SitesBLAST
Comparing PfGW456L13_1082 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1082 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: 2:540/566 of query aligns to 2:457/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G11), G13 (= G13), S14 (= S14), A15 (= A15), E35 (= E35), A36 (= A36), W47 (= W64), P65 (≠ G82), G67 (= G84), V180 (≠ T224), A214 (≠ S260), G215 (= G261), A218 (= A264), T270 (= T337), Y391 (≠ F474), A424 (= A507), I435 (≠ L518), N436 (= N519)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
34% identity, 95% coverage: 3:542/566 of query aligns to 22:578/578 of 5nccA
- active site: R347 (vs. gap), L420 (≠ M388), I421 (≠ G389), S507 (≠ A473), A509 (≠ H475), G552 (= G516), Q553 (≠ N517)
- binding flavin-adenine dinucleotide: G30 (= G11), G32 (= G13), T33 (≠ S14), A34 (= A15), L53 (= L34), E54 (= E35), A55 (= A36), F74 (≠ L57), W80 (= W64), A98 (≠ G82), G100 (= G84), G105 (= G89), S106 (= S90), N110 (= N94), A111 (≠ G95), T112 (≠ M96), L113 (≠ C97), V238 (≠ T224), A278 (≠ S260), H282 (≠ A264), L286 (≠ I268), N508 (≠ F474), Q553 (≠ N517), T554 (≠ L518), G555 (≠ N519), V558 (≠ T522)
6yrvAAA structure of fap after illumination at 100k (see paper)
34% identity, 96% coverage: 3:544/566 of query aligns to 6:571/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H365), N499 (≠ F474)
- binding flavin-adenine dinucleotide: G14 (= G11), G16 (= G13), T17 (≠ S14), A18 (= A15), L37 (= L34), E38 (= E35), A39 (= A36), F58 (≠ L57), W64 (= W64), A82 (≠ G82), G89 (= G89), S90 (= S90), N94 (= N94), A95 (≠ G95), T96 (≠ M96), L97 (≠ C97), M191 (≠ V193), V222 (≠ T224), C264 (= C259), A265 (≠ S260), G266 (= G261), H269 (≠ A264), N499 (≠ F474), A534 (= A507), Q544 (≠ N517), T545 (≠ L518), G546 (≠ N519)
- binding heptadecane: V377 (≠ L367), G379 (vs. gap), M380 (≠ V369), G386 (= G375), T389 (vs. gap), Y390 (vs. gap), 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: 3:539/566 of query aligns to 82:642/654 of A0A248QE08
- TA 93:94 (≠ SA 14:15) binding
- E114 (= E35) binding
- L162 (≠ G86) binding
- S166 (= S90) binding
- NATL 170:173 (≠ NGMC 94:97) binding
- V298 (≠ T224) binding
- C432 (≠ F345) binding
- R451 (≠ H365) binding
- Y466 (vs. gap) binding
- Q486 (≠ H387) binding
- G622 (≠ N519) binding
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 95% coverage: 3:537/566 of query aligns to 12:530/530 of 3ljpA
- active site: I333 (≠ A347), P377 (≠ M388), N378 (≠ G389), A464 (= A473), H466 (= H475), V509 (≠ G516), N510 (= N517)
- binding dihydroflavine-adenine dinucleotide: G22 (= G13), S23 (= S14), E44 (= E35), A45 (= A36), W71 (= W64), R89 (= R83), A90 (≠ G84), G95 (= G89), C96 (≠ S90), H99 (≠ I93), N100 (= N94), S101 (≠ G95), I103 (≠ C97), A232 (≠ T224), T269 (≠ S260), D273 (≠ A264), Y465 (≠ F474), 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)
34% identity, 95% coverage: 3:537/566 of query aligns to 12:530/532 of 4mjwA
- active site: I333 (≠ A347), P377 (≠ M388), N378 (≠ G389), V464 (≠ A473), H466 (= H475), V509 (≠ G516), N510 (= N517)
- binding flavin-adenine dinucleotide: G20 (= G11), G22 (= G13), S23 (= S14), E44 (= E35), A45 (= A36), W71 (= W64), R89 (= R83), A90 (≠ G84), G95 (= G89), C96 (≠ S90), H99 (≠ I93), N100 (= N94), S101 (≠ G95), I103 (≠ C97), R231 (≠ L223), A232 (≠ T224), T269 (≠ S260), G270 (= G261), D273 (≠ A264), Y465 (≠ F474), 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)
34% identity, 94% coverage: 3:534/566 of query aligns to 12:527/527 of 2jbvA
- active site: I333 (≠ A347), P377 (≠ M388), 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 (= G13), S23 (= S14), E44 (= E35), A45 (= A36), W71 (= W64), A90 (≠ G84), G95 (= G89), C96 (≠ S90), H99 (≠ I93), N100 (= N94), S101 (≠ G95), I103 (≠ C97), R231 (≠ L223), A232 (≠ T224), T269 (≠ S260), G270 (= G261), D273 (≠ A264), V464 (≠ A473), Y465 (≠ F474), H466 (= H475), D499 (= D506), A500 (= A507), N510 (= N517), P511 (≠ L518), N512 (= N519), V515 (≠ T522)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
33% identity, 93% coverage: 6:530/566 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ M388), G361 (= G389), H444 (≠ A473), H446 (= H475), G487 (= G516), P488 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), S11 (= S14), A12 (= A15), E32 (= E35), A33 (= A36), W58 (= W64), R77 (= R83), G78 (= G84), G83 (= G89), S84 (= S90), L87 (≠ I93), H88 (≠ N94), A89 (≠ G95), M90 (= M96), G91 (≠ C97), V218 (≠ T224), A251 (≠ S260), G252 (= G261), E255 (≠ A264), H445 (≠ F474), A478 (= A507), P488 (≠ N517), I489 (≠ L518), H490 (≠ N519)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G95), S314 (≠ N324), H444 (≠ A473), H446 (= H475)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
33% identity, 93% coverage: 6:530/566 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ M388), G361 (= G389), H444 (≠ A473), H446 (= H475), G487 (= G516), P488 (≠ N517)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), S11 (= S14), A12 (= A15), E32 (= E35), A33 (= A36), W58 (= W64), R77 (= R83), G78 (= G84), R79 (≠ K85), G83 (= G89), S84 (= S90), H88 (≠ N94), A89 (≠ G95), G91 (≠ C97), R217 (≠ L223), V218 (≠ T224), A251 (≠ S260), E255 (≠ A264), H445 (≠ F474), A478 (= A507), P488 (≠ N517), I489 (≠ L518), H490 (≠ N519)
8bxlB Patulin synthase from penicillium expansum
31% identity, 94% coverage: 2:535/566 of query aligns to 11:588/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G11), G22 (= G13), T23 (≠ S14), A24 (= A15), E44 (= E35), A45 (= A36), W80 (= W64), G100 (= G84), G105 (= G89), S106 (= S90), R109 (≠ I93), N110 (= N94), Y111 (≠ G95), A113 (≠ C97), L253 (= L223), A254 (≠ T224), A288 (≠ S260), Q292 (≠ A264), F525 (= F474), D559 (= D506), A560 (= A507), H570 (≠ N517), P571 (≠ L518), Q572 (≠ N519), L575 (≠ 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, 93% coverage: 5:533/566 of query aligns to 6:527/531 of E4QP00
- V101 (≠ I93) mutation to H: Abolishes activity.
- M103 (≠ G95) 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 (≠ F474) 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
33% identity, 93% coverage: 5:533/566 of query aligns to 2:523/525 of 4udqA
- active site: L331 (≠ T337), F364 (= F384), W365 (≠ Q385), V461 (≠ A473), H463 (= H475), A506 (≠ G516), N507 (= N517)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), T11 (≠ S14), A12 (= A15), E32 (= E35), A33 (= A36), W64 (= W64), G88 (= G84), G93 (= G89), G94 (≠ S90), N98 (= N94), M99 (≠ G95), V101 (≠ C97), V229 (≠ T224), T261 (≠ C259), A262 (≠ S260), W462 (≠ F474), H463 (= H475), A497 (= A507), N507 (= N517), T508 (≠ L518), N509 (= N519), T512 (= T522)
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
28% identity, 93% coverage: 4:527/566 of query aligns to 15:566/577 of 4h7uA
- active site: A343 (= A327), V426 (≠ G389), Y510 (≠ A473), H512 (= H475), A555 (≠ G516), H556 (≠ N517)
- 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 (= G11), G24 (= G13), T25 (≠ S14), A26 (= A15), E46 (= E35), A47 (= A36), W74 (= W64), G99 (= G89), C100 (≠ S90), H103 (≠ I93), N104 (= N94), G105 (= G95), V107 (≠ C97), L242 (= L223), V243 (≠ T224), G282 (≠ S260), G283 (= G261), A286 (= A264), H512 (= H475), A546 (= A507), H556 (≠ N517), T557 (≠ L518), Q558 (≠ N519), V561 (≠ T522)
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, 93% coverage: 4:527/566 of query aligns to 40:591/602 of Q3L245
- N100 (≠ A65) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I93) modified: Tele-8alpha-FAD histidine
- N344 (= N297) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H475) active site, Proton acceptor
- H581 (≠ N517) active site
Sites not aligning to the query:
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
29% identity, 94% coverage: 5:534/566 of query aligns to 4:563/566 of 7vzsA
- binding D-glucal: Y6 (= Y7), L22 (= L23), N25 (≠ D26), Y51 (≠ A51), I349 (= I328), Q356 (≠ N335), E411 (≠ H387), E444 (= E420), W445 (≠ Q421), K448 (≠ Q424), R499 (≠ E471), N501 (≠ A473), H546 (≠ N517), K563 (≠ R534)
- binding flavin-adenine dinucleotide: G10 (= G11), G12 (= G13), T13 (≠ S14), S14 (≠ A15), E34 (= E35), A35 (= A36), Y51 (≠ A51), F55 (= F55), W61 (= W64), R79 (≠ G82), G81 (= G84), G86 (= G89), T87 (≠ S90), N91 (= N94), G92 (= G95), M93 (= M96), A94 (≠ C97), T232 (≠ L223), A233 (≠ T224), A273 (≠ S260), G274 (= G261), R277 (≠ A264), F502 (= F474), A536 (= A507), H546 (≠ N517), L547 (= L518), V548 (≠ N519), L551 (≠ T522)
Sites not aligning to the query:
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
29% identity, 94% coverage: 5:534/566 of query aligns to 4:563/569 of 4ynuA
- active site: V341 (≠ L321), F412 (≠ M388), W413 (≠ G389), N501 (≠ A473), H503 (= H475), G545 (= G516), H546 (≠ N517)
- binding flavin-adenine dinucleotide: G12 (= G13), T13 (≠ S14), S14 (≠ A15), E34 (= E35), A35 (= A36), Y51 (≠ A51), F55 (= F55), W61 (= W64), R79 (≠ G82), G81 (= G84), G86 (= G89), T87 (≠ S90), N91 (= N94), G92 (= G95), T232 (≠ L223), A233 (≠ T224), A273 (≠ S260), G274 (= G261), R277 (≠ A264), F502 (= F474), A536 (= A507), H546 (≠ N517), L547 (= L518), V548 (≠ N519), L551 (≠ T522)
- binding D-glucono-1,5-lactone: Y51 (≠ A51), E411 (≠ H387), A496 (≠ E468), N497 (≠ H469), R499 (≠ E471), R499 (≠ E471), N501 (≠ A473), H503 (= H475), H546 (≠ N517)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
29% identity, 94% coverage: 5:534/566 of query aligns to 5:564/570 of 4yntA
- active site: V342 (≠ L321), F413 (≠ M388), W414 (≠ G389), N502 (≠ A473), H504 (= H475), G546 (= G516), H547 (≠ N517)
- binding dihydroflavine-adenine dinucleotide: G13 (= G13), T14 (≠ S14), S15 (≠ A15), E35 (= E35), A36 (= A36), F56 (= F55), W62 (= W64), R80 (≠ G82), G82 (= G84), G87 (= G89), T88 (≠ S90), N92 (= N94), G93 (= G95), M94 (= M96), A95 (≠ C97), A234 (≠ T224), A274 (≠ S260), R278 (≠ A264), F503 (= F474), A537 (= A507), H547 (≠ N517), L548 (= L518), V549 (≠ N519), L552 (≠ T522)
3q9tA Crystal structure analysis of formate oxidase (see paper)
27% identity, 94% coverage: 3:535/566 of query aligns to 5:571/577 of 3q9tA
- active site: A335 (= A327), D422 (vs. gap), 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 (= G13), T16 (≠ S14), E37 (= E35), A38 (= A36), W65 (= W64), T85 (≠ G82), R86 (= R83), G87 (= G84), G92 (= G89), S93 (= S90), N97 (= N94), Y98 (≠ G95), F99 (≠ M96), T100 (≠ C97), S229 (≠ T224), S265 (≠ C259), Q266 (≠ S260), E270 (≠ A264), F509 (= F474), D542 (= D506), A543 (= A507), R553 (≠ N517), I554 (≠ L518), Q555 (≠ N519), V558 (≠ T522)
5zu2A Effect of mutation (r554a) on fad modification in aspergillus oryzae rib40formate oxidase (see paper)
27% identity, 94% coverage: 3:535/566 of query aligns to 5:571/577 of 5zu2A
- binding flavin-adenine dinucleotide: G15 (= G13), T16 (≠ S14), E37 (= E35), A38 (= A36), W65 (= W64), T85 (≠ G82), R86 (= R83), G87 (= G84), G92 (= G89), S93 (= S90), N97 (= N94), Y98 (≠ G95), T100 (≠ C97), S229 (≠ T224), S265 (≠ C259), Q266 (≠ S260), E270 (≠ A264), F509 (= F474), D542 (= D506), A543 (= A507), A553 (≠ N517), I554 (≠ L518), Q555 (≠ N519), V558 (≠ T522)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
36% identity, 55% coverage: 3:314/566 of query aligns to 1:320/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G11), G11 (= G13), I12 (≠ S14), S13 (≠ A15), E33 (= E35), A34 (= A36), W57 (= W64), A78 (≠ G84), G83 (= G89), G84 (≠ S90), N88 (= N94), A89 (≠ G95), V91 (≠ C97), L228 (= L223), V229 (≠ T224), A266 (≠ S260)
- binding p-nitrophenol: L93 (≠ I99)
Sites not aligning to the query:
- binding dihydroflavine-adenine dinucleotide: 519, 520, 552, 553, 563, 564, 565
- binding p-nitrophenol: 361, 432, 434, 562, 563
Query Sequence
>PfGW456L13_1082 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1082
MSQEFDYIIIGAGSAGNTLATRLTEDAGVTVLLLEAGGPDYRSDFRTQMPAALAFPLQGR
RYNWAYETDPEPHMDGRRMECGRGKGLGGSSLINGMCYIRGNAMDYDGWAKLPGLEDWSY
LDCLPYFRKAETRDIGPNDYHGGDGPVSVTTPKAGNNPLFHAMVEAGVQAGYPRTEDLNG
YQQEGFGPMDRTVTPKGRRASTARGYLDVAKKRSTLTIVTHALTDKILFEGKRAVGVRYL
VGAAEERVEVKARKEVLLCSGAIASPQILQRSGVGPAELLNKLDIPVVHDLPGVGENLQD
HLELYLQYACTQPVSLYPSLLWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRTRPEFEWP
NIQYHFLPVAINYNGSNGVKEHGFQAHMGSMRSPSRGRIQAKSKDPRQHPSILFNYMATE
QDWQEFRDGIRLTREIMQQPALDAFRGREISPGIEVQTDEQLDKFIREHAETAFHPSCSC
KMGTDEMAVVDSEGRVHGMQGLRVVDASIMPIITTGNLNAPTIMMAEKIADKIRGRKPLP
RSTATYYVAGEAPVKGKPVREVSQTA
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