SitesBLAST
Comparing WP_012113637.1 NCBI__GCF_000017645.1:WP_012113637.1 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)
36% identity, 99% coverage: 4:533/533 of query aligns to 5:455/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), S14 (≠ T13), A15 (= A14), E35 (= E34), A36 (= A35), W47 (= W61), P65 (= P79), G67 (= G81), V180 (≠ A220), A214 (= A254), G215 (= G255), A218 (≠ Q258), T270 (≠ L336), Y391 (= Y469), A424 (= A502), I435 (≠ T513), N436 (≠ A514)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
37% identity, 99% coverage: 4:532/533 of query aligns to 24:573/578 of 5nccA
- active site: R347 (≠ K321), L420 (≠ V383), I421 (≠ T384), S507 (≠ I468), A509 (≠ H470), G552 (≠ A511), Q553 (≠ N512)
- binding flavin-adenine dinucleotide: G30 (= G10), G32 (= G12), T33 (= T13), A34 (= A14), L53 (= L33), E54 (= E34), A55 (= A35), F74 (≠ L54), W80 (= W61), A98 (≠ P79), G100 (= G81), G105 (= G86), S106 (= S87), N110 (= N91), A111 (≠ G92), T112 (≠ M93), L113 (≠ I94), V238 (≠ A220), A278 (= A254), H282 (≠ Q258), L286 (= L262), N508 (≠ Y469), Q553 (≠ N512), T554 (= T513), G555 (≠ A514), V558 (= V517)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
37% identity, 99% coverage: 4:532/533 of query aligns to 84:640/654 of A0A248QE08
- TA 93:94 (= TA 13:14) binding FAD
- E114 (= E34) binding FAD
- L162 (≠ G83) binding FAD
- S166 (= S87) binding FAD
- NATL 170:173 (≠ NGMI 91:94) binding FAD
- V298 (≠ A220) binding FAD
- C432 (≠ L340) binding hexadecanoate
- R451 (≠ F359) binding hexadecanoate
- Y466 (≠ H362) binding hexadecanoate
- Q486 (≠ G382) binding hexadecanoate
- G622 (≠ A514) binding FAD
6yrvAAA structure of fap after illumination at 100k (see paper)
37% identity, 99% coverage: 4:532/533 of query aligns to 8:564/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ F359), N499 (≠ Y469)
- binding flavin-adenine dinucleotide: G14 (= G10), G16 (= G12), T17 (= T13), A18 (= A14), L37 (= L33), E38 (= E34), A39 (= A35), F58 (≠ L54), W64 (= W61), A82 (≠ P79), G89 (= G86), S90 (= S87), N94 (= N91), A95 (≠ G92), T96 (≠ M93), L97 (≠ I94), M191 (≠ N189), V222 (≠ A220), C264 (≠ A253), A265 (= A254), G266 (= G255), H269 (≠ Q258), N499 (≠ Y469), A534 (= A502), Q544 (≠ N512), T545 (= T513), G546 (≠ A514)
- binding heptadecane: V377 (≠ M361), G379 (vs. gap), M380 (vs. gap), G386 (vs. gap), T389 (vs. gap), Y390 (≠ H362), F393 (≠ Y365), T408 (= T380), Q410 (≠ G382)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
35% identity, 99% coverage: 3:530/533 of query aligns to 13:528/532 of 4mjwA
- active site: I333 (≠ L319), P377 (≠ I381), N378 (≠ G382), V464 (≠ I468), H466 (= H470), V509 (≠ A511), N510 (= N512)
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), S23 (≠ T13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ Q219), A232 (= A220), T269 (≠ A254), G270 (= G255), D273 (≠ Q258), Y465 (= Y469), H466 (= H470), A500 (= A502), N510 (= N512), P511 (≠ T513), N512 (≠ A514), V515 (= V517)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
35% identity, 99% coverage: 3:529/533 of query aligns to 13:527/527 of 2jbvA
- active site: I333 (≠ L319), P377 (≠ I381), N378 (≠ G382), V464 (≠ I468), H466 (= H470), V509 (≠ A511), N510 (= N512)
- 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 (= G12), S23 (≠ T13), E44 (= E34), A45 (= A35), W71 (= W61), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ Q219), A232 (= A220), T269 (≠ A254), G270 (= G255), D273 (≠ Q258), V464 (≠ I468), Y465 (= Y469), H466 (= H470), D499 (= D501), A500 (= A502), N510 (= N512), P511 (≠ T513), N512 (≠ A514), V515 (= V517)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
35% identity, 99% coverage: 3:530/533 of query aligns to 13:528/530 of 3ljpA
- active site: I333 (≠ L319), P377 (≠ I381), N378 (≠ G382), A464 (≠ I468), H466 (= H470), V509 (≠ A511), N510 (= N512)
- binding dihydroflavine-adenine dinucleotide: G22 (= G12), S23 (≠ T13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (≠ S87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), A232 (= A220), T269 (≠ A254), D273 (≠ Q258), Y465 (= Y469), H466 (= H470), D499 (= D501), A500 (= A502), N510 (= N512), P511 (≠ T513), N512 (≠ A514), V515 (= V517)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
32% identity, 99% coverage: 4:531/533 of query aligns to 2:564/565 of 5oc1A
- active site: V339 (≠ K321), N413 (≠ V383), A414 (≠ T384), I499 (= I468), H501 (= H470), A544 (= A511), H545 (≠ N512)
- binding 4-methoxybenzoic acid: Y91 (≠ G92), I356 (≠ L336), I390 (vs. gap), F396 (≠ Y365), T412 (≠ G382), I499 (= I468), H501 (= H470), H545 (≠ N512)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), N11 (≠ T13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (= S87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (≠ A220), S270 (≠ A253), A271 (= A254), G272 (= G255), F500 (≠ Y469), H545 (≠ N512), T546 (= T513), Q547 (≠ A514), I550 (≠ V517)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 99% coverage: 4:531/533 of query aligns to 2:564/565 of 3fimB
- active site: V339 (≠ K321), N413 (≠ V383), A414 (≠ T384), I499 (= I468), H501 (= H470), A544 (= A511), H545 (≠ N512)
- binding flavin-adenine dinucleotide: G8 (= G10), N11 (≠ T13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (= S87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (≠ A220), S270 (≠ A253), A271 (= A254), F500 (≠ Y469), H501 (= H470), H545 (≠ N512), T546 (= T513), Q547 (≠ A514), I550 (≠ V517)
8bxlB Patulin synthase from penicillium expansum (see paper)
32% identity, 99% coverage: 3:532/533 of query aligns to 13:590/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), T23 (= T13), A24 (= A14), E44 (= E34), A45 (= A35), W80 (= W61), G100 (= G81), G105 (= G86), S106 (= S87), R109 (≠ I90), N110 (= N91), Y111 (≠ G92), A113 (≠ I94), L253 (≠ Q219), A254 (= A220), A288 (= A254), Q292 (= Q258), F525 (≠ Y469), D559 (= D501), A560 (= A502), H570 (≠ N512), P571 (≠ T513), Q572 (≠ A514), L575 (≠ V517)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
33% identity, 98% coverage: 3:525/533 of query aligns to 1:501/509 of 3t37A
- active site: F360 (≠ I381), G361 (= G382), H444 (≠ I468), H446 (= H470), G487 (≠ A511), P488 (≠ N512)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (≠ T13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), R79 (≠ K82), G83 (= G86), S84 (= S87), H88 (≠ N91), A89 (≠ G92), G91 (≠ I94), R217 (≠ Q219), V218 (≠ A220), A251 (= A254), E255 (≠ Q258), H445 (≠ Y469), A478 (= A502), P488 (≠ N512), I489 (≠ T513), H490 (≠ A514)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
33% identity, 98% coverage: 3:525/533 of query aligns to 1:501/508 of 4ha6A
- active site: F360 (≠ I381), G361 (= G382), H444 (≠ I468), H446 (= H470), G487 (≠ A511), P488 (≠ N512)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (≠ T13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), G83 (= G86), S84 (= S87), L87 (≠ I90), H88 (≠ N91), A89 (≠ G92), M90 (= M93), G91 (≠ I94), V218 (≠ A220), A251 (= A254), G252 (= G255), E255 (≠ Q258), H445 (≠ Y469), A478 (= A502), P488 (≠ N512), I489 (≠ T513), H490 (≠ A514)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G92), S314 (≠ G316), H444 (≠ I468), H446 (= H470)
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: 4:532/533 of query aligns to 6:531/531 of E4QP00
- V101 (≠ I90) mutation to H: Abolishes activity.
- M103 (≠ G92) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V383) 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 (≠ I468) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ Y469) 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 (= H470) mutation to A: Abolishes activity.
- N511 (= N512) 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: 4:528/533 of query aligns to 2:523/525 of 4udqA
- active site: L331 (= L328), F364 (≠ T384), W365 (≠ Q385), V461 (≠ I468), H463 (= H470), A506 (= A511), N507 (= N512)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), T11 (= T13), A12 (= A14), E32 (= E34), A33 (= A35), W64 (= W61), G88 (= G81), G93 (= G86), G94 (≠ S87), N98 (= N91), M99 (≠ G92), V101 (≠ I94), V229 (≠ A220), T261 (≠ A253), A262 (= A254), W462 (≠ Y469), H463 (= H470), A497 (= A502), N507 (= N512), T508 (= T513), N509 (≠ A514), T512 (≠ V517)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
30% identity, 100% coverage: 3:533/533 of query aligns to 4:568/570 of 4yntA
- active site: V342 (vs. gap), F413 (vs. gap), W414 (vs. gap), N502 (≠ I468), H504 (= H470), G546 (≠ A511), H547 (≠ N512)
- binding dihydroflavine-adenine dinucleotide: G13 (= G12), T14 (= T13), S15 (≠ A14), E35 (= E34), A36 (= A35), F56 (≠ A55), W62 (= W61), R80 (≠ P79), G82 (= G81), G87 (= G86), T88 (≠ S87), N92 (= N91), G93 (= G92), M94 (= M93), A95 (≠ I94), A234 (= A220), A274 (= A254), R278 (≠ Q258), F503 (≠ Y469), A537 (= A502), H547 (≠ N512), L548 (≠ T513), V549 (≠ A514), L552 (≠ V517)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
30% identity, 100% coverage: 3:533/533 of query aligns to 3:567/569 of 4ynuA
- active site: V341 (vs. gap), F412 (vs. gap), W413 (vs. gap), N501 (≠ I468), H503 (= H470), G545 (≠ A511), H546 (≠ N512)
- binding flavin-adenine dinucleotide: G12 (= G12), T13 (= T13), S14 (≠ A14), E34 (= E34), A35 (= A35), Y51 (≠ S51), F55 (≠ A55), W61 (= W61), R79 (≠ P79), G81 (= G81), G86 (= G86), T87 (≠ S87), N91 (= N91), G92 (= G92), T232 (≠ Q219), A233 (= A220), A273 (= A254), G274 (= G255), R277 (≠ Q258), F502 (≠ Y469), A536 (= A502), H546 (≠ N512), L547 (≠ T513), V548 (≠ A514), L551 (≠ V517)
- binding D-glucono-1,5-lactone: Y51 (≠ S51), E411 (vs. gap), A496 (≠ R463), N497 (≠ T464), R499 (≠ Q466), R499 (≠ Q466), N501 (≠ I468), H503 (= H470), H546 (≠ N512)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
30% identity, 99% coverage: 3:532/533 of query aligns to 3:566/566 of 7vzsA
- binding D-glucal: Y6 (= Y6), L22 (= L22), N25 (≠ D25), Y51 (≠ S51), I349 (≠ G332), Q356 (≠ G339), E411 (vs. gap), E444 (≠ Q415), W445 (≠ E416), K448 (≠ D419), R499 (≠ Q466), N501 (≠ I468), H546 (≠ N512), K563 (≠ R529), A566 (= A532)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), T13 (= T13), S14 (≠ A14), E34 (= E34), A35 (= A35), Y51 (≠ S51), F55 (≠ A55), W61 (= W61), R79 (≠ P79), G81 (= G81), G86 (= G86), T87 (≠ S87), N91 (= N91), G92 (= G92), M93 (= M93), A94 (≠ I94), T232 (≠ Q219), A233 (= A220), A273 (= A254), G274 (= G255), R277 (≠ Q258), F502 (≠ Y469), A536 (= A502), H546 (≠ N512), L547 (≠ T513), V548 (≠ A514), L551 (≠ V517)
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)
30% identity, 98% coverage: 4:528/533 of query aligns to 41:597/602 of Q3L245
- N100 (≠ R62) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I90) modified: Tele-8alpha-FAD histidine
- N344 (= N291) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H470) active site, Proton acceptor
- H581 (≠ N512) active site
Sites not aligning to the query:
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
30% identity, 98% coverage: 4:528/533 of query aligns to 16:572/577 of 4h7uA
- active site: A343 (≠ K321), V426 (≠ T384), Y510 (≠ I468), H512 (= H470), A555 (= A511), H556 (≠ N512)
- 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 (= G10), G24 (= G12), T25 (= T13), A26 (= A14), E46 (= E34), A47 (= A35), W74 (= W61), G99 (= G86), C100 (≠ S87), H103 (≠ I90), N104 (= N91), G105 (= G92), V107 (≠ I94), L242 (= L225), V243 (≠ D226), G282 (≠ A254), G283 (= G255), A286 (≠ Q258), H512 (= H470), A546 (= A502), H556 (≠ N512), T557 (= T513), Q558 (≠ A514), V561 (= V517)
6xuuA Crystallographic structure of oligosaccharide dehydrogenase from pycnoporus cinnabarinus, glucose-bound form (see paper)
28% identity, 99% coverage: 3:530/533 of query aligns to 14:587/589 of 6xuuA
- binding beta-D-glucopyranose: E35 (= E24), N67 (= N60), H83 (≠ P79), N104 (≠ R100), D108 (= D104), S139 (≠ E130), A140 (= A131), N142 (vs. gap), T166 (≠ V148), D169 (≠ G151), T188 (≠ A167), W213 (vs. gap), A225 (≠ G201), Y226 (= Y202), Q329 (≠ A297), N330 (≠ T298), A331 (≠ R299), Q357 (= Q306), F414 (= F359), K474 (≠ R430), N517 (≠ Q466), G520 (vs. gap), A522 (vs. gap), V524 (≠ I468), H526 (= H470), H569 (≠ N512)
- binding flavin-adenine dinucleotide: G21 (= G10), G23 (= G12), L24 (≠ T13), T25 (≠ A14), E45 (= E34), A46 (= A35), F66 (= F59), W72 (≠ T65), H83 (≠ P79), G85 (= G81), G90 (= G86), S91 (= S87), N95 (= N91), G96 (= G92), A97 (≠ M93), A98 (≠ I94), M244 (≠ Q219), A245 (= A220), A286 (= A254), Q290 (= Q258), A525 (≠ Y469), A559 (= A502), H569 (≠ N512), L570 (≠ T513), S571 (≠ A514), L574 (≠ V517)
- binding alpha-D-glucopyranose: G96 (= G92), F414 (= F359), W428 (≠ T384)
Query Sequence
>WP_012113637.1 NCBI__GCF_000017645.1:WP_012113637.1
MDSFDYIVVGGGTAGAILAARLSEDPRRTVLLLEAGGTDRGFWVPIPAGFSKLLAGSAFN
WRFHTEPEENTYDRPIVVPRGKGLGGSTLINGMIFVRGQRQDYDGWAQLGATGWGWDDVK
PYFKKFETFEASDIDTNERGTDGPINIVRVGERPVLSEVFIKAAEQAGYPRNPDYNGKVQ
DGFGYYQVNQKNGRRWTVVDGYLRPALSRPNLKVATHAQALCLTLDGRRVTGVTYRQGGR
EVAATARAEVLLAAGAVQSPQLLELSGIGHPETLKAAGIPVVHALSGVGNNYRDHFATRM
NWRVKQPVTLNEQTRGLALAKAVAQYFLTRKGILTLGTGLAHGFVKTRPGLEGPDVQYFF
MHASYANAADRALDRQPGMTIGVTQLRPQSIGSIHVTSPDPFKAPAIRPNFLAVQEDRDC
LVEGMKLARRIIEQPAMDPYRAFEMNPGPDVRSDADFLEFARRTGQTIYHPVGTCAMGTG
PAAVVDPRLKVIGLEGLRVVDASVMPTIVSANTAAAVMMIAEKAADMIRADAR
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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