SitesBLAST
Comparing WP_020563804.1 NCBI__GCF_000372865.1:WP_020563804.1 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)
33% identity, 60% coverage: 247:619/624 of query aligns to 141:450/458 of 8b7sA
Sites not aligning to the query:
8bxlB Patulin synthase from penicillium expansum (see paper)
28% identity, 98% coverage: 6:616/624 of query aligns to 11:583/590 of 8bxlB
- binding flavin-adenine dinucleotide: G20 (= G15), G22 (= G17), T23 (≠ A18), A24 (≠ G19), E44 (= E38), A45 (= A39), W80 (= W80), G100 (≠ A111), G105 (= G116), S106 (≠ C117), R109 (≠ H120), N110 (= N121), Y111 (≠ A122), A113 (≠ I124), L253 (= L285), A254 (≠ V286), A288 (≠ G335), Q292 (≠ N339), F525 (≠ H558), D559 (= D592), A560 (= A593), H570 (≠ F603), P571 (≠ I604), Q572 (≠ V605), L575 (≠ I608)
5nccA Structure of fatty acid photodecarboxylase in complex with fad and palmitic acid (see paper)
29% identity, 98% coverage: 8:619/624 of query aligns to 23:569/578 of 5nccA
- active site: R347 (≠ P399), L420 (vs. gap), I421 (vs. gap), S507 (≠ H558), A509 (= A560), G552 (≠ F602), Q553 (≠ F603)
- binding flavin-adenine dinucleotide: G30 (= G15), G32 (= G17), T33 (≠ A18), A34 (≠ G19), L53 (= L37), E54 (= E38), A55 (= A39), F74 (vs. gap), W80 (= W80), A98 (≠ P109), G100 (≠ A111), G105 (= G116), S106 (≠ C117), N110 (= N121), A111 (= A122), T112 (= T125), L113 (≠ V126), V238 (= V286), A278 (≠ G335), H282 (≠ N339), L286 (= L343), N508 (≠ H559), Q553 (≠ F603), T554 (≠ I604), G555 (≠ V605), V558 (≠ I608)
A0A248QE08 Fatty acid photodecarboxylase, chloroplastic; CvFAP; EC 4.1.1.106 from Chlorella variabilis (Green alga) (see paper)
28% identity, 98% coverage: 8:619/624 of query aligns to 83:636/654 of A0A248QE08
- TA 93:94 (≠ AG 18:19) binding FAD
- E114 (= E38) binding FAD
- L162 (≠ C113) binding FAD
- S166 (≠ C117) binding FAD
- NA--TL 170:173 (≠ NAMITV 121:126) binding FAD
- V298 (= V286) binding FAD
- C432 (≠ A419) binding hexadecanoate
- R451 (vs. gap) binding hexadecanoate
- Y466 (≠ F449) binding hexadecanoate
- Q486 (≠ K469) binding hexadecanoate
- G622 (≠ V605) binding FAD
3ljpA Crystal structure of choline oxidase v464a mutant (see paper)
30% identity, 100% coverage: 1:622/624 of query aligns to 6:529/530 of 3ljpA
- active site: I333 (≠ K411), P377 (≠ W465), N378 (≠ A466), A464 (≠ G557), H466 (= H559), V509 (≠ F602), N510 (≠ F603)
- binding dihydroflavine-adenine dinucleotide: G22 (= G17), S23 (≠ A18), E44 (= E38), A45 (= A39), W71 (≠ Q95), R89 (= R110), A90 (= A111), G95 (= G116), C96 (= C117), H99 (= H120), N100 (= N121), S101 (≠ A122), I103 (= I124), A232 (≠ V286), T269 (≠ G335), D273 (≠ N339), Y465 (≠ H558), H466 (= H559), D499 (= D592), A500 (= A593), N510 (≠ F603), P511 (≠ I604), N512 (≠ V605), V515 (≠ I608)
6yrvAAA structure of fap after illumination at 100k (see paper)
28% identity, 98% coverage: 8:619/624 of query aligns to 7:560/573 of 6yrvAAA
- binding carbon dioxide: R375 (vs. gap), N499 (≠ H559)
- binding flavin-adenine dinucleotide: G14 (= G15), G16 (= G17), T17 (≠ A18), A18 (≠ G19), L37 (= L37), E38 (= E38), A39 (= A39), F58 (vs. gap), W64 (= W80), A82 (≠ P109), G89 (= G116), S90 (≠ C117), N94 (= N121), A95 (= A122), T96 (= T125), L97 (≠ V126), M191 (≠ A254), V222 (= V286), C264 (≠ S334), A265 (≠ G335), G266 (= G336), H269 (≠ N339), N499 (≠ H559), A534 (= A593), Q544 (≠ F603), T545 (≠ I604), G546 (≠ V605)
- binding heptadecane: V377 (vs. gap), G379 (vs. gap), M380 (≠ F439), G386 (≠ F445), T389 (≠ Y448), Y390 (≠ F449), F393 (≠ Y452), T408 (≠ V467), Q410 (≠ K469)
4mjwA Crystal structure of choline oxidase in complex with the reaction product glycine betaine (see paper)
30% identity, 100% coverage: 1:624/624 of query aligns to 6:531/532 of 4mjwA
- active site: I333 (≠ K411), P377 (≠ W465), N378 (≠ A466), V464 (≠ G557), H466 (= H559), V509 (≠ F602), N510 (≠ F603)
- binding flavin-adenine dinucleotide: G20 (= G15), G22 (= G17), S23 (≠ A18), E44 (= E38), A45 (= A39), W71 (≠ Q95), R89 (= R110), A90 (= A111), G95 (= G116), C96 (= C117), H99 (= H120), N100 (= N121), S101 (≠ A122), I103 (= I124), R231 (≠ L285), A232 (≠ V286), T269 (≠ G335), G270 (= G336), D273 (≠ N339), Y465 (≠ H558), H466 (= H559), A500 (= A593), N510 (≠ F603), P511 (≠ I604), N512 (≠ V605), V515 (≠ I608)
2jbvA Crystal structure of choline oxidase reveals insights into the catalytic mechanism (see paper)
30% identity, 99% coverage: 1:619/624 of query aligns to 6:526/527 of 2jbvA
- active site: I333 (≠ K411), P377 (≠ W465), N378 (≠ A466), V464 (≠ G557), H466 (= H559), V509 (≠ F602), N510 (≠ F603)
- 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 (= G17), S23 (≠ A18), E44 (= E38), A45 (= A39), W71 (≠ Q95), A90 (= A111), G95 (= G116), C96 (= C117), H99 (= H120), N100 (= N121), S101 (≠ A122), I103 (= I124), R231 (≠ L285), A232 (≠ V286), T269 (≠ G335), G270 (= G336), D273 (≠ N339), V464 (≠ G557), Y465 (≠ H558), H466 (= H559), D499 (= D592), A500 (= A593), N510 (≠ F603), P511 (≠ I604), N512 (≠ V605), V515 (≠ I608)
5oc1A Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with p-anisic acid (see paper)
24% identity, 98% coverage: 8:619/624 of query aligns to 1:561/565 of 5oc1A
- active site: V339 (≠ P402), N413 (≠ W465), A414 (= A466), I499 (vs. gap), H501 (= H559), A544 (≠ F602), H545 (≠ F603)
- binding 4-methoxybenzoic acid: Y91 (≠ A122), I356 (= I424), I390 (≠ L442), F396 (≠ Y448), T412 (= T464), I499 (vs. gap), H501 (= H559), H545 (≠ F603)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), N11 (≠ A18), A12 (≠ G19), E32 (= E38), A33 (= A39), W60 (= W80), P78 (= P109), G80 (≠ A111), G85 (= G116), S86 (≠ C117), H90 (≠ N121), Y91 (≠ A122), V93 (≠ I124), V230 (= V286), S270 (= S334), A271 (≠ G335), G272 (= G336), F500 (≠ H558), H545 (≠ F603), T546 (≠ I604), Q547 (≠ V605), I550 (= I608)
3fimB Crystal structure of aryl-alcohol-oxidase from pleurotus eryingii (see paper)
23% identity, 98% coverage: 8:619/624 of query aligns to 1:561/565 of 3fimB
- active site: V339 (≠ P402), N413 (≠ W465), A414 (= A466), I499 (vs. gap), H501 (= H559), A544 (≠ F602), H545 (≠ F603)
- binding flavin-adenine dinucleotide: G8 (= G15), N11 (≠ A18), A12 (≠ G19), E32 (= E38), A33 (= A39), W60 (= W80), P78 (= P109), G80 (≠ A111), G85 (= G116), S86 (≠ C117), H90 (≠ N121), Y91 (≠ A122), V93 (≠ I124), V230 (= V286), S270 (= S334), A271 (≠ G335), F500 (≠ H558), H501 (= H559), H545 (≠ F603), T546 (≠ I604), Q547 (≠ V605), I550 (= I608)
3q9tA Crystal structure analysis of formate oxidase (see paper)
26% identity, 99% coverage: 4:619/624 of query aligns to 2:569/577 of 3q9tA
- active site: A335 (≠ P399), D422 (≠ L468), A508 (≠ G557), H510 (= H559), C552 (≠ F602), R553 (≠ F603)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl(2R,3S,4S)-5-(8-formyl-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-2,3,4-trihydroxypentyl dihydrogendiphosphate: G15 (= G17), T16 (≠ A18), E37 (= E38), A38 (= A39), W65 (≠ R85), T85 (≠ P109), R86 (= R110), G87 (≠ A111), G92 (= G116), S93 (≠ C117), N97 (= N121), Y98 (≠ A122), F99 (≠ M123), T100 (≠ I124), S229 (≠ V286), S265 (= S334), Q266 (≠ G335), E270 (≠ N339), F509 (≠ H558), D542 (= D592), A543 (= A593), R553 (≠ F603), I554 (= I604), Q555 (≠ V605), V558 (≠ I608)
5zu2A Effect of mutation (r554a) on fad modification in aspergillus oryzae rib40formate oxidase (see paper)
26% identity, 99% coverage: 4:619/624 of query aligns to 2:569/577 of 5zu2A
- binding flavin-adenine dinucleotide: G15 (= G17), T16 (≠ A18), E37 (= E38), A38 (= A39), W65 (≠ R85), T85 (≠ P109), R86 (= R110), G87 (≠ A111), G92 (= G116), S93 (≠ C117), N97 (= N121), Y98 (≠ A122), T100 (≠ I124), S229 (≠ V286), S265 (= S334), Q266 (≠ G335), E270 (≠ N339), F509 (≠ H558), D542 (= D592), A543 (= A593), A553 (≠ F603), I554 (= I604), Q555 (≠ V605), V558 (≠ I608)
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)
26% identity, 98% coverage: 8:619/624 of query aligns to 40:597/602 of Q3L245
- N100 (≠ D81) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H128 (= H120) modified: Tele-8alpha-FAD histidine
- N344 (= N372) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- H537 (= H559) active site, Proton acceptor
- H581 (≠ F603) active site
Sites not aligning to the query:
4h7uA Crystal structure of pyranose dehydrogenase from agaricus meleagris, wildtype (see paper)
26% identity, 98% coverage: 8:619/624 of query aligns to 15:572/577 of 4h7uA
- active site: A343 (≠ P402), V426 (≠ L468), Y510 (≠ H558), H512 (= H559), A555 (≠ F602), H556 (≠ F603)
- 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 (= G15), G24 (= G17), T25 (≠ A18), A26 (≠ G19), E46 (= E38), A47 (= A39), W74 (= W80), G99 (= G116), C100 (= C117), H103 (= H120), N104 (= N121), G105 (≠ A122), V107 (≠ I124), L242 (= L285), V243 (= V286), G282 (= G335), G283 (= G336), A286 (≠ N339), H512 (= H559), A546 (= A593), H556 (≠ F603), T557 (≠ I604), Q558 (≠ V605), V561 (≠ I608)
6xuuA Crystallographic structure of oligosaccharide dehydrogenase from pycnoporus cinnabarinus, glucose-bound form (see paper)
24% identity, 99% coverage: 5:619/624 of query aligns to 11:585/589 of 6xuuA
- binding beta-D-glucopyranose: E35 (= E29), N67 (= N75), H83 (≠ P109), N104 (= N130), D108 (= D134), S139 (≠ H162), A140 (≠ R163), N142 (≠ K165), T166 (≠ L197), D169 (= D200), T188 (≠ Q230), W213 (vs. gap), A225 (≠ R266), Y226 (≠ L267), Q329 (≠ E378), N330 (≠ V379), A331 (≠ G380), Q357 (≠ T415), F414 (= F437), K474 (≠ S520), N517 (vs. gap), G520 (≠ H558), A522 (= A560), V524 (≠ C562), H526 (≠ C564), H569 (≠ F603)
- binding flavin-adenine dinucleotide: G21 (= G15), G23 (= G17), L24 (≠ A18), T25 (≠ G19), E45 (= E38), A46 (= A39), F66 (≠ E74), W72 (= W80), H83 (≠ P109), G85 (≠ A111), G90 (= G116), S91 (≠ C117), N95 (= N121), G96 (≠ A122), A97 (≠ M123), A98 (≠ I124), M244 (≠ L285), A245 (≠ V286), A286 (≠ G335), Q290 (≠ N339), A525 (≠ T563), A559 (= A593), H569 (≠ F603), L570 (≠ I604), S571 (≠ V605), L574 (≠ I608)
- binding alpha-D-glucopyranose: G96 (≠ A122), F414 (= F437), W428 (= W465)
6xutA Crystallographic structure of oligosaccharide dehydrogenase from pycnoporus cinnabarinus, ligand-free form (see paper)
24% identity, 99% coverage: 5:619/624 of query aligns to 11:585/589 of 6xutA
- binding flavin-adenine dinucleotide: G21 (= G15), G23 (= G17), L24 (≠ A18), T25 (≠ G19), E45 (= E38), A46 (= A39), F66 (≠ E74), W72 (= W80), H83 (≠ P109), G85 (≠ A111), G90 (= G116), S91 (≠ C117), N95 (= N121), G96 (≠ A122), A97 (≠ M123), A98 (≠ I124), M244 (≠ L285), A245 (≠ V286), A286 (≠ G335), G287 (= G336), Q290 (≠ N339), A525 (≠ T563), H526 (≠ C564), A559 (= A593), H569 (≠ F603), L570 (≠ I604), S571 (≠ V605), L574 (≠ I608)
6o9nA Structural insights on a new fungal aryl-alcohol oxidase (see paper)
25% identity, 98% coverage: 8:621/624 of query aligns to 4:609/613 of 6o9nA
- binding calcium ion: T46 (≠ E56), F47 (≠ K57), D48 (≠ R58), Y369 (= Y414), L371 (≠ T416)
- binding flavin-adenine dinucleotide: G11 (= G15), G13 (= G17), T14 (≠ A18), S15 (≠ G19), I35 (≠ L37), E36 (= E38), Y37 (≠ Q47), W64 (= W80), L82 (≠ R110), G84 (= G112), G89 (= G116), S90 (≠ C117), N94 (= N121), G95 (≠ A122), M96 (= M123), F97 (≠ I124), V243 (= V286), S281 (= S334), A282 (≠ G335), H286 (≠ N339), M547 (≠ H558), H548 (= H559), D580 (= D592), M581 (≠ A593), H591 (≠ F603), L592 (≠ I604), S593 (≠ V605)
1cf3A Glucose oxidase from apergillus niger (see paper)
26% identity, 98% coverage: 10:620/624 of query aligns to 19:574/581 of 1cf3A
- active site: T355 (≠ K396), W424 (≠ L468), N512 (≠ G557), H514 (= H559), S556 (≠ F602), H557 (≠ F603)
- binding flavin-adenine dinucleotide: G24 (= G15), L27 (≠ A18), T28 (≠ G19), E48 (= E38), S49 (≠ A39), H76 (= H86), R93 (≠ P109), G95 (≠ A111), N96 (≠ G112), G100 (= G116), S101 (≠ C117), N105 (= N121), G106 (≠ A122), T108 (≠ I124), Y247 (≠ L285), V248 (= V286), A287 (≠ G335), Y513 (≠ H558), H514 (= H559), H557 (≠ F603), V558 (≠ I604), M559 (≠ V605), F562 (≠ I608)
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)
25% identity, 98% coverage: 9:621/624 of query aligns to 6:529/531 of E4QP00
- V101 (≠ H120) mutation to H: Abolishes activity.
- M103 (≠ A122) mutation to A: 16-fold reduction in catalytic efficiency on vanillyl alcohol.
- V367 (= V467) 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 (≠ K469) 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 (≠ H558) 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 (= H559) mutation to A: Abolishes activity.
- N511 (≠ F603) mutation to A: 53-fold reduction in catalytic efficiency on vanillyl alcohol.
4udqA Crystal structure of 5-hydroxymethylfurfural oxidase (hmfo) in the reduced state
25% identity, 98% coverage: 9:621/624 of query aligns to 2:525/525 of 4udqA
- active site: L331 (= L408), F364 (≠ L468), W365 (≠ K469), V461 (vs. gap), H463 (= H559), A506 (≠ F602), N507 (≠ F603)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), T11 (≠ A18), A12 (≠ G19), E32 (= E38), A33 (= A39), W64 (≠ H69), G88 (≠ A111), G93 (= G116), G94 (≠ C117), N98 (= N121), M99 (≠ A122), V101 (≠ I124), V229 (= V286), T261 (≠ S334), A262 (≠ G335), W462 (≠ H558), H463 (= H559), A497 (= A593), N507 (≠ F603), T508 (≠ I604), N509 (≠ V605), T512 (≠ I608)
Query Sequence
>WP_020563804.1 NCBI__GCF_000372865.1:WP_020563804.1
MTNSNNAEYEYIVVGSGAGGGTVAARLAERGKKVLVLEAGGDPKQLQGDNLAFPGEKRLP
DDYDVPVFHPFSTENEAMRWDFFVRHYETESIQAQDPKYTPAEKGVLYPRAGCLGGCTAH
NAMITVYPHNADWDEVADITGDASWKADNMRKYFELMENCEHRPKLRKLATWLGINPSRH
GFKGWFQTEAALPLEALAKDKKLVLAILDSAVKAAGKLPSFFDRLKWQIQGLADPNDWRL
VKDNAIGLHYPPLATTKGKRHSTRERLLEVQQKHPGNLTIELDALVTRVILDDNNRAVGV
EYLKGAKLYKAHANPSNKPGELREAYAAKEVILSGGAYNTPQLLMLSGIGPKEELQKHGI
AVKHHLPGIGANLQDRYEVGVTNRMNQDWEVLKGAKYSPGDPEYNDWLNGKGVYTTNGAV
LAVIKRSVEERPLPDLFCFALLGNFRGYFPGYSKLIKDNLNYLTWAVLKAHTVNRAGEVR
LVSADPRDRPYINFRYFEEGTDTTGQDLDSVVEGIKFVRSIAKPLFDQGILAEEVAPGKS
VQTDEQLRDFVRYNAWGHHASCTCPIGADNDPMAVLDSQFRVRGIQGLRVVDASVFPRIP
GFFIVSSIYMIGEKAADVILNASA
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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