SitesBLAST
Comparing YP_001328534.1 NCBI__GCF_000017145.1:YP_001328534.1 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, 98% coverage: 4:526/531 of query aligns to 5:450/458 of 8b7sA
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), S14 (= S13), A15 (= A14), E35 (= E34), A36 (= A35), W47 (= W61), P65 (= P79), G67 (= G81), V180 (= V218), A214 (= A252), G215 (= G253), A218 (≠ G256), T270 (≠ S314), Y391 (≠ F467), A424 (= A500), I435 (≠ T511), N436 (= N512)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
36% identity, 98% coverage: 4:526/531 of query aligns to 24:569/578 of 5nccA
- active site: R347 (vs. gap), L420 (≠ V381), I421 (≠ C382), S507 (≠ I466), A509 (≠ H468), G552 (= G509), Q553 (≠ N510)
- binding flavin-adenine dinucleotide: G30 (= G10), G32 (= G12), T33 (≠ S13), A34 (= A14), L53 (= L33), E54 (= E34), A55 (= A35), F74 (≠ I54), W80 (= W61), A98 (≠ P79), G100 (= G81), G105 (= G86), S106 (≠ C87), N110 (= N91), A111 (≠ G92), T112 (≠ M93), L113 (≠ I94), V238 (= V218), A278 (= A252), H282 (≠ G256), L286 (≠ I260), N508 (≠ F467), Q553 (≠ N510), T554 (= T511), G555 (≠ N512), V558 (≠ T515)
6yrvAAA structure of fap after illumination at 100k (see paper)
36% identity, 98% coverage: 4:526/531 of query aligns to 8:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H358), N499 (≠ F467)
- binding flavin-adenine dinucleotide: G14 (= G10), G16 (= G12), T17 (≠ S13), A18 (= A14), L37 (= L33), E38 (= E34), A39 (= A35), F58 (≠ I54), W64 (= W61), A82 (≠ P79), G89 (= G86), S90 (≠ C87), N94 (= N91), A95 (≠ G92), T96 (≠ M93), L97 (≠ I94), M191 (≠ N187), V222 (= V218), C264 (≠ S251), A265 (= A252), G266 (= G253), H269 (≠ G256), N499 (≠ F467), A534 (= A500), Q544 (≠ N510), T545 (= T511), G546 (≠ N512)
- binding heptadecane: V377 (≠ Q360), G379 (vs. gap), M380 (vs. gap), G386 (vs. gap), T389 (vs. gap), Y390 (vs. gap), F393 (≠ L364), T408 (= T378), Q410 (≠ S380)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
36% identity, 98% coverage: 4:526/531 of query aligns to 84:636/654 of A0A248QE08
- TA 93:94 (≠ SA 13:14) binding FAD
- E114 (= E34) binding FAD
- L162 (≠ V83) binding FAD
- S166 (≠ C87) binding FAD
- NATL 170:173 (≠ NGMI 91:94) binding FAD
- V298 (= V218) binding FAD
- C432 (≠ S338) binding hexadecanoate
- R451 (≠ H358) binding hexadecanoate
- Y466 (vs. gap) binding hexadecanoate
- Q486 (≠ S380) binding hexadecanoate
- G622 (≠ N512) binding FAD
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
34% identity, 99% coverage: 4:528/531 of query aligns to 2:563/565 of 5oc1A
- active site: V339 (≠ I321), N413 (= N383), A414 (vs. gap), I499 (= I466), H501 (= H468), A544 (≠ G509), H545 (≠ N510)
- binding 4-methoxybenzoic acid: Y91 (≠ G92), I356 (vs. gap), I390 (≠ V362), F396 (≠ G368), T412 (≠ C382), I499 (= I466), H501 (= H468), H545 (≠ N510)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), N11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (≠ C87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (= V218), S270 (= S251), A271 (= A252), G272 (= G253), F500 (= F467), H545 (≠ N510), T546 (= T511), Q547 (≠ N512), I550 (≠ T515)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
33% identity, 99% coverage: 4:528/531 of query aligns to 2:563/565 of 3fimB
- active site: V339 (≠ I321), N413 (= N383), A414 (vs. gap), I499 (= I466), H501 (= H468), A544 (≠ G509), H545 (≠ N510)
- binding flavin-adenine dinucleotide: G8 (= G10), N11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W60 (= W61), P78 (= P79), G80 (= G81), G85 (= G86), S86 (≠ C87), H90 (≠ N91), Y91 (≠ G92), V93 (≠ I94), V230 (= V218), S270 (= S251), A271 (= A252), F500 (= F467), H501 (= H468), H545 (≠ N510), T546 (= T511), Q547 (≠ N512), I550 (≠ T515)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
36% identity, 99% coverage: 4:529/531 of query aligns to 14:529/532 of 4mjwA
- active site: I333 (≠ L340), P377 (≠ A379), N378 (≠ S380), V464 (≠ I466), H466 (= H468), V509 (≠ G509), N510 (= N510)
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (= C87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ H217), A232 (≠ V218), T269 (≠ A252), G270 (= G253), D273 (≠ G256), Y465 (≠ F467), H466 (= H468), A500 (= A500), N510 (= N510), P511 (≠ T511), N512 (= N512), V515 (≠ T515)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
36% identity, 98% coverage: 4:526/531 of query aligns to 14:526/527 of 2jbvA
- active site: I333 (≠ L340), P377 (≠ A379), N378 (≠ S380), V464 (≠ I466), H466 (= H468), V509 (≠ G509), N510 (= N510)
- 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 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), A90 (≠ G81), G95 (= G86), C96 (= C87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), R231 (≠ H217), A232 (≠ V218), T269 (≠ A252), G270 (= G253), D273 (≠ G256), V464 (≠ I466), Y465 (≠ F467), H466 (= H468), D499 (= D499), A500 (= A500), N510 (= N510), P511 (≠ T511), N512 (= N512), V515 (≠ T515)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
36% identity, 99% coverage: 4:529/531 of query aligns to 14:529/530 of 3ljpA
- active site: I333 (≠ L340), P377 (≠ A379), N378 (≠ S380), A464 (≠ I466), H466 (= H468), V509 (≠ G509), N510 (= N510)
- binding dihydroflavine-adenine dinucleotide: G22 (= G12), S23 (= S13), E44 (= E34), A45 (= A35), W71 (= W61), R89 (= R80), A90 (≠ G81), G95 (= G86), C96 (= C87), H99 (≠ I90), N100 (= N91), S101 (≠ G92), I103 (= I94), A232 (≠ V218), T269 (≠ A252), D273 (≠ G256), Y465 (≠ F467), H466 (= H468), D499 (= D499), A500 (= A500), N510 (= N510), P511 (≠ T511), N512 (= N512), V515 (≠ T515)
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
32% identity, 99% coverage: 3:526/531 of query aligns to 3:562/566 of 7vzsA
- binding D-glucal: Y6 (= Y6), L22 (= L22), N25 (= N25), Y51 (= Y50), I349 (≠ L323), Q356 (≠ S330), E411 (≠ S380), E444 (= E413), W445 (≠ A414), K448 (≠ E417), R499 (≠ T464), N501 (≠ I466), H546 (≠ N510)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), T13 (≠ S13), S14 (≠ A14), E34 (= E34), A35 (= A35), Y51 (= Y50), F55 (≠ I54), W61 (= W61), R79 (≠ P79), G81 (= G81), G86 (= G86), T87 (≠ C87), N91 (= N91), G92 (= G92), M93 (= M93), A94 (≠ I94), T232 (≠ H217), A233 (≠ V218), A273 (= A252), G274 (= G253), R277 (≠ G256), F502 (= F467), A536 (= A500), H546 (≠ N510), L547 (≠ T511), V548 (≠ N512), L551 (≠ T515)
Sites not aligning to the query:
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
32% identity, 99% coverage: 3:526/531 of query aligns to 3:562/569 of 4ynuA
- active site: V341 (≠ L315), F412 (≠ V381), W413 (≠ C382), N501 (≠ I466), H503 (= H468), G545 (= G509), H546 (≠ N510)
- binding flavin-adenine dinucleotide: G12 (= G12), T13 (≠ S13), S14 (≠ A14), E34 (= E34), A35 (= A35), Y51 (= Y50), F55 (≠ I54), W61 (= W61), R79 (≠ P79), G81 (= G81), G86 (= G86), T87 (≠ C87), N91 (= N91), G92 (= G92), T232 (≠ H217), A233 (≠ V218), A273 (= A252), G274 (= G253), R277 (≠ G256), F502 (= F467), A536 (= A500), H546 (≠ N510), L547 (≠ T511), V548 (≠ N512), L551 (≠ T515)
- binding D-glucono-1,5-lactone: Y51 (= Y50), E411 (≠ S380), A496 (≠ E461), N497 (≠ I462), R499 (≠ T464), R499 (≠ T464), N501 (≠ I466), H503 (= H468), H546 (≠ N510)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
32% identity, 99% coverage: 3:526/531 of query aligns to 4:563/570 of 4yntA
- active site: V342 (≠ L315), F413 (≠ V381), W414 (≠ C382), N502 (≠ I466), H504 (= H468), G546 (= G509), H547 (≠ N510)
- binding dihydroflavine-adenine dinucleotide: G13 (= G12), T14 (≠ S13), S15 (≠ A14), E35 (= E34), A36 (= A35), F56 (≠ I54), W62 (= W61), R80 (≠ P79), G82 (= G81), G87 (= G86), T88 (≠ C87), N92 (= N91), G93 (= G92), M94 (= M93), A95 (≠ I94), A234 (≠ V218), A274 (= A252), R278 (≠ G256), F503 (= F467), A537 (= A500), H547 (≠ N510), L548 (≠ T511), V549 (≠ N512), L552 (≠ T515)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
34% identity, 98% coverage: 5:523/531 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I466), H446 (= H468), G487 (= G509), P488 (≠ N510)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), G83 (= G86), S84 (≠ C87), L87 (≠ I90), H88 (≠ N91), A89 (≠ G92), M90 (= M93), G91 (≠ I94), V218 (= V218), A251 (= A252), G252 (= G253), E255 (≠ G256), H445 (≠ F467), A478 (= A500), P488 (≠ N510), I489 (≠ T511), H490 (≠ N512)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G92), S314 (vs. gap), H444 (≠ I466), H446 (= H468)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
34% identity, 98% coverage: 5:523/531 of query aligns to 3:501/509 of 3t37A
- active site: F360 (vs. gap), G361 (vs. gap), H444 (≠ I466), H446 (= H468), G487 (= G509), P488 (≠ N510)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), S11 (= S13), A12 (= A14), E32 (= E34), A33 (= A35), W58 (= W61), R77 (= R80), G78 (= G81), R79 (≠ K82), G83 (= G86), S84 (≠ C87), H88 (≠ N91), A89 (≠ G92), G91 (≠ I94), R217 (≠ H217), V218 (= V218), A251 (= A252), E255 (≠ G256), H445 (≠ F467), A478 (= A500), P488 (≠ N510), I489 (≠ T511), H490 (≠ N512)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
34% identity, 99% coverage: 4:527/531 of query aligns to 2:524/525 of 4udqA
- active site: L331 (= L340), F364 (≠ C382), W365 (≠ N383), V461 (≠ I466), H463 (= H468), A506 (≠ G509), N507 (= N510)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), T11 (≠ S13), A12 (= A14), E32 (= E34), A33 (= A35), W64 (= W61), G88 (= G81), G93 (= G86), G94 (≠ C87), N98 (= N91), M99 (≠ G92), V101 (≠ I94), V229 (= V218), T261 (≠ S251), A262 (= A252), W462 (≠ F467), H463 (= H468), A497 (= A500), N507 (= N510), T508 (= T511), N509 (= N512), T512 (= T515)
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: 4:527/531 of query aligns to 6:528/531 of E4QP00
- V101 (≠ I90) mutation to H: Abolishes activity.
- M103 (≠ G92) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V381) 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 (≠ N383) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (≠ I466) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F467) 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 (= H468) mutation to A: Abolishes activity.
- N511 (= N510) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
8bxlB Patulin synthase from penicillium expansum (see paper)
30% identity, 98% coverage: 3:523/531 of query aligns to 13:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G10), G22 (= G12), T23 (≠ S13), A24 (= A14), E44 (= E34), A45 (= A35), W80 (= W61), G100 (= G81), G105 (= G86), S106 (≠ C87), R109 (≠ I90), N110 (= N91), Y111 (≠ G92), A113 (≠ I94), L253 (≠ H217), A254 (≠ V218), A288 (= A252), Q292 (≠ G256), F525 (= F467), D559 (= D499), A560 (= A500), H570 (≠ N510), P571 (≠ T511), Q572 (≠ N512), L575 (≠ T515)
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
30% identity, 98% coverage: 4:526/531 of query aligns to 16:572/577 of 4h7uA
- active site: A343 (= A320), V426 (≠ C382), Y510 (≠ I466), H512 (= H468), A555 (≠ G509), H556 (≠ N510)
- 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 (≠ S13), A26 (= A14), E46 (= E34), A47 (= A35), W74 (= W61), G99 (= G86), C100 (= C87), H103 (≠ I90), N104 (= N91), G105 (= G92), V107 (≠ I94), L242 (≠ H217), V243 (= V218), G282 (≠ A252), G283 (= G253), A286 (≠ G256), H512 (= H468), A546 (= A500), H556 (≠ N510), T557 (= T511), Q558 (≠ N512), V561 (≠ T515)
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: 4:526/531 of query aligns to 41:597/602 of Q3L245
- N100 (≠ C62) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (≠ I90) modified: Tele-8alpha-FAD histidine
- N344 (= N289) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H468) active site, Proton acceptor
- H581 (≠ N510) active site
Sites not aligning to the query:
6ze6A Fad-dependent oxidoreductase from chaetomium thermophilum in complex with fragment 4-nitrocatechol (see paper)
30% identity, 98% coverage: 4:526/531 of query aligns to 2:578/585 of 6ze6A
- binding 4-nitrocatechol: I75 (≠ P79), L92 (≠ M96), Q306 (≠ H293), V360 (vs. gap), Y431 (≠ C382), L433 (= L384), N514 (≠ G463), S516 (≠ T465), N517 (≠ I466), H519 (= H468), G561 (= G509), S562 (≠ N510)
- binding dihydroflavine-adenine dinucleotide: G8 (= G10), G10 (= G12), I11 (≠ S13), S12 (≠ A14), E32 (= E34), A33 (= A35), W56 (vs. gap), A77 (≠ G81), G82 (= G86), G83 (≠ C87), N87 (= N91), A88 (≠ G92), V90 (≠ I94), L227 (≠ H217), V228 (= V218), A265 (= A252), A518 (≠ F467), H519 (= H468), D551 (= D499), I552 (≠ A500), S562 (≠ N510), P563 (≠ T511), M564 (≠ N512)
Query Sequence
>YP_001328534.1 NCBI__GCF_000017145.1:YP_001328534.1
MDTFDYIIVGAGSAGCVLANRLSENPDRRVLLLEAGGSDNYHWIHIPVGYLYCINNPRTD
WCFTTAAEEGLNGRSLGYPRGKVLGGCSSINGMIYMRGQARDYDLWRQLGCAGWSWNDVL
PLFRKCEDHHRGADEMHGAGGEWRVEKARVRWAVLDAFQKAATEAGIPETDDFNRGTNEG
SGYFDVNQRSGIRWNTAKAFLRPAMRRRNLTILTKAHVRRLVLNDRRVSGVEFQHDGVTK
SVLARREVVLSAGAIGSPHILELSGIGRPDVLRENGIEVRHELPAVGENLQDHLQLRLAY
KVTGVPTLNEKATSLFGKAAIGLEYLVRRSGPMAMAPSQLGIFTRSGPEKETPDLQYHVQ
PVTLEKFGEPVHPFPAITASVCNLRPESRGSVHLKSPDFAAAPNIRPRYLSAEADREVAV
KAIRLTRRIVSQPAFARYKPVEFKPGPSYETDEDLKRAAGEIGTTIFHPVGTCRMGGDQA
SVVDPELRLRGLAGLRIADASIMPTITSGNTNSPTIMIAEKAAEMILAADR
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