M564 (≠ N515)
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, 99% coverage: 4:531/531 of query aligns to 2:580/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P79), V90 (≠ I94), Y431 (≠ C383), N517 (≠ G472), D576 (= D527), K580 (= K531)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (≠ A14), E32 (= E34), A33 (= A35), W56 (= W61), A77 (≠ G81), G82 (= G86), G83 (≠ S87), N87 (= N91), A88 (≠ G92), V90 (≠ I94), L227 (≠ Q217), V228 (≠ A218), A265 (= A252), A518 (≠ T473), H519 (≠ A474), D551 (= D502), I552 (≠ C503), S562 (≠ N513), P563 (≠ T514), M564 (≠ N515)
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, 99% coverage: 4:531/531 of query aligns to 2:580/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (≠ G92), V90 (≠ I94), L354 (≠ V335), H421 (= H373), L429 (≠ S381), Y431 (≠ C383), N517 (≠ G472)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (≠ A14), E32 (= E34), A33 (= A35), W56 (= W61), A77 (≠ G81), G82 (= G86), G83 (≠ S87), N87 (= N91), A88 (≠ G92), V90 (≠ I94), L227 (≠ Q217), V228 (≠ A218), A265 (= A252), A518 (≠ T473), H519 (≠ A474), D551 (= D502), I552 (≠ C503), S562 (≠ N513), P563 (≠ T514), M564 (≠ N515)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
30% identity, 99% coverage: 4:531/531 of query aligns to 2:580/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (≠ G92), L354 (≠ V335), Y431 (≠ C383), N517 (≠ G472)
- binding dihydroflavine-adenine dinucleotide: G10 (= G12), I11 (≠ S13), S12 (≠ A14), E32 (= E34), A33 (= A35), W56 (= W61), G82 (= G86), G83 (≠ S87), I86 (= I90), N87 (= N91), A88 (≠ G92), V90 (≠ I94), L227 (≠ Q217), V228 (≠ A218), A265 (= A252), A518 (≠ T473), H519 (≠ A474), D551 (= D502), I552 (≠ C503), S562 (≠ N513), M564 (≠ N515)
Query Sequence
>RR42_RS29710 FitnessBrowser__Cup4G11:RR42_RS29710
MQTFDYVIVGAGSAGSVLANRLSESGKYTVCLLEAGPKDRYPWIHIPIGYAKTMQHPKYN
WRFYTEPEPELANRKIYQPRGRTLGGSSSINGLIYIRGQKRDYDEWRDLGNPGWGWDDVL
PYFRKLETNDLGASATRGDSGPMHATSVPPEHELVDAFIGASERLGVPRTNDFNDGRQEG
VGYFQVSTKNGFRCSTAVGYLKPAKSRANLHIETLAQATKVLFEGKRATGVRYVRDGRTL
EVKATREVLLCAGAIQSPQLLQLSGVGPAALLSEFGIKPVHVSPGVGENLQDHLQVRLMY
EVTKPITTNDAVRSLTGRAKMGLQWLLRRSGPLAVGINHGGMFCRALPDENATPDIQFHF
AALSADSTAGEVHDFPGCTYSICQLRPESRGFVRIRSLEALEPPRIQCNYLSTETDRRTT
VAGVKFARKVAATEPMAAYMKREYRPGPNVRTDDEILQFCREYGTTIFHPSGTAKMGSAD
DPMAVVDGELRVRGVEGLRVIDCSIMPTLISGNTNIPTVMIAEKAADMILK
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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