SitesBLAST
Comparing GFF4425 FitnessBrowser__Marino:GFF4425 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)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
38% identity, 98% coverage: 5:531/536 of query aligns to 25:573/578 of 5nccA
- active site: R347 (= R322), L420 (≠ V383), I421 (≠ C384), S507 (≠ V467), A509 (≠ H469), G552 (= G510), Q553 (≠ N511)
- binding flavin-adenine dinucleotide: G30 (= G10), G32 (= G12), T33 (≠ S13), A34 (≠ S14), L53 (= L33), E54 (= E34), A55 (= A35), F74 (≠ V55), W80 (= W62), A98 (≠ P80), G100 (= G82), G105 (= G87), S106 (= S88), N110 (= N92), A111 (= A93), T112 (≠ M94), L113 (≠ A95), V238 (≠ A220), A278 (= A254), H282 (≠ Q258), L286 (= L262), N508 (≠ Y468), Q553 (≠ N511), T554 (= T512), G555 (≠ N513), V558 (≠ A516)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
37% identity, 98% coverage: 5:531/536 of query aligns to 85:640/654 of A0A248QE08
- TA 93:94 (≠ SS 13:14) binding
- E114 (= E34) binding
- L162 (≠ V84) binding
- S166 (= S88) binding
- NATL 170:173 (≠ NAMA 92:95) binding
- V298 (≠ A220) binding
- C432 (≠ A340) binding
- R451 (≠ H360) binding
- Y466 (vs. gap) binding
- Q486 (≠ H382) binding
- G622 (≠ N513) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
37% identity, 98% coverage: 5:531/536 of query aligns to 9:564/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H360), N499 (≠ Y468)
- binding flavin-adenine dinucleotide: G14 (= G10), G16 (= G12), T17 (≠ S13), A18 (≠ S14), L37 (= L33), E38 (= E34), A39 (= A35), F58 (≠ V55), W64 (= W62), A82 (≠ P80), G89 (= G87), S90 (= S88), N94 (= N92), A95 (= A93), T96 (≠ M94), L97 (≠ A95), M191 (≠ T188), V222 (≠ A220), C264 (≠ S253), A265 (= A254), G266 (= G255), H269 (≠ Q258), N499 (≠ Y468), A534 (= A501), Q544 (≠ N511), T545 (= T512), G546 (≠ N513)
- binding heptadecane: V377 (= V362), G379 (≠ A364), M380 (≠ L365), G386 (vs. gap), T389 (vs. gap), Y390 (vs. gap), F393 (vs. gap), T408 (≠ S380), Q410 (≠ H382)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
35% identity, 99% coverage: 2:531/536 of query aligns to 3:454/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), S14 (= S13), A15 (≠ S14), E35 (= E34), A36 (= A35), W47 (= W62), P65 (= P80), G67 (= G82), V180 (≠ A220), A214 (= A254), G215 (= G255), A218 (≠ Q258), T270 (≠ S337), Y391 (= Y468), A424 (= A501), I435 (≠ T512), N436 (= N513)
8bxlB Patulin synthase from penicillium expansum
33% identity, 98% coverage: 2:524/536 of query aligns to 12:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), T23 (≠ S13), A24 (≠ S14), E44 (= E34), A45 (= A35), W80 (vs. gap), G100 (= G82), G105 (= G87), S106 (= S88), R109 (≠ I91), N110 (= N92), Y111 (≠ A93), A113 (= A95), L253 (≠ I219), A254 (= A220), A288 (= A254), Q292 (= Q258), F525 (≠ Y468), D559 (= D500), A560 (= A501), H570 (≠ N511), P571 (≠ T512), Q572 (≠ N513), L575 (≠ A516)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
30% identity, 98% coverage: 5:530/536 of query aligns to 3:564/565 of 5oc1A
- active site: V339 (≠ R322), N413 (≠ V383), A414 (≠ C384), I499 (≠ V467), H501 (= H469), A544 (≠ G510), H545 (≠ N511)
- binding 4-methoxybenzoic acid: Y91 (≠ A93), I356 (≠ L335), I390 (≠ A364), F396 (≠ A370), T412 (≠ H382), I499 (≠ V467), H501 (= H469), H545 (≠ N511)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), N11 (≠ S13), A12 (≠ S14), E32 (= E34), A33 (= A35), W60 (= W62), P78 (= P80), G80 (= G82), G85 (= G87), S86 (= S88), H90 (≠ N92), Y91 (≠ A93), V93 (≠ A95), V230 (≠ A220), S270 (= S253), A271 (= A254), G272 (= G255), F500 (≠ Y468), H545 (≠ N511), T546 (= T512), Q547 (≠ N513), I550 (≠ A516)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
30% identity, 98% coverage: 5:530/536 of query aligns to 3:564/565 of 3fimB
- active site: V339 (≠ R322), N413 (≠ V383), A414 (≠ C384), I499 (≠ V467), H501 (= H469), A544 (≠ G510), H545 (≠ N511)
- binding flavin-adenine dinucleotide: G8 (= G10), N11 (≠ S13), A12 (≠ S14), E32 (= E34), A33 (= A35), W60 (= W62), P78 (= P80), G80 (= G82), G85 (= G87), S86 (= S88), H90 (≠ N92), Y91 (≠ A93), V93 (≠ A95), V230 (≠ A220), S270 (= S253), A271 (= A254), F500 (≠ Y468), H501 (= H469), H545 (≠ N511), T546 (= T512), Q547 (≠ N513), I550 (≠ A516)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
34% identity, 98% coverage: 5:527/536 of query aligns to 15:526/532 of 4mjwA
- active site: I333 (≠ G342), P377 (≠ V383), N378 (≠ C384), V464 (= V467), H466 (= H469), V509 (≠ G510), N510 (= N511)
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W62), R89 (= R81), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ A95), R231 (≠ I219), A232 (= A220), T269 (≠ A254), G270 (= G255), D273 (≠ Q258), Y465 (= Y468), H466 (= H469), A500 (= A501), N510 (= N511), P511 (≠ T512), N512 (= N513), V515 (≠ A516)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
34% identity, 98% coverage: 2:527/536 of query aligns to 12:526/527 of 2jbvA
- active site: I333 (≠ G342), P377 (≠ V383), N378 (≠ C384), V464 (= V467), H466 (= H469), V509 (≠ G510), N510 (= N511)
- 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 (= W62), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ A95), R231 (≠ I219), A232 (= A220), T269 (≠ A254), G270 (= G255), D273 (≠ Q258), V464 (= V467), Y465 (= Y468), H466 (= H469), D499 (= D500), A500 (= A501), N510 (= N511), P511 (≠ T512), N512 (= N513), V515 (≠ A516)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 98% coverage: 5:527/536 of query aligns to 15:526/530 of 3ljpA
- active site: I333 (≠ G342), P377 (≠ V383), N378 (≠ C384), A464 (≠ V467), H466 (= H469), V509 (≠ G510), N510 (= N511)
- binding dihydroflavine-adenine dinucleotide: G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W62), R89 (= R81), A90 (≠ G82), G95 (= G87), C96 (≠ S88), H99 (≠ I91), N100 (= N92), S101 (≠ A93), I103 (≠ A95), A232 (= A220), T269 (≠ A254), D273 (≠ Q258), Y465 (= Y468), H466 (= H469), D499 (= D500), A500 (= A501), N510 (= N511), P511 (≠ T512), N512 (= N513), V515 (≠ A516)
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, 98% coverage: 5:531/536 of query aligns to 7:531/531 of E4QP00
- V101 (≠ I91) mutation to H: Abolishes activity.
- M103 (≠ A93) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ H382) 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 (≠ C384) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (= V467) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ Y468) 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 (= N511) 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, 98% coverage: 5:527/536 of query aligns to 3:523/525 of 4udqA
- active site: L331 (≠ I325), F364 (≠ V383), W365 (≠ C384), V461 (= V467), H463 (= H469), A506 (≠ G510), N507 (= N511)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), T11 (≠ S13), A12 (≠ S14), E32 (= E34), A33 (= A35), W64 (vs. gap), G88 (= G82), G93 (= G87), G94 (≠ S88), N98 (= N92), M99 (≠ A93), V101 (≠ A95), V229 (≠ A220), T261 (≠ S253), A262 (= A254), W462 (≠ Y468), H463 (= H469), A497 (= A501), N507 (= N511), T508 (= T512), N509 (= N513), T512 (≠ A516)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
32% identity, 98% coverage: 6:530/536 of query aligns to 4:581/584 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 (= W62), A88 (= A93), V90 (≠ A95), L354 (= L312), Y431 (≠ C384), N517 (≠ V467), H519 (= H469), S562 (≠ N511)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (= S14), E32 (= E34), A33 (= A35), W56 (vs. gap), A77 (≠ G82), G82 (= G87), G83 (≠ S88), I86 (= I91), N87 (= N92), A88 (= A93), V90 (≠ A95), L227 (≠ I219), V228 (≠ A220), A265 (= A254), A518 (≠ Y468), H519 (= H469), D551 (= D500), I552 (≠ A501), S562 (≠ N511), P563 (≠ T512), M564 (≠ N513)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
32% identity, 98% coverage: 6:530/536 of query aligns to 5:582/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G10), G11 (= G12), I12 (≠ S13), S13 (= S14), E33 (= E34), A34 (= A35), W57 (vs. gap), A78 (≠ G82), G83 (= G87), G84 (≠ S88), N88 (= N92), A89 (= A93), V91 (≠ A95), L228 (≠ I219), V229 (≠ A220), A266 (= A254), A519 (≠ Y468), H520 (= H469), D552 (= D500), I553 (≠ A501), S563 (≠ N511), P564 (≠ T512), M565 (≠ N513)
- binding p-nitrophenol: L93 (≠ I97), V361 (≠ M318), Y432 (≠ C384), L434 (= L386), G562 (= G510), S563 (≠ N511)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
32% identity, 98% coverage: 6:530/536 of query aligns to 4:581/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P80), L92 (≠ I97), Q306 (≠ H295), V360 (≠ M318), Y431 (≠ C384), L433 (= L386), N514 (≠ D465), S516 (≠ T466), N517 (≠ V467), H519 (= H469), G561 (= G510), S562 (≠ N511)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (= S14), E32 (= E34), A33 (= A35), W56 (vs. gap), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ A95), L227 (≠ I219), V228 (≠ A220), A265 (= A254), A518 (≠ Y468), H519 (= H469), D551 (= D500), I552 (≠ A501), S562 (≠ N511), P563 (≠ T512), M564 (≠ N513)
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)
32% identity, 98% coverage: 6:530/536 of query aligns to 4:581/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P80), V90 (≠ A95), Y431 (≠ C384), N517 (≠ V467), D576 (= D525), K580 (≠ E529)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (= S14), E32 (= E34), A33 (= A35), W56 (vs. gap), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ A95), L227 (≠ I219), V228 (≠ A220), A265 (= A254), A518 (≠ Y468), H519 (= H469), D551 (= D500), I552 (≠ A501), S562 (≠ N511), P563 (≠ T512), M564 (≠ N513)
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)
32% identity, 98% coverage: 6:530/536 of query aligns to 4:581/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (= A93), V90 (≠ A95), L354 (= L312), H421 (= H374), L429 (≠ H382), Y431 (≠ C384), N517 (≠ V467)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (= S14), E32 (= E34), A33 (= A35), W56 (vs. gap), A77 (≠ G82), G82 (= G87), G83 (≠ S88), N87 (= N92), A88 (= A93), V90 (≠ A95), L227 (≠ I219), V228 (≠ A220), A265 (= A254), A518 (≠ Y468), H519 (= H469), D551 (= D500), I552 (≠ A501), S562 (≠ N511), P563 (≠ T512), M564 (≠ N513)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
32% identity, 98% coverage: 6:530/536 of query aligns to 4:581/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (= A93), L354 (= L312), Y431 (≠ C384), N517 (≠ V467)
- binding dihydroflavine-adenine dinucleotide: G10 (= G12), I11 (≠ S13), S12 (= S14), E32 (= E34), A33 (= A35), W56 (vs. gap), G82 (= G87), G83 (≠ S88), I86 (= I91), N87 (= N92), A88 (= A93), V90 (≠ A95), L227 (≠ I219), V228 (≠ A220), A265 (= A254), A518 (≠ Y468), H519 (= H469), D551 (= D500), I552 (≠ A501), S562 (≠ N511), M564 (≠ N513)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
32% identity, 97% coverage: 3:524/536 of query aligns to 1:501/508 of 4ha6A
- active site: F360 (≠ V383), G361 (≠ C384), H444 (≠ V467), H446 (= H469), G487 (= G510), P488 (≠ N511)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (≠ S14), E32 (= E34), A33 (= A35), W58 (= W62), R77 (= R81), G78 (= G82), G83 (= G87), S84 (= S88), L87 (≠ I91), H88 (≠ N92), A89 (= A93), M90 (= M94), G91 (≠ A95), V218 (≠ A220), A251 (= A254), G252 (= G255), E255 (≠ Q258), H445 (≠ Y468), A478 (= A501), P488 (≠ N511), I489 (≠ T512), H490 (≠ N513)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (= A93), S314 (≠ R328), H444 (≠ V467), H446 (= H469)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
32% identity, 97% coverage: 3:524/536 of query aligns to 1:501/509 of 3t37A
- active site: F360 (≠ V383), G361 (≠ C384), H444 (≠ V467), H446 (= H469), G487 (= G510), P488 (≠ N511)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (≠ S14), E32 (= E34), A33 (= A35), W58 (= W62), R77 (= R81), G78 (= G82), R79 (= R83), G83 (= G87), S84 (= S88), H88 (≠ N92), A89 (= A93), G91 (≠ A95), R217 (≠ I219), V218 (≠ A220), A251 (= A254), E255 (≠ Q258), H445 (≠ Y468), A478 (= A501), P488 (≠ N511), I489 (≠ T512), H490 (≠ N513)
Query Sequence
>GFF4425 FitnessBrowser__Marino:GFF4425
MKSADYIIIGGGSSGCTLAGRLSENPRSEVALLEAGPDRGSSALIRTPAAVVAMVPRKVN
NWAFETTPQPGLNGRRGYQPRGRVLGGSSAINAMAYIRGHASDYDAWEAAGNEGWGFNDV
LPYFKKSEANQRFHDDWHGNSGPLKVSDLQSDNPFQKHYLEAARQVGYPITEDFNGPQQE
GIGLYQVTQLNGERWSAYRAYIEPHRSSRRNLSIHTEAIAQRIVFEGKRAIGVEFTRRGR
LEYIRARKEVILSAGAFQSPQLLMLSGIGDKAELSEKGIEVMHHLPGVGKNLQDHPDFIF
GYRSNDSNLLGLSLKGGMHGIRQFIKYRQTRRGLLASNFAEGGGFLKTSPELEAPNIQLH
FVVALVDDHARRLHRGHGFSCHVCLLRPKSRGTVVLKNNNPASPPVIDPGFLNDANDVEE
LVDGYKMTRRLMAAPALAKFCTEDPFTANVKTDKQIIDILRNRTDTVYHPVGTCKMGTSK
DSVVDPRLRVYGVEGLRVVDASIMPTIIGGNTNAPAIMIAEKAADLIAEDADDTQS
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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