SitesBLAST
Comparing PP_1949 FitnessBrowser__Putida:PP_1949 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, 95% coverage: 8:530/550 of query aligns to 5:450/458 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 (= V222), A214 (= A255), G215 (= G256), A218 (≠ D259), T270 (≠ M337), Y391 (≠ M471), A424 (= A504), I435 (≠ T515), N436 (= N516)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
37% identity, 96% coverage: 8:537/550 of query aligns to 24:576/578 of 5nccA
- active site: R347 (= R316), L420 (≠ T386), I421 (≠ C387), S507 (= S469), A509 (≠ M471), G552 (= G513), Q553 (≠ N514)
- binding flavin-adenine dinucleotide: G30 (= G14), G32 (= G16), T33 (≠ S17), A34 (= A18), L53 (= L37), E54 (= E38), A55 (= A39), F74 (≠ L59), W80 (= W65), A98 (≠ P83), G100 (= G85), G105 (= G90), S106 (= S91), N110 (= N95), A111 (≠ G96), T112 (≠ M97), L113 (≠ A98), V238 (= V222), A278 (= A255), H282 (≠ D259), L286 (= L263), N508 (≠ M470), Q553 (≠ N514), T554 (= T515), G555 (≠ N516), V558 (≠ T519)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
36% identity, 96% coverage: 8:537/550 of query aligns to 84:643/654 of A0A248QE08
- TA 93:94 (≠ SA 17:18) binding
- E114 (= E38) binding
- L162 (≠ A87) binding
- S166 (= S91) binding
- NATL 170:173 (≠ NGMA 95:98) binding
- V298 (= V222) binding
- C432 (≠ S340) binding
- R451 (≠ N360) binding
- Y466 (≠ H367) binding
- Q486 (≠ S385) binding
- G622 (≠ N516) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
36% identity, 96% coverage: 8:537/550 of query aligns to 8:567/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ N360), N499 (≠ M470)
- binding flavin-adenine dinucleotide: G14 (= G14), G16 (= G16), T17 (≠ S17), A18 (= A18), L37 (= L37), E38 (= E38), A39 (= A39), F58 (≠ L59), W64 (= W65), A82 (≠ P83), G89 (= G90), S90 (= S91), N94 (= N95), A95 (≠ G96), T96 (≠ M97), L97 (≠ A98), M191 (vs. gap), V222 (= V222), C264 (≠ S254), A265 (= A255), G266 (= G256), H269 (≠ D259), N499 (≠ M470), A534 (= A504), Q544 (≠ N514), T545 (= T515), G546 (≠ N516)
- binding heptadecane: V377 (≠ R362), G379 (vs. gap), M380 (vs. gap), G386 (vs. gap), T389 (≠ W366), Y390 (≠ H367), F393 (vs. gap), T408 (= T383), Q410 (≠ S385)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
31% identity, 96% coverage: 8:534/550 of query aligns to 2:565/565 of 5oc1A
- active site: V339 (≠ K313), N413 (≠ T386), A414 (≠ C387), I499 (≠ M470), H501 (= H472), A544 (≠ G513), H545 (≠ N514)
- binding 4-methoxybenzoic acid: Y91 (≠ G96), I356 (≠ R330), I390 (≠ P363), F396 (≠ N369), T412 (≠ S385), I499 (≠ M470), H501 (= H472), H545 (≠ N514)
- 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 (≠ A98), V230 (= V222), S270 (= S254), A271 (= A255), G272 (= G256), F500 (≠ M471), H545 (≠ N514), T546 (= T515), Q547 (≠ N516), I550 (≠ T519)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
31% identity, 96% coverage: 8:534/550 of query aligns to 2:565/565 of 3fimB
- active site: V339 (≠ K313), N413 (≠ T386), A414 (≠ C387), I499 (≠ M470), H501 (= H472), A544 (≠ G513), H545 (≠ N514)
- 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 (≠ A98), V230 (= V222), S270 (= S254), A271 (= A255), F500 (≠ M471), H501 (= H472), H545 (≠ N514), T546 (= T515), Q547 (≠ N516), I550 (≠ T519)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
32% identity, 95% coverage: 8:530/550 of query aligns to 14:526/527 of 2jbvA
- active site: I333 (≠ L345), P377 (≠ T386), N378 (≠ C387), V464 (≠ M470), 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 (= S17), E44 (= E38), A45 (= A39), W71 (= W65), A90 (≠ G85), G95 (= G90), C96 (≠ S91), H99 (≠ I94), N100 (= N95), S101 (≠ G96), I103 (≠ A98), R231 (≠ L221), A232 (≠ V222), T269 (≠ A255), G270 (= G256), D273 (= D259), V464 (≠ M470), Y465 (≠ M471), H466 (= H472), D499 (= D503), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (= N516), V515 (≠ T519)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
32% identity, 96% coverage: 8:534/550 of query aligns to 14:530/532 of 4mjwA
- active site: I333 (≠ L345), P377 (≠ T386), N378 (≠ C387), V464 (≠ M470), H466 (= H472), V509 (≠ G513), N510 (= N514)
- 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 (≠ A98), R231 (≠ L221), A232 (≠ V222), T269 (≠ A255), G270 (= G256), D273 (= D259), Y465 (≠ M471), H466 (= H472), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (= N516), V515 (≠ T519)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
32% identity, 96% coverage: 8:534/550 of query aligns to 14:530/530 of 3ljpA
- active site: I333 (≠ L345), P377 (≠ T386), N378 (≠ C387), A464 (≠ M470), H466 (= H472), V509 (≠ G513), N510 (= N514)
- 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 (≠ A98), A232 (≠ V222), T269 (≠ A255), D273 (= D259), Y465 (≠ M471), H466 (= H472), D499 (= D503), A500 (= A504), N510 (= N514), P511 (≠ T515), N512 (= N516), V515 (≠ T519)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
32% identity, 95% coverage: 7:531/550 of query aligns to 1:524/525 of 4udqA
- active site: L331 (= L335), F364 (≠ L389), W365 (vs. gap), V461 (≠ M470), H463 (= H472), A506 (≠ G513), N507 (= N514)
- binding flavin-adenine dinucleotide: G8 (= G14), G10 (= G16), T11 (≠ S17), A12 (= A18), E32 (= E38), A33 (= A39), W64 (vs. gap), G88 (= G85), G93 (= G90), G94 (≠ S91), N98 (= N95), M99 (≠ G96), V101 (≠ A98), V229 (= V222), T261 (≠ S254), A262 (= A255), W462 (≠ M471), H463 (= H472), A497 (= A504), N507 (= N514), T508 (= T515), N509 (= N516), 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)
32% identity, 95% coverage: 7:531/550 of query aligns to 5:528/531 of E4QP00
- V101 (≠ I94) mutation to H: Abolishes activity.
- M103 (≠ G96) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ Q388) 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 (≠ M470) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ M471) 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.
8bxlB Patulin synthase from penicillium expansum
29% identity, 95% coverage: 7:530/550 of query aligns to 13:586/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G14), G22 (= G16), T23 (≠ S17), A24 (= A18), E44 (= E38), A45 (= A39), W80 (= W65), G100 (= G85), G105 (= G90), S106 (= S91), R109 (≠ I94), N110 (= N95), Y111 (≠ G96), A113 (= A98), L253 (= L221), A254 (≠ V222), A288 (= A255), Q292 (≠ D259), F525 (≠ M471), D559 (= D503), A560 (= A504), H570 (≠ N514), P571 (≠ T515), Q572 (≠ N516), L575 (≠ T519)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
32% identity, 94% coverage: 9:527/550 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ T386), G361 (≠ C387), H444 (≠ M470), H446 (= H472), G487 (= G513), P488 (≠ N514)
- 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 (≠ A98), R217 (≠ L221), V218 (= V222), A251 (= A255), E255 (≠ D259), H445 (≠ M471), A478 (= A504), P488 (≠ N514), I489 (≠ T515), H490 (≠ N516)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
32% identity, 94% coverage: 9:527/550 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ T386), G361 (≠ C387), H444 (≠ M470), H446 (= H472), G487 (= G513), P488 (≠ N514)
- 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 (≠ A98), V218 (= V222), A251 (= A255), G252 (= G256), E255 (≠ D259), H445 (≠ M471), A478 (= A504), P488 (≠ N514), I489 (≠ T515), H490 (≠ N516)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G96), S314 (≠ L318), H444 (≠ M470), H446 (= H472)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
31% identity, 96% coverage: 8:533/550 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 (= W65), A88 (≠ G96), V90 (≠ A98), L354 (= L328), Y431 (≠ C387), N517 (≠ M470), H519 (= H472), S562 (≠ N514)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (vs. gap), A77 (≠ G85), G82 (= G90), G83 (≠ S91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (≠ A98), L227 (= L221), V228 (= V222), A265 (= A255), A518 (≠ M471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ N516)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
31% identity, 96% coverage: 8:533/550 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 (vs. gap), A78 (≠ G85), G83 (= G90), G84 (≠ S91), N88 (= N95), A89 (≠ G96), V91 (≠ A98), L228 (= L221), V229 (= V222), A266 (= A255), A519 (≠ M471), H520 (= H472), D552 (= D503), I553 (≠ A504), S563 (≠ N514), P564 (≠ T515), M565 (≠ N516)
- binding p-nitrophenol: L93 (= L100), V361 (≠ C334), Y432 (≠ C387), L434 (= L389), G562 (= G513), S563 (≠ N514)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
31% identity, 96% coverage: 8:533/550 of query aligns to 2:581/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P83), L92 (= L100), Q306 (vs. gap), V360 (≠ C334), Y431 (≠ C387), L433 (= L389), N514 (≠ A467), S516 (= S469), N517 (≠ M470), H519 (= H472), G561 (= G513), S562 (≠ N514)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (vs. gap), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (≠ A98), L227 (= L221), V228 (= V222), A265 (= A255), A518 (≠ M471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ N516)
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, 96% coverage: 8:533/550 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 (≠ A98), Y431 (≠ C387), N517 (≠ M470), D576 (≠ A528), K580 (≠ E532)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (vs. gap), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (≠ A98), L227 (= L221), V228 (= V222), A265 (= A255), A518 (≠ M471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ N516)
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, 96% coverage: 8:533/550 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 (≠ A98), L354 (= L328), H421 (≠ E375), L429 (≠ T383), Y431 (≠ C387), N517 (≠ M470)
- binding dihydroflavine-adenine dinucleotide: G8 (= G14), G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (vs. gap), A77 (≠ G85), G82 (= G90), G83 (≠ S91), N87 (= N95), A88 (≠ G96), V90 (≠ A98), L227 (= L221), V228 (= V222), A265 (= A255), A518 (≠ M471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), P563 (≠ T515), M564 (≠ N516)
6ze3A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment (4-methoxycarbonylphenyl)methylazanium (see paper)
31% identity, 96% coverage: 8:533/550 of query aligns to 2:581/585 of 6ze3A
- binding (4-methoxycarbonylphenyl)methylazanium: A88 (≠ G96), L354 (= L328), Y431 (≠ C387), N517 (≠ M470)
- binding dihydroflavine-adenine dinucleotide: G10 (= G16), I11 (≠ S17), S12 (≠ A18), E32 (= E38), A33 (= A39), W56 (vs. gap), G82 (= G90), G83 (≠ S91), I86 (= I94), N87 (= N95), A88 (≠ G96), V90 (≠ A98), L227 (= L221), V228 (= V222), A265 (= A255), A518 (≠ M471), H519 (= H472), D551 (= D503), I552 (≠ A504), S562 (≠ N514), M564 (≠ N516)
Query Sequence
>PP_1949 FitnessBrowser__Putida:PP_1949
MSEEQPVYDYIIIGAGSAGCVLANRLSANPEHSVLLLEAGSRPKGLWASMPAGVSRVILP
GPTNWAYQSEPDPSLAGRRIYVPRGKALGGSSAINGMAYLRGHREDYDHWVSLGCAGWGW
DDVLPFYKKFEHREEGDEAFRGRDGELWVTDPVFKHPSSQAFIESCVEAGIPRLDDLNAP
SPEGTGFLQFTIKGGRRHSAATAFLQPVLKRPNLHVLTGALVQKIVIEAERATGVEYSLG
NQSIFAAAREIILSAGAIDSPKLLMLSGVGPAQELTRHGIPVLRDLPGVGENLHDHVYVH
SGIETDRVASLNKDLRGLRSVLQGMNYLLRGKGCLTMGASQAVALAQVLPGARRPDTQIN
YRPLSWHFNKQGLVEIGKDNAVTISTCQLNPLSRGRLTLKSSNPIDAPAIYPNYFGNERD
MVAAIAAVRKVREISCVGPLAKHIVNISPPDSMSDGEIADYIRQEGASSMMHWVGSCKMG
IDSMAVVDERLKVRGLQGLRVVDASIMPTITSGNTNAPTIMIGEKGAAMILEDRLIGPRR
KFRSESARAN
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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