SitesBLAST
Comparing Ac3H11_3320 FitnessBrowser__acidovorax_3H11:Ac3H11_3320 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)
33% identity, 98% coverage: 6:556/562 of query aligns to 5:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G12), G13 (= G14), S14 (≠ T15), A15 (= A16), E35 (= E36), A36 (= A37), W47 (= W63), P65 (= P81), G67 (= G83), V180 (≠ A236), A214 (= A275), G215 (= G276), A218 (≠ N279), T270 (≠ M358), Y391 (≠ F490), A424 (= A530), I435 (≠ T541), N436 (= N542)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
33% identity, 100% coverage: 1:560/562 of query aligns to 9:530/532 of 4mjwA
- active site: I333 (≠ L363), P377 (= P409), N378 (≠ T410), V464 (≠ I489), H466 (= H491), V509 (≠ G539), N510 (= N540)
- binding flavin-adenine dinucleotide: G20 (= G12), G22 (= G14), S23 (≠ T15), E44 (= E36), A45 (= A37), W71 (= W63), R89 (= R82), A90 (≠ G83), G95 (= G88), C96 (= C89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (= I96), R231 (≠ Q235), A232 (= A236), T269 (≠ A275), G270 (= G276), D273 (≠ N279), Y465 (≠ F490), H466 (= H491), A500 (= A530), N510 (= N540), P511 (≠ T541), N512 (= N542), V515 (≠ T545)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
34% identity, 98% coverage: 6:556/562 of query aligns to 84:636/654 of A0A248QE08
- TA 93:94 (= TA 15:16) binding
- E114 (= E36) binding
- L162 (≠ T85) binding
- S166 (≠ C89) binding
- NATL 170:173 (≠ NGMI 93:96) binding
- V298 (≠ A236) binding
- C432 (≠ S361) binding
- R451 (≠ H381) binding
- Y466 (≠ H395) binding
- Q486 (≠ S403) binding
- G622 (≠ N542) binding
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
33% identity, 100% coverage: 1:560/562 of query aligns to 9:530/530 of 3ljpA
- active site: I333 (≠ L363), P377 (= P409), N378 (≠ T410), A464 (≠ I489), H466 (= H491), V509 (≠ G539), N510 (= N540)
- binding dihydroflavine-adenine dinucleotide: G22 (= G14), S23 (≠ T15), E44 (= E36), A45 (= A37), W71 (= W63), R89 (= R82), A90 (≠ G83), G95 (= G88), C96 (= C89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (= I96), A232 (= A236), T269 (≠ A275), D273 (≠ N279), Y465 (≠ F490), H466 (= H491), D499 (= D529), A500 (= A530), N510 (= N540), P511 (≠ T541), N512 (= N542), V515 (≠ T545)
6yrvAAA structure of fap after illumination at 100k (see paper)
34% identity, 98% coverage: 6:556/562 of query aligns to 8:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H381), N499 (≠ F490)
- binding flavin-adenine dinucleotide: G14 (= G12), G16 (= G14), T17 (= T15), A18 (= A16), L37 (≠ I35), E38 (= E36), A39 (= A37), F58 (≠ I56), W64 (= W63), A82 (≠ P81), G89 (= G88), S90 (≠ C89), N94 (= N93), A95 (≠ G94), T96 (≠ M95), L97 (≠ I96), M191 (≠ N204), V222 (≠ A236), C264 (≠ S274), A265 (= A275), G266 (= G276), H269 (≠ N279), N499 (≠ F490), A534 (= A530), Q544 (≠ N540), T545 (= T541), G546 (≠ N542)
- binding heptadecane: V377 (≠ Q383), G379 (vs. gap), M380 (≠ L385), G386 (= G391), T389 (≠ L394), Y390 (≠ H395), F393 (= F397), T408 (= T401), Q410 (≠ S403)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
33% identity, 99% coverage: 1:556/562 of query aligns to 9:526/527 of 2jbvA
- active site: I333 (≠ L363), P377 (= P409), N378 (≠ T410), V464 (≠ I489), H466 (= H491), V509 (≠ G539), N510 (= N540)
- 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 (= G14), S23 (≠ T15), E44 (= E36), A45 (= A37), W71 (= W63), A90 (≠ G83), G95 (= G88), C96 (= C89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (= I96), R231 (≠ Q235), A232 (= A236), T269 (≠ A275), G270 (= G276), D273 (≠ N279), V464 (≠ I489), Y465 (≠ F490), H466 (= H491), D499 (= D529), A500 (= A530), N510 (= N540), P511 (≠ T541), N512 (= N542), V515 (≠ T545)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
34% identity, 98% coverage: 6:556/562 of query aligns to 24:569/578 of 5nccA
- active site: R347 (≠ A342), L420 (≠ V404), I421 (≠ C405), S507 (≠ I489), A509 (≠ H491), G552 (= G539), Q553 (≠ N540)
- binding flavin-adenine dinucleotide: G30 (= G12), G32 (= G14), T33 (= T15), A34 (= A16), L53 (≠ I35), E54 (= E36), A55 (= A37), F74 (≠ I56), W80 (= W63), A98 (≠ P81), G100 (= G83), G105 (= G88), S106 (≠ C89), N110 (= N93), A111 (≠ G94), T112 (≠ M95), L113 (≠ I96), V238 (≠ A236), A278 (= A275), H282 (≠ N279), L286 (= L283), N508 (≠ F490), Q553 (≠ N540), T554 (= T541), G555 (≠ N542), V558 (≠ T545)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
31% identity, 98% coverage: 6:558/562 of query aligns to 2:563/565 of 5oc1A
- active site: V339 (≠ I344), N413 (= N406), A414 (vs. gap), I499 (= I489), H501 (= H491), A544 (≠ G539), H545 (≠ N540)
- binding 4-methoxybenzoic acid: Y91 (≠ G94), I356 (≠ P360), I390 (≠ L385), F396 (≠ G391), T412 (≠ C405), I499 (= I489), H501 (= H491), H545 (≠ N540)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), N11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W60 (= W63), P78 (= P81), G80 (= G83), G85 (= G88), S86 (≠ C89), H90 (≠ N93), Y91 (≠ G94), V93 (≠ I96), V230 (≠ A236), S270 (= S274), A271 (= A275), G272 (= G276), F500 (= F490), H545 (≠ N540), T546 (= T541), Q547 (≠ N542), I550 (≠ T545)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
31% identity, 98% coverage: 6:558/562 of query aligns to 2:563/565 of 3fimB
- active site: V339 (≠ I344), N413 (= N406), A414 (vs. gap), I499 (= I489), H501 (= H491), A544 (≠ G539), H545 (≠ N540)
- binding flavin-adenine dinucleotide: G8 (= G12), N11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W60 (= W63), P78 (= P81), G80 (= G83), G85 (= G88), S86 (≠ C89), H90 (≠ N93), Y91 (≠ G94), V93 (≠ I96), V230 (≠ A236), S270 (= S274), A271 (= A275), F500 (= F490), H501 (= H491), H545 (≠ N540), T546 (= T541), Q547 (≠ N542), I550 (≠ T545)
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, 99% coverage: 1:557/562 of query aligns to 1:528/531 of E4QP00
- V101 (≠ I92) mutation to H: Abolishes activity.
- M103 (≠ G94) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V404) 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 (≠ N406) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I489) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F490) 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 (= H491) mutation to A: Abolishes activity.
- N511 (= N540) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
34% identity, 98% coverage: 6:557/562 of query aligns to 2:524/525 of 4udqA
- active site: L331 (= L363), F364 (≠ C405), W365 (≠ N406), V461 (≠ I489), H463 (= H491), A506 (≠ G539), N507 (= N540)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), T11 (= T15), A12 (= A16), E32 (= E36), A33 (= A37), W64 (= W63), G88 (= G83), G93 (= G88), G94 (≠ C89), N98 (= N93), M99 (≠ G94), V101 (≠ I96), V229 (≠ A236), T261 (≠ S274), A262 (= A275), W462 (≠ F490), H463 (= H491), A497 (= A530), N507 (= N540), T508 (= T541), N509 (= N542), T512 (= T545)
8bxlB Patulin synthase from penicillium expansum
30% identity, 98% coverage: 3:553/562 of query aligns to 11:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G12), G22 (= G14), T23 (= T15), A24 (= A16), E44 (= E36), A45 (= A37), W80 (= W63), G100 (= G83), G105 (= G88), S106 (≠ C89), R109 (≠ I92), N110 (= N93), Y111 (≠ G94), A113 (≠ I96), L253 (≠ Q235), A254 (= A236), A288 (= A275), Q292 (≠ N279), F525 (= F490), D559 (= D529), A560 (= A530), H570 (≠ N540), P571 (≠ T541), Q572 (≠ N542), L575 (≠ T545)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
33% identity, 97% coverage: 7:553/562 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ V404), G361 (≠ C405), H444 (≠ I489), H446 (= H491), G487 (= G539), P488 (≠ N540)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), S11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W58 (= W63), R77 (= R82), G78 (= G83), G83 (= G88), S84 (≠ C89), L87 (≠ I92), H88 (≠ N93), A89 (≠ G94), M90 (= M95), G91 (≠ I96), V218 (≠ A236), A251 (= A275), G252 (= G276), E255 (≠ N279), H445 (≠ F490), A478 (= A530), P488 (≠ N540), I489 (≠ T541), H490 (≠ N542)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G94), S314 (= S353), H444 (≠ I489), H446 (= H491)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
33% identity, 97% coverage: 7:553/562 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ V404), G361 (≠ C405), H444 (≠ I489), H446 (= H491), G487 (= G539), P488 (≠ N540)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), S11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W58 (= W63), R77 (= R82), G78 (= G83), R79 (≠ K84), G83 (= G88), S84 (≠ C89), H88 (≠ N93), A89 (≠ G94), G91 (≠ I96), R217 (≠ Q235), V218 (≠ A236), A251 (= A275), E255 (≠ N279), H445 (≠ F490), A478 (= A530), P488 (≠ N540), I489 (≠ T541), H490 (≠ N542)
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)
27% identity, 99% coverage: 2:556/562 of query aligns to 37:597/602 of Q3L245
- N100 (≠ L64) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I92) modified: Tele-8alpha-FAD histidine
- N344 (= N312) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H491) active site, Proton acceptor
- H581 (≠ N540) active site
Sites not aligning to the query:
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
27% identity, 99% coverage: 2:556/562 of query aligns to 12:572/577 of 4h7uA
- active site: A343 (≠ N336), V426 (≠ C405), Y510 (≠ I489), H512 (= H491), A555 (≠ G539), H556 (≠ N540)
- 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 (= G12), G24 (= G14), T25 (= T15), A26 (= A16), E46 (= E36), A47 (= A37), W74 (= W63), G99 (= G88), C100 (= C89), H103 (≠ I92), N104 (= N93), G105 (= G94), V107 (≠ I96), L242 (≠ Q235), V243 (≠ A236), G282 (≠ A275), G283 (= G276), A286 (≠ N279), H512 (= H491), A546 (= A530), H556 (≠ N540), T557 (= T541), Q558 (≠ N542), V561 (≠ T545)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
28% identity, 98% coverage: 4:556/562 of query aligns to 2:562/569 of 4ynuA
- active site: V341 (≠ E347), F412 (≠ V404), W413 (≠ C405), N501 (≠ I489), H503 (= H491), G545 (= G539), H546 (≠ N540)
- binding flavin-adenine dinucleotide: G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (= Y52), F55 (≠ I56), W61 (= W63), R79 (≠ P81), G81 (= G83), G86 (= G88), T87 (≠ C89), N91 (= N93), G92 (= G94), T232 (≠ Q235), A233 (= A236), A273 (= A275), G274 (= G276), R277 (≠ N279), F502 (= F490), A536 (= A530), H546 (≠ N540), L547 (≠ T541), V548 (≠ N542), L551 (≠ T545)
- binding D-glucono-1,5-lactone: Y51 (= Y52), E411 (≠ S403), A496 (≠ D484), N497 (≠ I485), R499 (≠ T487), R499 (≠ T487), N501 (≠ I489), H503 (= H491), H546 (≠ N540)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
28% identity, 98% coverage: 4:556/562 of query aligns to 2:562/566 of 7vzsA
- binding D-glucal: Y6 (≠ T8), L22 (= L24), N25 (≠ D27), Y51 (= Y52), I349 (≠ P355), Q356 (= Q362), E411 (≠ S403), E444 (≠ P436), W445 (≠ E437), K448 (≠ Q440), R499 (≠ T487), N501 (≠ I489), H546 (≠ N540)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (= Y52), F55 (≠ I56), W61 (= W63), R79 (≠ P81), G81 (= G83), G86 (= G88), T87 (≠ C89), N91 (= N93), G92 (= G94), M93 (= M95), A94 (≠ I96), T232 (≠ Q235), A233 (= A236), A273 (= A275), G274 (= G276), R277 (≠ N279), F502 (= F490), A536 (= A530), H546 (≠ N540), L547 (≠ T541), V548 (≠ N542), L551 (≠ T545)
Sites not aligning to the query:
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
28% identity, 98% coverage: 4:556/562 of query aligns to 3:563/570 of 4yntA
- active site: V342 (≠ E347), F413 (≠ V404), W414 (≠ C405), N502 (≠ I489), H504 (= H491), G546 (= G539), H547 (≠ N540)
- binding dihydroflavine-adenine dinucleotide: G13 (= G14), T14 (= T15), S15 (≠ A16), E35 (= E36), A36 (= A37), F56 (≠ I56), W62 (= W63), R80 (≠ P81), G82 (= G83), G87 (= G88), T88 (≠ C89), N92 (= N93), G93 (= G94), M94 (= M95), A95 (≠ I96), A234 (= A236), A274 (= A275), R278 (≠ N279), F503 (= F490), A537 (= A530), H547 (≠ N540), L548 (≠ T541), V549 (≠ N542), L552 (≠ T545)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
30% identity, 100% coverage: 2:561/562 of query aligns to 1:584/586 of 6ze7B
- binding dihydroflavine-adenine dinucleotide: G9 (= G12), G11 (= G14), I12 (≠ T15), S13 (≠ A16), E33 (= E36), A34 (= A37), W57 (vs. gap), A78 (≠ G83), G83 (= G88), G84 (≠ C89), N88 (= N93), A89 (≠ G94), V91 (≠ I96), L228 (≠ Q235), V229 (≠ A236), A266 (= A275), A519 (≠ F490), H520 (= H491), D552 (= D529), I553 (≠ A530), S563 (≠ N540), P564 (≠ T541), M565 (≠ N542)
- binding p-nitrophenol: L93 (≠ M98), V361 (≠ L346), Y432 (≠ C405), L434 (= L407), G562 (= G539), S563 (≠ N540)
Query Sequence
>Ac3H11_3320 FitnessBrowser__acidovorax_3H11:Ac3H11_3320
MSDTTFDTIIIGGGTAGALLANRLSADGRHRVLLIEAGRKDDYHWIHIPVGYLYCIGNPR
TDWLYNTEPDTGLNGRTLRYPRGKTLGGCSSINGMIYMRGQARDYDQWAELTGDAGWRWD
NALPYFRRHEDHWRLDQPGSANENFKRLHGNKATGSTGEWRVEKQRLRWDVLDAFAHAAQ
QAGIPATDDFNGGSNEGVGYFEVNQKSGWRWNTAKAFLRPTCYGRPNFEMWTSAQAAKLV
VETQPDGSKRCTGVMVWDGQEMVTAQATGEVILSAGAVNSPQLLQLSGIGPAALLRQHGI
DVAVDLPGVGANLQDHLQIRAVFKVQGVQTLNTMANSLVGKAKIGLEYALKRSGPMSMAP
SQLGAFTRSSADQPYPNIEYHVQPLSLDAFGEPLHSFPAFTASVCNLNPTSRGTVNIKSA
DFKTAPAIAPNYLSTPEDRQVAADSLRVTRRIVAQPALAKYRPEEWKPGVQFESDEDLAR
LAGDIATTIFHPVGTTKMGLDGDPMAVLDAQMRVRDGRGGVVAGLRVVDAGAMPTITSGN
TNSPTLMMAEKAAEWIIAARRA
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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