SitesBLAST
Comparing WP_038210731.1 NCBI__GCF_000745855.1:WP_038210731.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
34% identity, 99% coverage: 6:552/555 of query aligns to 5:454/458 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 (= V233), A214 (= A272), G215 (= G273), A218 (≠ G276), T270 (≠ M355), Y391 (≠ F487), A424 (= A522), I435 (≠ T533), N436 (= N534)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
35% identity, 99% coverage: 6:555/555 of query aligns to 84:643/654 of A0A248QE08
- TA 93:94 (= TA 15:16) binding FAD
- E114 (= E36) binding FAD
- L162 (≠ T85) binding FAD
- S166 (≠ C89) binding FAD
- NATL 170:173 (≠ NGMI 93:96) binding FAD
- V298 (= V233) binding FAD
- C432 (≠ S358) binding hexadecanoate
- R451 (≠ H378) binding hexadecanoate
- Y466 (≠ H392) binding hexadecanoate
- Q486 (≠ S400) binding hexadecanoate
- G622 (≠ N534) binding FAD
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
35% identity, 99% coverage: 6:555/555 of query aligns to 24:576/578 of 5nccA
- active site: R347 (= R340), L420 (≠ V401), I421 (≠ C402), S507 (≠ I486), A509 (≠ H488), G552 (= G531), Q553 (≠ N532)
- 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 (= V233), A278 (= A272), H282 (≠ G276), L286 (= L280), N508 (≠ F487), Q553 (≠ N532), T554 (= T533), G555 (≠ N534), V558 (≠ T537)
6yrvAAA structure of fap after illumination at 100k (see paper)
35% identity, 99% coverage: 6:555/555 of query aligns to 8:567/573 of 6yrvAAA
- binding carbon dioxide: R375 (≠ H378), N499 (≠ F487)
- 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 (≠ N201), V222 (= V233), C264 (= C271), A265 (= A272), G266 (= G273), H269 (≠ G276), N499 (≠ F487), A534 (= A522), Q544 (≠ N532), T545 (= T533), G546 (≠ N534)
- binding heptadecane: V377 (≠ Q380), G379 (vs. gap), M380 (≠ L382), G386 (= G388), T389 (≠ L391), Y390 (≠ H392), F393 (= F394), T408 (= T398), Q410 (≠ S400)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
32% identity, 98% coverage: 6:551/555 of query aligns to 2:564/565 of 5oc1A
- active site: V339 (≠ I341), N413 (= N403), A414 (vs. gap), I499 (= I486), H501 (= H488), A544 (≠ G531), H545 (≠ N532)
- binding 4-methoxybenzoic acid: Y91 (≠ G94), I356 (vs. gap), I390 (≠ L382), F396 (≠ G388), T412 (≠ C402), I499 (= I486), H501 (= H488), H545 (≠ N532)
- 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 (= V233), S270 (≠ C271), A271 (= A272), G272 (= G273), F500 (= F487), H545 (≠ N532), T546 (= T533), Q547 (≠ N534), I550 (≠ T537)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
32% identity, 98% coverage: 6:551/555 of query aligns to 2:564/565 of 3fimB
- active site: V339 (≠ I341), N413 (= N403), A414 (vs. gap), I499 (= I486), H501 (= H488), A544 (≠ G531), H545 (≠ N532)
- 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 (= V233), S270 (≠ C271), A271 (= A272), F500 (= F487), H501 (= H488), H545 (≠ N532), T546 (= T533), Q547 (≠ N534), I550 (≠ T537)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
34% identity, 100% coverage: 1:554/555 of query aligns to 9:532/532 of 4mjwA
- active site: I333 (≠ L360), P377 (= P406), N378 (≠ T407), V464 (≠ I486), H466 (= H488), V509 (≠ G531), N510 (= N532)
- 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 (≠ Q232), A232 (≠ V233), T269 (≠ A272), G270 (= G273), D273 (≠ G276), Y465 (≠ F487), H466 (= H488), A500 (= A522), N510 (= N532), P511 (≠ T533), N512 (= N534), V515 (≠ T537)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
34% identity, 99% coverage: 1:549/555 of query aligns to 9:527/527 of 2jbvA
- active site: I333 (≠ L360), P377 (= P406), N378 (≠ T407), V464 (≠ I486), H466 (= H488), V509 (≠ G531), N510 (= N532)
- 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 (≠ Q232), A232 (≠ V233), T269 (≠ A272), G270 (= G273), D273 (≠ G276), V464 (≠ I486), Y465 (≠ F487), H466 (= H488), D499 (= D521), A500 (= A522), N510 (= N532), P511 (≠ T533), N512 (= N534), V515 (≠ T537)
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
34% identity, 99% coverage: 1:550/555 of query aligns to 9:528/530 of 3ljpA
- active site: I333 (≠ L360), P377 (= P406), N378 (≠ T407), A464 (≠ I486), H466 (= H488), V509 (≠ G531), N510 (= N532)
- 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 (≠ V233), T269 (≠ A272), D273 (≠ G276), Y465 (≠ F487), H466 (= H488), D499 (= D521), A500 (= A522), N510 (= N532), P511 (≠ T533), N512 (= N534), V515 (≠ T537)
4ha6A Crystal structure of pyridoxine 4-oxidase - pyridoxamine complex (see paper)
35% identity, 97% coverage: 7:545/555 of query aligns to 3:501/508 of 4ha6A
- active site: F360 (≠ V401), G361 (≠ C402), H444 (≠ I486), H446 (= H488), G487 (= G531), P488 (≠ N532)
- 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 (= V233), A251 (= A272), G252 (= G273), E255 (≠ G276), H445 (≠ F487), A478 (= A522), P488 (≠ N532), I489 (≠ T533), H490 (≠ N534)
- binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: A89 (≠ G94), S314 (= S350), H444 (≠ I486), H446 (= H488)
3t37A Crystal structure of pyridoxine 4-oxidase from mesorbium loti
35% identity, 97% coverage: 7:545/555 of query aligns to 3:501/509 of 3t37A
- active site: F360 (≠ V401), G361 (≠ C402), H444 (≠ I486), H446 (= H488), G487 (= G531), P488 (≠ N532)
- 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 (≠ Q232), V218 (= V233), A251 (= A272), E255 (≠ G276), H445 (≠ F487), A478 (= A522), P488 (≠ N532), I489 (≠ T533), H490 (≠ N534)
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)
35% identity, 98% coverage: 1:545/555 of query aligns to 1:524/531 of E4QP00
- V101 (≠ I92) mutation to H: Abolishes activity.
- M103 (≠ G94) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V401) 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 (≠ N403) mutation to A: 7.5-fold reduction in catalytic efficiency on vanillyl alcohol.
- V465 (vs. gap) mutation to A: 18-fold reduction in catalytic efficiency on vanillyl alcohol.
- W466 (≠ F487) 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 (= H488) mutation to A: Abolishes activity.
- N511 (= N532) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
8bxlB Patulin synthase from penicillium expansum (see paper)
31% identity, 99% coverage: 3:551/555 of query aligns to 11:589/590 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 (≠ Q232), A254 (≠ V233), A288 (= A272), Q292 (≠ G276), F525 (= F487), D559 (= D521), A560 (= A522), H570 (≠ N532), P571 (≠ T533), Q572 (≠ N534), L575 (≠ T537)
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
35% identity, 97% coverage: 6:545/555 of query aligns to 2:520/525 of 4udqA
- active site: L331 (= L360), F364 (≠ C402), W365 (≠ N403), V461 (vs. gap), H463 (= H488), A506 (≠ G531), N507 (= N532)
- 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 (= V233), T261 (≠ C271), A262 (= A272), W462 (≠ F487), H463 (= H488), A497 (= A522), N507 (= N532), T508 (= T533), N509 (= N534), T512 (= T537)
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
29% identity, 99% coverage: 2:548/555 of query aligns to 12:572/577 of 4h7uA
- active site: A343 (≠ R340), V426 (≠ C402), Y510 (≠ I486), H512 (= H488), A555 (≠ G531), H556 (≠ N532)
- 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 (≠ Q232), V243 (= V233), G282 (≠ A272), G283 (= G273), A286 (≠ G276), H512 (= H488), A546 (= A522), H556 (≠ N532), T557 (= T533), Q558 (≠ N534), V561 (≠ T537)
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)
29% identity, 99% coverage: 2:548/555 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 (= N309) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H488) active site, Proton acceptor
- H581 (≠ N532) active site
Sites not aligning to the query:
7vzsA Fad-dpendent glucose dehydrogenase complexed with an inhibitor at ph7.56
30% identity, 99% coverage: 4:552/555 of query aligns to 2:566/566 of 7vzsA
- binding D-glucal: Y6 (= Y8), L22 (= L24), N25 (≠ D27), Y51 (= Y52), I349 (≠ L343), Q356 (≠ M355), E411 (≠ S400), E444 (≠ D433), W445 (≠ A434), K448 (= K437), R499 (≠ T484), N501 (≠ I486), H546 (≠ N532), K563 (≠ R549), A566 (= A552)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (= Y52), F55 (≠ I56), W61 (= W63), R79 (= R79), G81 (= G83), G86 (= G88), T87 (≠ C89), N91 (= N93), G92 (= G94), M93 (= M95), A94 (≠ I96), T232 (≠ Q232), A233 (≠ V233), A273 (= A272), G274 (= G273), R277 (≠ G276), F502 (= F487), A536 (= A522), H546 (≠ N532), L547 (≠ T533), V548 (≠ N534), L551 (≠ T537)
6ze7B Chaetomium thermophilum fad-dependent oxidoreductase in complex with 4-nitrophenol (see paper)
29% identity, 99% coverage: 4:551/555 of query aligns to 1:582/586 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 (≠ Q232), V229 (= V233), A266 (= A272), A519 (≠ F487), H520 (= H488), D552 (= D521), I553 (≠ A522), S563 (≠ N532), P564 (≠ T533), M565 (≠ N534)
- binding p-nitrophenol: L93 (≠ M98), V361 (≠ A362), Y432 (≠ C402), L434 (= L404), G562 (= G531), S563 (≠ N532)
4ynuA Crystal structure of aspergillus flavus fadgdh in complex with d- glucono-1,5-lactone (see paper)
30% identity, 99% coverage: 4:552/555 of query aligns to 2:566/569 of 4ynuA
- active site: V341 (≠ L335), F412 (≠ V401), W413 (≠ C402), N501 (≠ I486), H503 (= H488), G545 (= G531), H546 (≠ N532)
- binding flavin-adenine dinucleotide: G12 (= G14), T13 (= T15), S14 (≠ A16), E34 (= E36), A35 (= A37), Y51 (= Y52), F55 (≠ I56), W61 (= W63), R79 (= R79), G81 (= G83), G86 (= G88), T87 (≠ C89), N91 (= N93), G92 (= G94), T232 (≠ Q232), A233 (≠ V233), A273 (= A272), G274 (= G273), R277 (≠ G276), F502 (= F487), A536 (= A522), H546 (≠ N532), L547 (≠ T533), V548 (≠ N534), L551 (≠ T537)
- binding D-glucono-1,5-lactone: Y51 (= Y52), E411 (≠ S400), A496 (≠ D481), N497 (≠ I482), R499 (≠ T484), R499 (≠ T484), N501 (≠ I486), H503 (= H488), H546 (≠ N532)
4yntA Crystal structure of aspergillus flavus fad glucose dehydrogenase (see paper)
30% identity, 99% coverage: 4:552/555 of query aligns to 3:567/570 of 4yntA
- active site: V342 (≠ L335), F413 (≠ V401), W414 (≠ C402), N502 (≠ I486), H504 (= H488), G546 (= G531), H547 (≠ N532)
- binding dihydroflavine-adenine dinucleotide: G13 (= G14), T14 (= T15), S15 (≠ A16), E35 (= E36), A36 (= A37), F56 (≠ I56), W62 (= W63), R80 (= R79), G82 (= G83), G87 (= G88), T88 (≠ C89), N92 (= N93), G93 (= G94), M94 (= M95), A95 (≠ I96), A234 (≠ V233), A274 (= A272), R278 (≠ G276), F503 (= F487), A537 (= A522), H547 (≠ N532), L548 (≠ T533), V549 (≠ N534), L552 (≠ T537)
Query Sequence
>WP_038210731.1 NCBI__GCF_000745855.1:WP_038210731.1
MSDTTFDYIVIGAGTAGALMANRLSADKRRRVLLIEAGRKDDYHWIHIPVGYLYCIGNPR
TDWLYQTEPDAGLNGRVLRYPRGKTLGGCSSINGMIYMRGQSRDYDGWAQLTGDDAWRWE
NVLPAFRQHEDHYLGDAAEAARRDADFDRFHGHGGEWRVERQRLRWDILDAFAEAAVQAG
IPHTADFNRGSNEGVGYFQVNQKAGWRWNTAKAFLRPICYGRPNFELWTGAQVTRLVVEA
QPDGPPRCTGVQVWNGSELVTASATREVLLCAGSIGSPQLLQLSGIGPGDLLQQHGIPVV
ADLPGVGANLQDHLQIRAVFKIDGAPTLNVLASSLFGKARIGLEYVLRRSGPMSMAPSQL
GAFTRSAPGHAWPNIQYHVQPLSLDAFGDPLHSFPAFTASVCNLNPTSRGSVRIKSPRFE
DAPAIAPCYLSTDADRKVAADSLRVTRRIAAQPALAKYRPQEWKPGPQYESDEDLARLAG
DIATTIFHPVGTAKMGAADDPMAVLDARLRVRGVQGLRVVDASAMPTITSGNTNSPTLMM
AEKAAAWVRADAAGG
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