SitesBLAST
Comparing H281DRAFT_03365 FitnessBrowser__Burk376:H281DRAFT_03365 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)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
33% identity, 96% coverage: 7:529/546 of query aligns to 25:569/578 of 5nccA
- active site: R347 (= R323), L420 (≠ V384), I421 (≠ W385), S507 (≠ V469), A509 (≠ H471), G552 (≠ T512), Q553 (≠ N513)
- binding flavin-adenine dinucleotide: G30 (= G12), G32 (= G14), T33 (= T15), A34 (= A16), L53 (≠ V35), E54 (= E36), A55 (= A37), F74 (≠ L56), W80 (= W63), A98 (≠ P81), G100 (= G83), G105 (= G88), S106 (= S89), N110 (= N93), A111 (≠ G94), T112 (≠ L95), L113 (= L96), V238 (= V221), A278 (= A256), H282 (≠ G260), L286 (= L264), N508 (≠ Y470), Q553 (≠ N513), T554 (= T514), G555 (≠ N515), V558 (= V518)
6yrvAAA structure of fap after illumination at 100k (see paper)
33% identity, 96% coverage: 7:529/546 of query aligns to 9:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ V360), N499 (≠ Y470)
- binding flavin-adenine dinucleotide: G14 (= G12), G16 (= G14), T17 (= T15), A18 (= A16), L37 (≠ V35), E38 (= E36), A39 (= A37), F58 (≠ L56), W64 (= W63), A82 (≠ P81), G89 (= G88), S90 (= S89), N94 (= N93), A95 (≠ G94), T96 (≠ L95), L97 (= L96), M191 (≠ T190), V222 (= V221), C264 (≠ S255), A265 (= A256), G266 (= G257), H269 (≠ G260), N499 (≠ Y470), A534 (≠ G503), Q544 (≠ N513), T545 (= T514), G546 (≠ N515)
- binding heptadecane: V377 (≠ A362), G379 (= G364), M380 (vs. gap), G386 (vs. gap), T389 (vs. gap), Y390 (vs. gap), F393 (= F366), T408 (≠ S381), Q410 (≠ G383)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
33% identity, 96% coverage: 7:529/546 of query aligns to 85:636/654 of A0A248QE08
- TA 93:94 (= TA 15:16) binding
- E114 (= E36) binding
- L162 (≠ G85) binding
- S166 (= S89) binding
- NATL 170:173 (≠ NGLL 93:96) binding
- V298 (= V221) binding
- C432 (≠ A341) binding
- R451 (≠ V360) binding
- Y466 (vs. gap) binding
- Q486 (≠ G383) binding
- G622 (≠ N515) binding
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
33% identity, 96% coverage: 7:531/546 of query aligns to 3:563/565 of 5oc1A
- active site: V339 (≠ R323), N413 (≠ V384), A414 (≠ W385), I499 (≠ V469), H501 (= H471), A544 (≠ T512), H545 (≠ N513)
- binding 4-methoxybenzoic acid: Y91 (≠ G94), I356 (≠ L342), I390 (vs. gap), F396 (vs. gap), T412 (≠ G383), I499 (≠ V469), H501 (= H471), H545 (≠ N513)
- 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 (= S89), H90 (≠ N93), Y91 (≠ G94), V93 (≠ L96), V230 (= V221), S270 (= S255), A271 (= A256), G272 (= G257), F500 (≠ Y470), H545 (≠ N513), T546 (= T514), Q547 (≠ N515), I550 (≠ V518)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 96% coverage: 7:531/546 of query aligns to 3:563/565 of 3fimB
- active site: V339 (≠ R323), N413 (≠ V384), A414 (≠ W385), I499 (≠ V469), H501 (= H471), A544 (≠ T512), H545 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G12), N11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W60 (= W63), P78 (= P81), G80 (= G83), G85 (= G88), S86 (= S89), H90 (≠ N93), Y91 (≠ G94), V93 (≠ L96), V230 (= V221), S270 (= S255), A271 (= A256), F500 (≠ Y470), H501 (= H471), H545 (≠ N513), T546 (= T514), Q547 (≠ N515), I550 (≠ V518)
8b7sA Crystal structure of the chloramphenicol-inactivating oxidoreductase from novosphingobium sp (see paper)
32% identity, 97% coverage: 3:530/546 of query aligns to 2:451/458 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 (= V221), A214 (= A256), G215 (= G257), A218 (≠ G260), T270 (≠ A312), Y391 (= Y470), A424 (≠ G503), I435 (≠ T514), N436 (= N515)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
32% identity, 96% coverage: 5:530/546 of query aligns to 3:563/569 of 4ynuA
- active site: V341 (≠ A320), F412 (≠ V384), W413 (= W385), N501 (≠ V469), H503 (= H471), G545 (≠ T512), H546 (≠ N513)
- binding flavin-adenine dinucleotide: G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (≠ F52), F55 (≠ D57), W61 (= W63), R79 (≠ P81), G81 (= G83), G86 (= G88), T87 (≠ S89), N91 (= N93), G92 (= G94), T232 (≠ Q220), A233 (≠ V221), A273 (= A256), G274 (= G257), R277 (≠ G260), F502 (≠ Y470), A536 (≠ G503), H546 (≠ N513), L547 (≠ T514), V548 (≠ N515), L551 (≠ V518)
- binding D-glucono-1,5-lactone: Y51 (≠ F52), E411 (≠ G383), A496 (≠ D464), N497 (= N465), R499 (≠ S467), R499 (≠ S467), N501 (≠ V469), H503 (= H471), H546 (≠ N513)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
32% identity, 96% coverage: 5:530/546 of query aligns to 4:564/570 of 4yntA
- active site: V342 (≠ A320), F413 (≠ V384), W414 (= W385), N502 (≠ V469), H504 (= H471), G546 (≠ T512), H547 (≠ N513)
- binding dihydroflavine-adenine dinucleotide: G13 (= G14), T14 (= T15), S15 (≠ A16), E35 (= E36), A36 (= A37), F56 (≠ D57), W62 (= W63), R80 (≠ P81), G82 (= G83), G87 (= G88), T88 (≠ S89), N92 (= N93), G93 (= G94), M94 (≠ L95), A95 (≠ L96), A234 (≠ V221), A274 (= A256), R278 (≠ G260), F503 (≠ Y470), A537 (≠ G503), H547 (≠ N513), L548 (≠ T514), V549 (≠ N515), L552 (≠ V518)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
34% identity, 97% coverage: 7:534/546 of query aligns to 15:531/532 of 4mjwA
- active site: I333 (≠ V330), P377 (≠ V384), N378 (≠ W385), V464 (= V469), H466 (= H471), V509 (≠ T512), N510 (= N513)
- binding flavin-adenine dinucleotide: G20 (= G12), G22 (= G14), S23 (≠ T15), E44 (= E36), A45 (= A37), W71 (= W63), R89 (= R82), A90 (≠ G83), G95 (= G88), C96 (≠ S89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (≠ L96), R231 (≠ Q220), A232 (≠ V221), T269 (≠ A256), G270 (= G257), D273 (≠ G260), Y465 (= Y470), H466 (= H471), A500 (≠ G503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (= V518)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
32% identity, 96% coverage: 5:530/546 of query aligns to 3:563/566 of 7vzsA
- binding D-glucal: Y6 (= Y8), L22 (= L24), N25 (≠ D27), Y51 (≠ F52), I349 (≠ Y328), Q356 (≠ V335), E411 (≠ G383), E444 (= E416), W445 (≠ L417), K448 (≠ N420), R499 (≠ S467), N501 (≠ V469), H546 (≠ N513), K563 (≠ R530)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (≠ F52), F55 (≠ D57), W61 (= W63), R79 (≠ P81), G81 (= G83), G86 (= G88), T87 (≠ S89), N91 (= N93), G92 (= G94), M93 (≠ L95), A94 (≠ L96), T232 (≠ Q220), A233 (≠ V221), A273 (= A256), G274 (= G257), R277 (≠ G260), F502 (≠ Y470), A536 (≠ G503), H546 (≠ N513), L547 (≠ T514), V548 (≠ N515), L551 (≠ V518)
Sites not aligning to the query:
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
34% identity, 96% coverage: 7:530/546 of query aligns to 15:527/527 of 2jbvA
- active site: I333 (≠ V330), P377 (≠ V384), N378 (≠ W385), V464 (= V469), H466 (= H471), V509 (≠ T512), N510 (= N513)
- 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 (≠ S89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (≠ L96), R231 (≠ Q220), A232 (≠ V221), T269 (≠ A256), G270 (= G257), D273 (≠ G260), V464 (= V469), Y465 (= Y470), H466 (= H471), D499 (= D502), A500 (≠ G503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (= V518)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 96% coverage: 7:531/546 of query aligns to 15:528/530 of 3ljpA
- active site: I333 (≠ V330), P377 (≠ V384), N378 (≠ W385), A464 (≠ V469), H466 (= H471), V509 (≠ T512), N510 (= N513)
- binding dihydroflavine-adenine dinucleotide: G22 (= G14), S23 (≠ T15), E44 (= E36), A45 (= A37), W71 (= W63), R89 (= R82), A90 (≠ G83), G95 (= G88), C96 (≠ S89), H99 (≠ I92), N100 (= N93), S101 (≠ G94), I103 (≠ L96), A232 (≠ V221), T269 (≠ A256), D273 (≠ G260), Y465 (= Y470), H466 (= H471), D499 (= D502), A500 (≠ G503), N510 (= N513), P511 (≠ T514), N512 (= N515), V515 (= V518)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
32% identity, 95% coverage: 5:523/546 of query aligns to 1:498/509 of 3t37A
- active site: F360 (≠ C382), G361 (= G383), H444 (≠ V469), H446 (= H471), G487 (≠ T512), P488 (≠ N513)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), S11 (≠ T15), A12 (= A16), E32 (= E36), A33 (= A37), W58 (= W63), R77 (= R82), G78 (= G83), R79 (= R84), G83 (= G88), S84 (= S89), H88 (≠ N93), A89 (≠ G94), G91 (≠ L96), R217 (≠ Q220), V218 (= V221), A251 (= A256), E255 (≠ G260), H445 (≠ Y470), A478 (≠ G503), P488 (≠ N513), I489 (≠ T514), H490 (≠ N515)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
32% identity, 95% coverage: 5:523/546 of query aligns to 1:498/508 of 4ha6A
- active site: F360 (≠ C382), G361 (= G383), H444 (≠ V469), H446 (= H471), G487 (≠ T512), P488 (≠ N513)
- 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 (= S89), L87 (≠ I92), H88 (≠ N93), A89 (≠ G94), M90 (≠ L95), G91 (≠ L96), V218 (= V221), A251 (= A256), G252 (= G257), E255 (≠ G260), H445 (≠ Y470), A478 (≠ G503), P488 (≠ N513), I489 (≠ T514), H490 (≠ N515)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G94), S314 (vs. gap), H444 (≠ V469), H446 (= H471)
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, 97% coverage: 1:529/546 of query aligns to 1:527/531 of E4QP00
- V101 (≠ I92) mutation to H: Abolishes activity.
- M103 (≠ G94) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (≠ 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 (= W385) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (= V469) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ Y470) 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 (= H471) mutation to A: Abolishes activity.
- N511 (= N513) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
32% identity, 96% coverage: 7:529/546 of query aligns to 3:523/525 of 4udqA
- active site: L331 (≠ M326), F364 (≠ V384), W365 (= W385), V461 (= V469), H463 (= H471), A506 (≠ T512), N507 (= N513)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), T11 (= T15), A12 (= A16), E32 (= E36), A33 (= A37), W64 (≠ H58), G88 (= G83), G93 (= G88), G94 (≠ S89), N98 (= N93), M99 (≠ G94), V101 (≠ L96), V229 (= V221), T261 (≠ S255), A262 (= A256), W462 (≠ Y470), H463 (= H471), A497 (≠ G503), N507 (= N513), T508 (= T514), N509 (= N515), T512 (≠ V518)
1cf3A Glucose oxidase from apergillus niger (see paper)
31% identity, 97% coverage: 5:535/546 of query aligns to 17:579/581 of 1cf3A
- active site: T355 (≠ M325), W424 (= W385), N512 (≠ V469), H514 (= H471), S556 (≠ T512), H557 (≠ N513)
- binding flavin-adenine dinucleotide: G24 (= G12), L27 (≠ T15), T28 (≠ A16), E48 (= E36), S49 (≠ A37), H76 (≠ W63), R93 (≠ P81), G95 (= G83), N96 (≠ R84), G100 (= G88), S101 (= S89), N105 (= N93), G106 (= G94), T108 (≠ L96), Y247 (≠ Q220), V248 (= V221), A287 (= A256), Y513 (= Y470), H514 (= H471), H557 (≠ N513), V558 (≠ T514), M559 (≠ N515), F562 (≠ V518)
5nitA Glucose oxidase mutant a2 (see paper)
30% identity, 97% coverage: 5:535/546 of query aligns to 17:579/581 of 5nitA
- active site: T355 (≠ M325), W424 (= W385), N512 (≠ V469), H514 (= H471), S556 (≠ T512), H557 (≠ N513)
- binding flavin-adenine dinucleotide: G24 (= G12), L27 (≠ T15), V28 (≠ A16), E48 (= E36), S49 (≠ A37), H76 (≠ W63), R93 (≠ P81), G95 (= G83), N96 (≠ R84), G100 (= G88), S101 (= S89), N105 (= N93), G106 (= G94), T108 (≠ L96), Y247 (≠ Q220), V248 (= V221), A287 (= A256), Y513 (= Y470), G547 (= G503), H557 (≠ N513), V558 (≠ T514), M559 (≠ N515), F562 (≠ V518)
- binding oxygen molecule: H514 (= H471), H557 (≠ N513), V558 (≠ T514)
8bxlB Patulin synthase from penicillium expansum
29% identity, 96% coverage: 2:526/546 of query aligns to 10:583/590 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 (= S89), R109 (≠ I92), N110 (= N93), Y111 (≠ G94), A113 (≠ L96), L253 (≠ Q220), A254 (≠ V221), A288 (= A256), Q292 (≠ G260), F525 (≠ Y470), D559 (= D502), A560 (≠ G503), H570 (≠ N513), P571 (≠ T514), Q572 (≠ N515), L575 (≠ V518)
1gpeB Glucose oxidase from penicillium amagasakiense (see paper)
30% identity, 98% coverage: 5:537/546 of query aligns to 24:587/587 of 1gpeB
- active site: T361 (vs. gap), W430 (= W385), N518 (≠ V469), H520 (= H471), S562 (≠ T512), H563 (≠ N513)
- binding beta-D-mannopyranose: R341 (= R305), E491 (= E445), Y496 (≠ R450)
- binding flavin-adenine dinucleotide: G31 (= G12), G33 (= G14), L34 (≠ T15), T35 (≠ A16), I54 (≠ V35), E55 (= E36), K56 (≠ A37), Q83 (≠ W63), K99 (≠ P81), G101 (= G83), G103 (= G85), G106 (= G88), S107 (= S89), N111 (= N93), G112 (= G94), S114 (≠ L96), M253 (≠ Q220), V254 (= V221), A292 (≠ S255), A293 (= A256), G294 (= G257), W450 (vs. gap), W519 (≠ Y470), H520 (= H471), G553 (= G503), H563 (≠ N513), V564 (≠ T514), M565 (≠ N515), F568 (≠ V518)
- binding alpha-D-mannopyranose: E491 (= E445), G495 (= G449), Q500 (≠ T454)
Query Sequence
>H281DRAFT_03365 FitnessBrowser__Burk376:H281DRAFT_03365
MKSYTADYVIVGAGTAGCVLANRLTEDPAIKVILVEAGERDRHPFIHVPAGFVRLLDHPT
VTWRYRTEADAGTSGRAILFPRGRGLGGSSAINGLLYVRPFAEDIDSWEQSGANGWNFKN
CLPFYSRSETWTEGSSPQRGTHGPIQVSRVKNPPEICGAVVEAAQRTGLDFVDDPNSDTR
GPSIWYYQQTRDGRRRSSAARGYLRPAMARPNLTVVTGLQVSTLEMNGTHVSGINGTTGA
GIPVQIRATREVILSAGVVGTPRLLEMSGIGDKAVLDNAGVKTRIALPGVGNNLQDHYVV
RLGYRVRGAGTANERAHGLALAREMMRYVVSGTGVLTYSAALVGGFAQTRLATRPDVQFV
IAPGSFAEGRIGVLESEPGVSCGVWQMRPESRGHVHITSSEITAAPTIAPSYLSSELDRN
TMVEGLKIGRRIFAQPEVARYIVDETVPGRQADTDEALLQYVRDNGSTVYHAVGTCRMGE
DEMSVVDSEMRVRGTTGLRVVDGSVMPSITSTNTNATVLMLAERAADMIRSPMAAHASST
YSKETV
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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