SitesBLAST
Comparing PP_0056 FitnessBrowser__Putida:PP_0056 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, 97% coverage: 4:538/550 of query aligns to 78:641/654 of A0A248QE08
- TA 93:94 (≠ PA 19:20) binding
- E114 (= E40) binding
- L162 (≠ V89) binding
- S166 (≠ C93) binding
- NATL 170:173 (≠ NGMI 97:100) binding
- V298 (= V224) binding
- C432 (≠ S344) binding
- R451 (≠ H364) binding
- Y466 (vs. gap) binding
- Q486 (≠ S386) binding
- G622 (≠ C518) binding
6yrvAAA structure of fap after illumination at 100k (see paper)
36% identity, 97% coverage: 4:538/550 of query aligns to 2:565/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H364), N499 (≠ F473)
- binding flavin-adenine dinucleotide: G14 (= G16), G16 (= G18), T17 (≠ P19), A18 (= A20), L37 (= L39), E38 (= E40), A39 (= A41), F58 (≠ I60), W64 (= W67), A82 (≠ P85), G89 (= G92), S90 (≠ C93), N94 (= N97), A95 (≠ G98), T96 (≠ M99), L97 (≠ I100), M191 (≠ N193), V222 (= V224), C264 (= C257), A265 (= A258), G266 (= G259), H269 (≠ G262), N499 (≠ F473), A534 (= A506), Q544 (≠ N516), T545 (= T517), G546 (≠ C518)
- binding heptadecane: V377 (≠ Q366), G379 (vs. gap), M380 (vs. gap), G386 (vs. gap), T389 (vs. gap), Y390 (vs. gap), F393 (≠ L370), T408 (= T384), Q410 (≠ S386)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
36% identity, 97% coverage: 4:538/550 of query aligns to 18:574/578 of 5nccA
- active site: R347 (≠ M327), L420 (≠ V387), I421 (≠ C388), S507 (≠ I472), A509 (≠ H474), G552 (= G515), Q553 (≠ N516)
- binding flavin-adenine dinucleotide: G30 (= G16), G32 (= G18), T33 (≠ P19), A34 (= A20), L53 (= L39), E54 (= E40), A55 (= A41), F74 (≠ I60), W80 (= W67), A98 (≠ P85), G100 (= G87), G105 (= G92), S106 (≠ C93), N110 (= N97), A111 (≠ G98), T112 (≠ M99), L113 (≠ I100), V238 (= V224), A278 (= A258), H282 (≠ G262), L286 (≠ I266), N508 (≠ F473), Q553 (≠ N516), T554 (= T517), G555 (≠ C518), V558 (≠ T521)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 95% coverage: 11:530/550 of query aligns to 3:502/509 of 3t37A
- active site: F360 (≠ V387), G361 (≠ C388), H444 (≠ I472), H446 (= H474), G487 (= G515), P488 (≠ N516)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), S11 (≠ P19), A12 (= A20), E32 (= E40), A33 (= A41), W58 (= W67), R77 (= R86), G78 (= G87), R79 (≠ K88), G83 (= G92), S84 (≠ C93), H88 (≠ N97), A89 (≠ G98), G91 (≠ I100), R217 (≠ Q223), V218 (= V224), A251 (= A258), E255 (≠ G262), H445 (≠ F473), A478 (= A506), P488 (≠ N516), I489 (≠ T517), H490 (≠ C518)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 95% coverage: 11:530/550 of query aligns to 3:502/508 of 4ha6A
- active site: F360 (≠ V387), G361 (≠ C388), H444 (≠ I472), H446 (= H474), G487 (= G515), P488 (≠ N516)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), S11 (≠ P19), A12 (= A20), E32 (= E40), A33 (= A41), W58 (= W67), R77 (= R86), G78 (= G87), G83 (= G92), S84 (≠ C93), L87 (≠ I96), H88 (≠ N97), A89 (≠ G98), M90 (= M99), G91 (≠ I100), V218 (= V224), A251 (= A258), G252 (= G259), E255 (≠ G262), H445 (≠ F473), A478 (= A506), P488 (≠ N516), I489 (≠ T517), H490 (≠ C518)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G98), S314 (= S344), H444 (≠ I472), H446 (= H474)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
31% identity, 96% coverage: 10:538/550 of query aligns to 5:456/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G16), G13 (= G18), S14 (≠ P19), A15 (= A20), E35 (= E40), A36 (= A41), W47 (= W67), P65 (= P85), G67 (= G87), V180 (= V224), A214 (= A258), G215 (= G259), A218 (≠ G262), T270 (≠ M341), Y391 (≠ F473), A424 (= A506), I435 (≠ T517), N436 (≠ C518)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
34% identity, 97% coverage: 6:537/550 of query aligns to 10:531/532 of 4mjwA
- active site: I333 (≠ M325), P377 (≠ A385), N378 (≠ S386), V464 (≠ I472), H466 (= H474), V509 (≠ G515), N510 (= N516)
- binding flavin-adenine dinucleotide: G20 (= G16), G22 (= G18), S23 (≠ P19), E44 (= E40), A45 (= A41), W71 (= W67), R89 (= R86), A90 (≠ G87), G95 (= G92), C96 (= C93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (= I100), R231 (≠ Q223), A232 (≠ V224), T269 (≠ A258), G270 (= G259), D273 (≠ G262), Y465 (≠ F473), H466 (= H474), A500 (= A506), N510 (= N516), P511 (≠ T517), N512 (≠ C518), V515 (≠ T521)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
34% identity, 96% coverage: 6:532/550 of query aligns to 10:526/527 of 2jbvA
- active site: I333 (≠ M325), P377 (≠ A385), N378 (≠ S386), V464 (≠ I472), H466 (= H474), V509 (≠ G515), N510 (= N516)
- 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 (= G18), S23 (≠ P19), E44 (= E40), A45 (= A41), W71 (= W67), A90 (≠ G87), G95 (= G92), C96 (= C93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (= I100), R231 (≠ Q223), A232 (≠ V224), T269 (≠ A258), G270 (= G259), D273 (≠ G262), V464 (≠ I472), Y465 (≠ F473), H466 (= H474), D499 (= D505), A500 (= A506), N510 (= N516), P511 (≠ T517), N512 (≠ C518), V515 (≠ T521)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
32% identity, 95% coverage: 10:532/550 of query aligns to 2:561/565 of 5oc1A
- active site: V339 (≠ M327), N413 (= N389), A414 (vs. gap), I499 (= I472), H501 (= H474), A544 (≠ G515), H545 (≠ N516)
- binding 4-methoxybenzoic acid: Y91 (≠ G98), I356 (vs. gap), I390 (≠ L368), F396 (≠ G374), T412 (≠ C388), I499 (= I472), H501 (= H474), H545 (≠ N516)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), N11 (≠ P19), A12 (= A20), E32 (= E40), A33 (= A41), W60 (= W67), P78 (= P85), G80 (= G87), G85 (= G92), S86 (≠ C93), H90 (≠ N97), Y91 (≠ G98), V93 (≠ I100), V230 (= V224), S270 (≠ C257), A271 (= A258), G272 (= G259), F500 (= F473), H545 (≠ N516), T546 (= T517), Q547 (≠ C518), I550 (≠ T521)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 96% coverage: 6:532/550 of query aligns to 10:526/530 of 3ljpA
- active site: I333 (≠ M325), P377 (≠ A385), N378 (≠ S386), A464 (≠ I472), H466 (= H474), V509 (≠ G515), N510 (= N516)
- binding dihydroflavine-adenine dinucleotide: G22 (= G18), S23 (≠ P19), E44 (= E40), A45 (= A41), W71 (= W67), R89 (= R86), A90 (≠ G87), G95 (= G92), C96 (= C93), H99 (≠ I96), N100 (= N97), S101 (≠ G98), I103 (= I100), A232 (≠ V224), T269 (≠ A258), D273 (≠ G262), Y465 (≠ F473), H466 (= H474), D499 (= D505), A500 (= A506), N510 (= N516), P511 (≠ T517), N512 (≠ C518), V515 (≠ T521)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 95% coverage: 10:532/550 of query aligns to 2:561/565 of 3fimB
- active site: V339 (≠ M327), N413 (= N389), A414 (vs. gap), I499 (= I472), H501 (= H474), A544 (≠ G515), H545 (≠ N516)
- binding flavin-adenine dinucleotide: G8 (= G16), N11 (≠ P19), A12 (= A20), E32 (= E40), A33 (= A41), W60 (= W67), P78 (= P85), G80 (= G87), G85 (= G92), S86 (≠ C93), H90 (≠ N97), Y91 (≠ G98), V93 (≠ I100), V230 (= V224), S270 (≠ C257), A271 (= A258), F500 (= F473), H501 (= H474), H545 (≠ N516), T546 (= T517), Q547 (≠ C518), I550 (≠ T521)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
30% identity, 97% coverage: 8:538/550 of query aligns to 3:569/570 of 4yntA
- active site: V342 (vs. gap), F413 (≠ V387), W414 (≠ C388), N502 (≠ I472), H504 (= H474), G546 (= G515), H547 (≠ N516)
- binding dihydroflavine-adenine dinucleotide: G13 (= G18), T14 (≠ P19), S15 (≠ A20), E35 (= E40), A36 (= A41), F56 (≠ I60), W62 (= W67), R80 (≠ P85), G82 (= G87), G87 (= G92), T88 (≠ C93), N92 (= N97), G93 (= G98), M94 (= M99), A95 (≠ I100), A234 (≠ V224), A274 (= A258), R278 (≠ G262), F503 (= F473), A537 (= A506), H547 (≠ N516), L548 (≠ T517), V549 (≠ C518), L552 (≠ T521)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
30% identity, 97% coverage: 8:538/550 of query aligns to 2:568/569 of 4ynuA
- active site: V341 (vs. gap), F412 (≠ V387), W413 (≠ C388), N501 (≠ I472), H503 (= H474), G545 (= G515), H546 (≠ N516)
- binding flavin-adenine dinucleotide: G12 (= G18), T13 (≠ P19), S14 (≠ A20), E34 (= E40), A35 (= A41), Y51 (= Y56), F55 (≠ I60), W61 (= W67), R79 (≠ P85), G81 (= G87), G86 (= G92), T87 (≠ C93), N91 (= N97), G92 (= G98), T232 (≠ Q223), A233 (≠ V224), A273 (= A258), G274 (= G259), R277 (≠ G262), F502 (= F473), A536 (= A506), H546 (≠ N516), L547 (≠ T517), V548 (≠ C518), L551 (≠ T521)
- binding D-glucono-1,5-lactone: Y51 (= Y56), E411 (≠ S386), A496 (≠ K467), N497 (≠ I468), R499 (≠ T470), R499 (≠ T470), N501 (≠ I472), H503 (= H474), H546 (≠ N516)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
30% identity, 96% coverage: 8:536/550 of query aligns to 2:566/566 of 7vzsA
- binding D-glucal: Y6 (= Y12), L22 (= L28), N25 (≠ D31), Y51 (= Y56), I349 (≠ P338), Q356 (= Q345), E411 (≠ S386), E444 (≠ P419), W445 (≠ Q420), K448 (≠ R423), R499 (≠ T470), N501 (≠ I472), H546 (≠ N516), K563 (≠ L533), A566 (= A536)
- binding flavin-adenine dinucleotide: G10 (= G16), G12 (= G18), T13 (≠ P19), S14 (≠ A20), E34 (= E40), A35 (= A41), Y51 (= Y56), F55 (≠ I60), W61 (= W67), R79 (≠ P85), G81 (= G87), G86 (= G92), T87 (≠ C93), N91 (= N97), G92 (= G98), M93 (= M99), A94 (≠ I100), T232 (≠ Q223), A233 (≠ V224), A273 (= A258), G274 (= G259), R277 (≠ G262), F502 (= F473), A536 (= A506), H546 (≠ N516), L547 (≠ T517), V548 (≠ C518), L551 (≠ T521)
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, 96% coverage: 7:536/550 of query aligns to 3:531/531 of E4QP00
- V101 (≠ I96) mutation to H: Abolishes activity.
- M103 (≠ G98) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ Q362) 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 (≠ H364) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I472) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F473) 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 (= H474) mutation to A: Abolishes activity.
- N511 (= N516) 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, 95% coverage: 9:533/550 of query aligns to 1:524/525 of 4udqA
- active site: L331 (≠ M327), F364 (≠ Y363), W365 (≠ H364), V461 (≠ I472), H463 (= H474), A506 (≠ G515), N507 (= N516)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), T11 (≠ P19), A12 (= A20), E32 (= E40), A33 (= A41), W64 (= W67), G88 (= G87), G93 (= G92), G94 (≠ C93), N98 (= N97), M99 (≠ G98), V101 (≠ I100), V229 (= V224), T261 (≠ C257), A262 (= A258), W462 (≠ F473), H463 (= H474), A497 (= A506), N507 (= N516), T508 (= T517), N509 (≠ C518), T512 (= T521)
8bxlB Patulin synthase from penicillium expansum
30% identity, 95% coverage: 7:529/550 of query aligns to 11:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G16), G22 (= G18), T23 (≠ P19), A24 (= A20), E44 (= E40), A45 (= A41), W80 (= W67), G100 (= G87), G105 (= G92), S106 (≠ C93), R109 (≠ I96), N110 (= N97), Y111 (≠ G98), A113 (≠ I100), L253 (≠ Q223), A254 (≠ V224), A288 (= A258), Q292 (≠ G262), F525 (= F473), D559 (= D505), A560 (= A506), H570 (≠ N516), P571 (≠ T517), Q572 (≠ C518), L575 (≠ T521)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
29% identity, 96% coverage: 8:534/550 of query aligns to 1:581/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G16), G11 (= G18), I12 (≠ P19), S13 (≠ A20), E33 (= E40), A34 (= A41), W57 (≠ P53), A78 (≠ G87), G83 (= G92), G84 (≠ C93), N88 (= N97), A89 (≠ G98), V91 (≠ I100), L228 (≠ Q223), V229 (= V224), A266 (= A258), A519 (≠ F473), H520 (= H474), D552 (= D505), I553 (≠ A506), S563 (≠ N516), P564 (≠ T517), M565 (≠ C518)
- binding p-nitrophenol: L93 (≠ M102), V361 (vs. gap), Y432 (≠ C388), L434 (= L390), G562 (= G515), S563 (≠ N516)
7aa2A Chaetomium thermophilum fad-dependent oxidoreductase in complex with abts (see paper)
29% identity, 95% coverage: 10:534/550 of query aligns to 2:580/584 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 (= W49), A88 (≠ G98), V90 (≠ I100), L354 (vs. gap), Y431 (≠ C388), N517 (≠ I472), H519 (= H474), S562 (≠ N516)
- binding dihydroflavine-adenine dinucleotide: G8 (= G16), G10 (= G18), I11 (≠ P19), S12 (≠ A20), E32 (= E40), A33 (= A41), W56 (≠ P53), A77 (≠ G87), G82 (= G92), G83 (≠ C93), I86 (= I96), N87 (= N97), A88 (≠ G98), V90 (≠ I100), L227 (≠ Q223), V228 (= V224), A265 (= A258), A518 (≠ F473), H519 (= H474), D551 (= D505), I552 (≠ A506), S562 (≠ N516), P563 (≠ T517), M564 (≠ C518)
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
29% identity, 95% coverage: 10:534/550 of query aligns to 2:580/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P85), L92 (≠ M102), Q306 (≠ H299), V360 (vs. gap), Y431 (≠ C388), L433 (= L390), N514 (≠ G469), S516 (≠ T471), N517 (≠ I472), H519 (= H474), G561 (= G515), S562 (≠ N516)
- binding dihydroflavine-adenine dinucleotide: G8 (= G16), G10 (= G18), I11 (≠ P19), S12 (≠ A20), E32 (= E40), A33 (= A41), W56 (≠ P53), A77 (≠ G87), G82 (= G92), G83 (≠ C93), N87 (= N97), A88 (≠ G98), V90 (≠ I100), L227 (≠ Q223), V228 (= V224), A265 (= A258), A518 (≠ F473), H519 (= H474), D551 (= D505), I552 (≠ A506), S562 (≠ N516), P563 (≠ T517), M564 (≠ C518)
Query Sequence
>PP_0056 FitnessBrowser__Putida:PP_0056
MHMPSADSVFDYVVVGAGPAGCLLANRLSADPSCRVLLLEAGGRDNYPWIHIPVGYLYCI
GNPRTDWCFKTEAQPGLGGRALGYPRGKVLGGCSSINGMIYMRGQAADYDHWAAQGNDGW
AWKDVLPLFKASENHFAGASEHHGAEGEWRVERQRYSWPILDAFRDAAEQSGIGKVDDFN
TGDNQGCGYFQVNQRSGVRWNASKAFLRPIKDRANLTVLTGVQVDQVLLDNTRARAVKAL
WQGAWHEFAARREIILCAGAVGSPGILQRSGIGPRQLLESLGIGVRHDMPGVGGNLQDHL
QLRLIYQIRNTRTLNQMANSLWGKMGMGLRYLYDRSGPLAMAPSQLGAFVRSSPEQATAN
LQYHVQPLSLERFGEPLHQFPAFTASVCNLRPASRGRIDICSTDMNSTPRIDPNYLSAPQ
DLRVAADAIRLTRRIVQAPALAAFEPKEYLPGPALQSEEDLFEAAGKIGTTIFHPVGTCR
MGNGAMDVVDNQLRVHGIPGLRVADASIMPQITSGNTCSPTLMIAEKAAQLILKGAATQT
YLNQDALPTP
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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