SitesBLAST
Comparing Pf1N1B4_4450 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4450 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)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
36% identity, 96% coverage: 7:535/549 of query aligns to 83:641/654 of A0A248QE08
- TA 93:94 (≠ PA 17:18) binding
- E114 (= E38) binding
- L162 (≠ V87) binding
- S166 (≠ C91) binding
- NATL 170:173 (≠ NGMI 95:98) binding
- V298 (= V222) binding
- C432 (≠ S342) binding
- R451 (≠ H362) binding
- Y466 (≠ H376) binding
- Q486 (≠ S384) binding
- G622 (≠ C516) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
36% identity, 96% coverage: 7:535/549 of query aligns to 7:565/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H362), N499 (≠ F471)
- binding flavin-adenine dinucleotide: G14 (= G14), G16 (= G16), T17 (≠ P17), A18 (= A18), L37 (= L37), E38 (= E38), A39 (= A39), F58 (≠ I58), W64 (= W65), A82 (≠ P83), G89 (= G90), S90 (≠ C91), N94 (= N95), A95 (≠ G96), T96 (≠ M97), L97 (≠ I98), M191 (≠ N191), V222 (= V222), C264 (= C255), A265 (= A256), G266 (= G257), H269 (≠ G260), N499 (≠ F471), A534 (= A504), Q544 (≠ N514), T545 (= T515), G546 (≠ C516)
- binding heptadecane: V377 (≠ Q364), G379 (vs. gap), M380 (≠ L366), G386 (= G372), T389 (≠ L375), Y390 (≠ H376), F393 (= F378), T408 (= T382), Q410 (≠ S384)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
36% identity, 96% coverage: 7:535/549 of query aligns to 23:574/578 of 5nccA
- active site: R347 (≠ K322), L420 (≠ V385), I421 (≠ C386), S507 (≠ I470), A509 (≠ H472), G552 (= G513), Q553 (≠ N514)
- binding flavin-adenine dinucleotide: G30 (= G14), G32 (= G16), T33 (≠ P17), A34 (= A18), L53 (= L37), E54 (= E38), A55 (= A39), F74 (≠ I58), W80 (= W65), A98 (≠ P83), G100 (= G85), G105 (= G90), S106 (≠ C91), N110 (= N95), A111 (≠ G96), T112 (≠ M97), L113 (≠ I98), V238 (= V222), A278 (= A256), H282 (≠ G260), L286 (≠ I264), N508 (≠ F471), Q553 (≠ N514), T554 (= T515), G555 (≠ C516), V558 (≠ T519)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
31% identity, 95% coverage: 7:530/549 of query aligns to 4:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G14), G13 (= G16), S14 (≠ P17), A15 (= A18), E35 (= E38), A36 (= A39), W47 (= W65), P65 (= P83), G67 (= G85), V180 (= V222), A214 (= A256), G215 (= G257), A218 (≠ G260), T270 (≠ M339), Y391 (≠ F471), A424 (= A504), I435 (≠ T515), N436 (≠ C516)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 95% coverage: 9:528/549 of query aligns to 3:502/509 of 3t37A
- active site: F360 (≠ V385), G361 (≠ C386), H444 (≠ I470), H446 (= H472), G487 (= G513), P488 (≠ N514)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), S11 (≠ P17), A12 (= A18), E32 (= E38), A33 (= A39), W58 (= W65), R77 (= R84), G78 (= G85), R79 (≠ K86), G83 (= G90), S84 (≠ C91), H88 (≠ N95), A89 (≠ G96), G91 (≠ I98), R217 (≠ E221), V218 (= V222), A251 (= A256), E255 (≠ G260), H445 (≠ F471), A478 (= A504), P488 (≠ N514), I489 (≠ T515), H490 (≠ C516)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 95% coverage: 9:528/549 of query aligns to 3:502/508 of 4ha6A
- active site: F360 (≠ V385), G361 (≠ C386), H444 (≠ I470), H446 (= H472), G487 (= G513), P488 (≠ N514)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), S11 (≠ P17), A12 (= A18), E32 (= E38), A33 (= A39), W58 (= W65), R77 (= R84), G78 (= G85), G83 (= G90), S84 (≠ C91), L87 (≠ I94), H88 (≠ N95), A89 (≠ G96), M90 (= M97), G91 (≠ I98), V218 (= V222), A251 (= A256), G252 (= G257), E255 (≠ G260), H445 (≠ F471), A478 (= A504), P488 (≠ N514), I489 (≠ T515), H490 (≠ C516)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G96), S314 (vs. gap), H444 (≠ I470), H446 (= H472)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
34% identity, 96% coverage: 8:532/549 of query aligns to 2:525/525 of 4udqA
- active site: L331 (= L344), F364 (≠ A383), W365 (≠ S384), V461 (≠ I470), H463 (= H472), A506 (≠ G513), N507 (= N514)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), T11 (≠ P17), A12 (= A18), E32 (= E38), A33 (= A39), W64 (≠ I58), G88 (= G85), G93 (= G90), G94 (≠ C91), N98 (= N95), M99 (≠ G96), V101 (≠ I98), V229 (= V222), T261 (≠ C255), A262 (= A256), W462 (≠ F471), H463 (= H472), A497 (= A504), N507 (= N514), T508 (= T515), N509 (≠ C516), T512 (= T519)
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, 96% coverage: 8:532/549 of query aligns to 6:529/531 of E4QP00
- V101 (≠ I94) mutation to H: Abolishes activity.
- M103 (≠ G96) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ T382) 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 (≠ S384) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I470) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F471) 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 (= H472) mutation to A: Abolishes activity.
- N511 (= N514) 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, 95% coverage: 7:530/549 of query aligns to 1:561/565 of 5oc1A
- active site: V339 (≠ M325), N413 (≠ V385), A414 (≠ C386), I499 (= I470), H501 (= H472), A544 (≠ G513), H545 (≠ N514)
- binding 4-methoxybenzoic acid: Y91 (≠ G96), I356 (vs. gap), I390 (≠ L366), F396 (≠ G372), T412 (≠ S384), I499 (= I470), H501 (= H472), H545 (≠ N514)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), N11 (≠ P17), A12 (= A18), E32 (= E38), A33 (= A39), W60 (= W65), P78 (= P83), G80 (= G85), G85 (= G90), S86 (≠ C91), H90 (≠ N95), Y91 (≠ G96), V93 (≠ I98), V230 (= V222), S270 (≠ C255), A271 (= A256), G272 (= G257), F500 (= F471), H545 (≠ N514), T546 (= T515), Q547 (≠ C516), I550 (≠ T519)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
31% identity, 95% coverage: 7:530/549 of query aligns to 1:561/565 of 3fimB
- active site: V339 (≠ M325), N413 (≠ V385), A414 (≠ C386), I499 (= I470), H501 (= H472), A544 (≠ G513), H545 (≠ N514)
- binding flavin-adenine dinucleotide: G8 (= G14), N11 (≠ P17), A12 (= A18), E32 (= E38), A33 (= A39), W60 (= W65), P78 (= P83), G80 (= G85), G85 (= G90), S86 (≠ C91), H90 (≠ N95), Y91 (≠ G96), V93 (≠ I98), V230 (= V222), S270 (≠ C255), A271 (= A256), F500 (= F471), H501 (= H472), H545 (≠ N514), T546 (= T515), Q547 (≠ C516), I550 (≠ T519)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
32% identity, 96% coverage: 7:532/549 of query aligns to 13:528/532 of 4mjwA
- active site: I333 (≠ M323), P377 (≠ V385), N378 (≠ C386), V464 (≠ I470), H466 (= H472), V509 (≠ G513), N510 (= N514)
- binding flavin-adenine dinucleotide: G20 (= G14), G22 (= G16), S23 (≠ P17), E44 (= E38), A45 (= A39), W71 (= W65), R89 (= R84), A90 (≠ G85), G95 (= G90), C96 (= C91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (= I98), R231 (≠ E221), A232 (≠ V222), T269 (≠ A256), G270 (= G257), D273 (≠ G260), Y465 (≠ F471), H466 (= H472), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (≠ C516), V515 (≠ T519)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
32% identity, 95% coverage: 7:530/549 of query aligns to 13:526/527 of 2jbvA
- active site: I333 (≠ M323), P377 (≠ V385), N378 (≠ C386), V464 (≠ I470), H466 (= H472), V509 (≠ G513), N510 (= N514)
- 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 (≠ P17), E44 (= E38), A45 (= A39), W71 (= W65), A90 (≠ G85), G95 (= G90), C96 (= C91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (= I98), R231 (≠ E221), A232 (≠ V222), T269 (≠ A256), G270 (= G257), D273 (≠ G260), V464 (≠ I470), Y465 (≠ F471), H466 (= H472), D499 (= D503), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (≠ C516), V515 (≠ T519)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
32% identity, 96% coverage: 7:532/549 of query aligns to 13:528/530 of 3ljpA
- active site: I333 (≠ M323), P377 (≠ V385), N378 (≠ C386), A464 (≠ I470), H466 (= H472), V509 (≠ G513), N510 (= N514)
- binding dihydroflavine-adenine dinucleotide: G22 (= G16), S23 (≠ P17), E44 (= E38), A45 (= A39), W71 (= W65), R89 (= R84), A90 (≠ G85), G95 (= G90), C96 (= C91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (= I98), A232 (≠ V222), T269 (≠ A256), D273 (≠ G260), Y465 (≠ F471), H466 (= H472), D499 (= D503), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (≠ C516), V515 (≠ T519)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
29% identity, 95% coverage: 7:530/549 of query aligns to 2:579/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G14), G11 (= G16), I12 (≠ P17), S13 (≠ A18), E33 (= E38), A34 (= A39), W57 (≠ P51), A78 (≠ G85), G83 (= G90), G84 (≠ C91), N88 (= N95), A89 (≠ G96), V91 (≠ I98), L228 (≠ E221), V229 (= V222), A266 (= A256), A519 (≠ F471), H520 (= H472), D552 (= D503), I553 (≠ A504), S563 (≠ N514), P564 (≠ T515), M565 (≠ C516)
- binding p-nitrophenol: L93 (≠ M100), V361 (≠ A346), Y432 (≠ C386), L434 (= L388), G562 (= G513), S563 (≠ N514)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
29% identity, 95% coverage: 7:530/549 of query aligns to 1:578/584 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 (= W47), A88 (≠ G96), V90 (≠ I98), L354 (vs. gap), Y431 (≠ C386), N517 (≠ I470), H519 (= H472), S562 (≠ N514)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ P17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (≠ P51), A77 (≠ G85), G82 (= G90), G83 (≠ C91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (≠ I98), L227 (≠ E221), V228 (= V222), A265 (= A256), A518 (≠ F471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ C516)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
29% identity, 95% coverage: 7:530/549 of query aligns to 1:578/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P83), L92 (≠ M100), Q306 (≠ H297), V360 (≠ A346), Y431 (≠ C386), L433 (= L388), N514 (≠ G467), S516 (≠ T469), N517 (≠ I470), H519 (= H472), G561 (= G513), S562 (≠ N514)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ P17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (≠ P51), A77 (≠ G85), G82 (= G90), G83 (≠ C91), N87 (= N95), A88 (≠ G96), V90 (≠ I98), L227 (≠ E221), V228 (= V222), A265 (= A256), A518 (≠ F471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ C516)
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)
29% identity, 95% coverage: 7:530/549 of query aligns to 1:578/585 of 6ze5A
- binding 2-(1H-indol-3-yl)-N-[(1-methyl-1H-pyrrol-2-yl)methyl]ethanamine: I75 (≠ P83), V90 (≠ I98), Y431 (≠ C386), N517 (≠ I470), D576 (≠ Q528)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ P17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (≠ P51), A77 (≠ G85), G82 (= G90), G83 (≠ C91), N87 (= N95), A88 (≠ G96), V90 (≠ I98), L227 (≠ E221), V228 (= V222), A265 (= A256), A518 (≠ F471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ C516)
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)
29% identity, 95% coverage: 7:530/549 of query aligns to 1:578/585 of 6ze4A
- binding 4-oxo-N-[(1S)-1-(pyridin-3-yl)ethyl]-4-(thiophen-2-yl)butanamide: A88 (≠ G96), V90 (≠ I98), L354 (vs. gap), H421 (= H376), L429 (≠ S384), Y431 (≠ C386), N517 (≠ I470)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ P17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (≠ P51), A77 (≠ G85), G82 (= G90), G83 (≠ C91), N87 (= N95), A88 (≠ G96), V90 (≠ I98), L227 (≠ E221), V228 (= V222), A265 (= A256), A518 (≠ F471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ C516)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
29% identity, 95% coverage: 7:530/549 of query aligns to 1:578/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (≠ G96), L354 (vs. gap), Y431 (≠ C386), N517 (≠ I470)
- binding dihydroflavine-adenine dinucleotide: G10 (= G16), I11 (≠ P17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (≠ P51), G82 (= G90), G83 (≠ C91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (≠ I98), L227 (≠ E221), V228 (= V222), A265 (= A256), A518 (≠ F471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), M564 (≠ C516)
8bxlB Patulin synthase from penicillium expansum
30% identity, 95% coverage: 8:527/549 of query aligns to 14:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G14), G22 (= G16), T23 (≠ P17), A24 (= A18), E44 (= E38), A45 (= A39), W80 (= W65), G100 (= G85), G105 (= G90), S106 (≠ C91), R109 (≠ I94), N110 (= N95), Y111 (≠ G96), A113 (≠ I98), L253 (≠ E221), A254 (≠ V222), A288 (= A256), Q292 (≠ G260), F525 (= F471), D559 (= D503), A560 (= A504), H570 (≠ N514), P571 (≠ T515), Q572 (≠ C516), L575 (≠ T519)
Query Sequence
>Pf1N1B4_4450 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4450
MQTSLDEYDYIVVGAGPAGCLLANRLSANPQHRVLLLEAGGRDNYPWIHIPVGYLFCIGN
PRTDWCFKTETQPGLQGRALSYPRGKVLGGCSSINGMIYMRGQAGDYDGWAAEGNAGWGW
QDVLPLFKQSENHFAGDSEFHGAAGQWRVERQRLSWPILDAFRTAAEQSGIASIDDFNQG
DNEGCGYFQVNQKAGIRWNAAKAFLKPIRQRANLTVLTDVEVDRVLLENGRASAVSARWQ
DQAKTFKARKEIVLCAGAVGSPGILQRSGIGPRPLLQKLGIGVTHELPGVGGNLQDHLQL
RLIYKLENARTLNQIAGTLWGKMGMGLRYLYDRSGPLSMAPSQLGAFARSGPEQTSANLE
YHVQPLSLERFGEPLHAFPAFTASVCDLRPQSRGRIDIRSADPREAPLIQPNYLSHPEDL
RVAADAIRLTRRIVSAPALQAFKPVEYLPGDSLQSEEQLHEAAARIGTTIFHPVGTCRMG
NDAHAVVDAELRVHGIPGLRIADASIMPRITSGNTCSPTLMIAEKAAQLMLSPSTRSLNP
QKELLSNPL
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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