SitesBLAST
Comparing WP_068167937.1 NCBI__GCF_001592305.1:WP_068167937.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
36% identity, 96% coverage: 8:540/556 of query aligns to 5:457/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G14), G13 (= G16), S14 (= S17), A15 (= A18), E35 (= E38), A36 (= A39), W47 (= W65), P65 (= P83), G67 (= G85), V180 (= V223), A214 (= A260), G215 (= G261), A218 (≠ Q264), T270 (= T337), Y391 (= Y474), A424 (= A507), I435 (≠ L518), N436 (= N519)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
35% identity, 95% coverage: 8:537/556 of query aligns to 24:573/578 of 5nccA
- active site: R347 (≠ G326), L420 (≠ V388), I421 (≠ G389), S507 (≠ A473), A509 (≠ H475), G552 (= G516), Q553 (≠ N517)
- binding flavin-adenine dinucleotide: G30 (= G14), G32 (= G16), T33 (≠ S17), A34 (= A18), L53 (≠ I37), E54 (= E38), A55 (= A39), F74 (≠ M58), W80 (= W65), A98 (≠ P83), G100 (= G85), G105 (= G90), S106 (= S91), N110 (= N95), A111 (≠ G96), T112 (≠ M97), L113 (≠ V98), V238 (= V223), A278 (= A260), H282 (≠ Q264), L286 (= L268), N508 (≠ Y474), Q553 (≠ N517), T554 (≠ L518), G555 (≠ N519), V558 (≠ T522)
6yrvAAA structure of fap after illumination at 100k (see paper)
34% identity, 95% coverage: 8:537/556 of query aligns to 8:564/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H365), N499 (≠ Y474)
- binding flavin-adenine dinucleotide: G14 (= G14), G16 (= G16), T17 (≠ S17), A18 (= A18), L37 (≠ I37), E38 (= E38), A39 (= A39), F58 (≠ M58), W64 (= W65), A82 (≠ P83), G89 (= G90), S90 (= S91), N94 (= N95), A95 (≠ G96), T96 (≠ M97), L97 (≠ V98), M191 (≠ T192), V222 (= V223), C264 (≠ S259), A265 (= A260), G266 (= G261), H269 (≠ Q264), N499 (≠ Y474), A534 (= A507), Q544 (≠ N517), T545 (≠ L518), G546 (≠ N519)
- binding heptadecane: V377 (≠ L367), G379 (vs. gap), M380 (= M369), G386 (= G375), T389 (= T378), Y390 (≠ V379), F393 (vs. gap), T408 (≠ Q385), Q410 (≠ H387)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
34% identity, 95% coverage: 8:537/556 of query aligns to 84:640/654 of A0A248QE08
- TA 93:94 (≠ SA 17:18) binding FAD
- E114 (= E38) binding FAD
- L162 (≠ T87) binding FAD
- S166 (= S91) binding FAD
- NATL 170:173 (≠ NGMV 95:98) binding FAD
- V298 (= V223) binding FAD
- C432 (≠ F345) binding hexadecanoate
- R451 (≠ H365) binding hexadecanoate
- Y466 (≠ V379) binding hexadecanoate
- Q486 (≠ H387) binding hexadecanoate
- G622 (≠ N519) binding FAD
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 94% coverage: 9:530/556 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ V388), G361 (= G389), H444 (≠ A473), H446 (= H475), G487 (= G516), P488 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), S11 (= S17), A12 (= A18), E32 (= E38), A33 (= A39), W58 (= W65), R77 (= R84), G78 (= G85), R79 (≠ K86), G83 (= G90), S84 (= S91), H88 (≠ N95), A89 (≠ G96), G91 (≠ V98), R217 (≠ A222), V218 (= V223), A251 (= A260), E255 (≠ Q264), H445 (≠ Y474), A478 (= A507), P488 (≠ N517), I489 (≠ L518), H490 (≠ N519)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 94% coverage: 9:530/556 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ V388), G361 (= G389), H444 (≠ A473), H446 (= H475), G487 (= G516), P488 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), S11 (= S17), A12 (= A18), E32 (= E38), A33 (= A39), W58 (= W65), R77 (= R84), G78 (= G85), G83 (= G90), S84 (= S91), L87 (≠ I94), H88 (≠ N95), A89 (≠ G96), M90 (= M97), G91 (≠ V98), V218 (= V223), A251 (= A260), G252 (= G261), E255 (≠ Q264), H445 (≠ Y474), A478 (= A507), P488 (≠ N517), I489 (≠ L518), H490 (≠ N519)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G96), S314 (≠ F345), H444 (≠ A473), H446 (= H475)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
33% identity, 95% coverage: 8:534/556 of query aligns to 14:527/530 of 3ljpA
- active site: I333 (≠ S347), P377 (≠ V388), N378 (≠ G389), A464 (= A473), H466 (= H475), V509 (≠ G516), N510 (= N517)
- binding dihydroflavine-adenine dinucleotide: G22 (= G16), S23 (= S17), E44 (= E38), A45 (= A39), W71 (= W65), R89 (= R84), A90 (≠ G85), G95 (= G90), C96 (≠ S91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (≠ V98), A232 (≠ V223), T269 (≠ A260), D273 (≠ Q264), Y465 (= Y474), H466 (= H475), D499 (= D506), A500 (= A507), N510 (= N517), P511 (≠ L518), N512 (= N519), V515 (≠ T522)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
33% identity, 95% coverage: 8:534/556 of query aligns to 14:527/532 of 4mjwA
- active site: I333 (≠ S347), P377 (≠ V388), N378 (≠ G389), V464 (≠ A473), H466 (= H475), V509 (≠ G516), N510 (= N517)
- binding flavin-adenine dinucleotide: G20 (= G14), G22 (= G16), S23 (= S17), E44 (= E38), A45 (= A39), W71 (= W65), R89 (= R84), A90 (≠ G85), G95 (= G90), C96 (≠ S91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (≠ V98), R231 (≠ A222), A232 (≠ V223), T269 (≠ A260), G270 (= G261), D273 (≠ Q264), Y465 (= Y474), H466 (= H475), A500 (= A507), N510 (= N517), P511 (≠ L518), N512 (= N519), V515 (≠ T522)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
33% identity, 95% coverage: 8:534/556 of query aligns to 14:527/527 of 2jbvA
- active site: I333 (≠ S347), P377 (≠ V388), N378 (≠ G389), V464 (≠ A473), H466 (= H475), V509 (≠ G516), N510 (= N517)
- 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 (= G16), S23 (= S17), E44 (= E38), A45 (= A39), W71 (= W65), A90 (≠ G85), G95 (= G90), C96 (≠ S91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (≠ V98), R231 (≠ A222), A232 (≠ V223), T269 (≠ A260), G270 (= G261), D273 (≠ Q264), V464 (≠ A473), Y465 (= Y474), H466 (= H475), D499 (= D506), A500 (= A507), N510 (= N517), P511 (≠ L518), N512 (= N519), V515 (≠ T522)
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, 95% coverage: 8:537/556 of query aligns to 6:531/531 of E4QP00
- V101 (≠ I94) mutation to H: Abolishes activity.
- M103 (≠ G96) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ G383) 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 (≠ Q385) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ A473) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ Y474) 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 (= H475) mutation to A: Abolishes activity.
- N511 (= N517) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
32% identity, 95% coverage: 8:533/556 of query aligns to 2:523/525 of 4udqA
- active site: L331 (= L339), F364 (= F384), W365 (≠ Q385), V461 (≠ A473), H463 (= H475), A506 (≠ G516), N507 (= N517)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), T11 (≠ S17), A12 (= A18), E32 (= E38), A33 (= A39), W64 (≠ N60), G88 (= G85), G93 (= G90), G94 (≠ S91), N98 (= N95), M99 (≠ G96), V101 (= V98), V229 (= V223), T261 (≠ S259), A262 (= A260), W462 (≠ Y474), H463 (= H475), A497 (= A507), N507 (= N517), T508 (≠ L518), N509 (= N519), T512 (= T522)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
30% identity, 95% coverage: 8:536/556 of query aligns to 2:564/565 of 5oc1A
- active site: V339 (≠ I328), N413 (≠ Q385), A414 (= A386), I499 (≠ A473), H501 (= H475), A544 (≠ G516), H545 (≠ N517)
- binding 4-methoxybenzoic acid: Y91 (≠ G96), I356 (vs. gap), I390 (vs. gap), F396 (= F366), T412 (≠ H382), I499 (≠ A473), H501 (= H475), H545 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), N11 (≠ S17), A12 (= A18), E32 (= E38), A33 (= A39), W60 (= W65), P78 (= P83), G80 (= G85), G85 (= G90), S86 (= S91), H90 (≠ N95), Y91 (≠ G96), V93 (= V98), V230 (= V223), S270 (= S259), A271 (= A260), G272 (= G261), F500 (≠ Y474), H545 (≠ N517), T546 (≠ L518), Q547 (≠ N519), I550 (≠ T522)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
29% identity, 95% coverage: 8:536/556 of query aligns to 2:564/565 of 3fimB
- active site: V339 (≠ I328), N413 (≠ Q385), A414 (= A386), I499 (≠ A473), H501 (= H475), A544 (≠ G516), H545 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G14), N11 (≠ S17), A12 (= A18), E32 (= E38), A33 (= A39), W60 (= W65), P78 (= P83), G80 (= G85), G85 (= G90), S86 (= S91), H90 (≠ N95), Y91 (≠ G96), V93 (= V98), V230 (= V223), S270 (= S259), A271 (= A260), F500 (≠ Y474), H501 (= H475), H545 (≠ N517), T546 (≠ L518), Q547 (≠ N519), I550 (≠ T522)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
31% identity, 95% coverage: 8:536/556 of query aligns to 3:582/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G14), G11 (= G16), I12 (≠ S17), S13 (≠ A18), E33 (= E38), A34 (= A39), W57 (= W65), A78 (≠ G85), G83 (= G90), G84 (≠ S91), N88 (= N95), A89 (≠ G96), V91 (= V98), L228 (≠ A222), V229 (= V223), A266 (= A260), A519 (vs. gap), H520 (= H475), D552 (= D506), I553 (≠ A507), S563 (≠ N517), P564 (≠ L518), M565 (≠ N519)
- binding p-nitrophenol: L93 (≠ I100), V361 (≠ L339), Y432 (≠ G389), L434 (≠ M391), G562 (= G516), S563 (≠ N517)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
31% identity, 95% coverage: 8:536/556 of query aligns to 2:581/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P83), L92 (≠ I100), Q306 (vs. gap), V360 (≠ L339), Y431 (≠ G389), L433 (≠ M391), N514 (≠ E471), S516 (≠ A473), N517 (≠ Y474), H519 (= H475), G561 (= G516), S562 (≠ N517)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (= W65), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (= V98), L227 (≠ A222), V228 (= V223), A265 (= A260), A518 (vs. gap), H519 (= H475), D551 (= D506), I552 (≠ A507), S562 (≠ N517), P563 (≠ L518), M564 (≠ N519)
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)
31% identity, 95% coverage: 8:536/556 of query aligns to 2:581/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P83), V90 (= V98), Y431 (≠ G389), N517 (≠ Y474), D576 (= D531), K580 (≠ G535)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (= W65), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (= V98), L227 (≠ A222), V228 (= V223), A265 (= A260), A518 (vs. gap), H519 (= H475), D551 (= D506), I552 (≠ A507), S562 (≠ N517), P563 (≠ L518), M564 (≠ N519)
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)
31% identity, 95% coverage: 8:536/556 of query aligns to 2:581/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (≠ G96), V90 (= V98), L354 (= L333), H421 (vs. gap), L429 (≠ H387), Y431 (≠ G389), N517 (≠ Y474)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (= W65), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (= V98), L227 (≠ A222), V228 (= V223), A265 (= A260), A518 (vs. gap), H519 (= H475), D551 (= D506), I552 (≠ A507), S562 (≠ N517), P563 (≠ L518), M564 (≠ N519)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
31% identity, 95% coverage: 8:536/556 of query aligns to 2:581/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (≠ G96), L354 (= L333), Y431 (≠ G389), N517 (≠ Y474)
- binding dihydroflavine-adenine dinucleotide: G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (= W65), G82 (= G90), G83 (≠ S91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (= V98), L227 (≠ A222), V228 (= V223), A265 (= A260), A518 (vs. gap), H519 (= H475), D551 (= D506), I552 (≠ A507), S562 (≠ N517), M564 (≠ N519)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
31% identity, 95% coverage: 8:536/556 of query aligns to 2:581/584 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 (≠ P57), A88 (≠ G96), V90 (= V98), L354 (= L333), Y431 (≠ G389), N517 (≠ Y474), H519 (= H475), S562 (≠ N517)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (= W65), A77 (≠ G85), G82 (= G90), G83 (≠ S91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (= V98), L227 (≠ A222), V228 (= V223), A265 (= A260), A518 (vs. gap), H519 (= H475), D551 (= D506), I552 (≠ A507), S562 (≠ N517), P563 (≠ L518), M564 (≠ N519)
3q9tA Crystal structure analysis of formate oxidase (see paper)
28% identity, 95% coverage: 8:536/556 of query aligns to 7:572/577 of 3q9tA
- active site: A335 (= A327), D422 (≠ G389), A508 (= A473), H510 (= H475), C552 (≠ G516), R553 (≠ N517)
- 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 (= G16), T16 (≠ S17), E37 (= E38), A38 (= A39), W65 (= W65), T85 (vs. gap), R86 (= R84), G87 (= G85), G92 (= G90), S93 (= S91), N97 (= N95), Y98 (≠ G96), F99 (≠ M97), T100 (≠ V98), S229 (≠ V223), S265 (= S259), Q266 (≠ A260), E270 (≠ Q264), F509 (≠ Y474), D542 (= D506), A543 (= A507), R553 (≠ N517), I554 (≠ L518), Q555 (≠ N519), V558 (≠ T522)
Query Sequence
>WP_068167937.1 NCBI__GCF_001592305.1:WP_068167937.1
MTKPAAAFDYIIIGAGSAGSTLAYRLGEDLDVKILVIEAGPMDHNLFIHMPSAFAYPMAN
PRYSWQFEAEADPGMNNRRIHCPRGKTIGGSSSINGMVYIRGHAEDYNGWAEQFGLPEWR
YANCLPYFRKSETREQGGDHYRGSDGPLKVSTGRCENPLYKAFIEAGQEAGYGYTADMNG
HRQEGFGPMDMTVHKGRRWSTAMAYLRPALKRGNVTLHTGTAVSRILFEGKDLPRAVGVE
VEQGGQKVVYRAQREVILSAGAIQSPQLLQLSGVGHPDLLRPLGIPVVAARAGVGENLQD
HLETYVQYACKEPITLYSATKPLAMGAIGAQWLLTRTGLGATNHFESGGFIRSDAGVRHP
DLQYHFLPMAVRYDGSATVAGHGFQAHVGPMRSTSRGHVRIRSASHRDAPEIRFNYMSTD
QDRKEFRAAIRLTREVFAQNAFHRFRGEELSPTAQVQSDAEIDEHIRNQAETAYHPSCSC
RMGHDDMAVVDGEGRVHGVQALRVVDASIMPLIVSGNLNVPTIMMAEKIADAIKGQALPP
SDAPVWLHPHWQTQQR
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