SitesBLAST
Comparing WP_104912863.1 NCBI__GCF_002950575.1:WP_104912863.1 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)
5ux5A Structure of proline utilization a (puta) from corynebacterium freiburgense (see paper)
45% identity, 88% coverage: 127:1169/1180 of query aligns to 28:961/963 of 5ux5A
- active site: C617 (= C772), K792 (= K951)
- binding flavin-adenine dinucleotide: D138 (= D237), M139 (= M238), R202 (= R301), V204 (= V303), K205 (= K304), G206 (= G305), A207 (= A306), L209 (= L308), T228 (≠ S327), K229 (= K328), V232 (≠ S331), S257 (≠ G357), N259 (= N359), E282 (= E382), M283 (= M383), N328 (= N428)
- binding nicotinamide-adenine-dinucleotide: S484 (≠ P639), W486 (= W641), K510 (= K665), A512 (= A667), E543 (= E698), G547 (= G702), G563 (= G718), A564 (= A719), T567 (= T722), F571 (= F726), F713 (= F872)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
31% identity, 69% coverage: 147:958/1180 of query aligns to 106:937/959 of 5ur2B
- active site: N618 (= N642), K641 (= K665), E722 (= E738), C756 (= C772), E851 (= E870), T931 (≠ A952)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K194), D215 (= D237), M216 (= M238), Q249 (= Q270), V278 (= V303), K279 (= K304), G280 (= G305), A281 (= A306), W283 (≠ L308), Y300 (≠ L325), T301 (≠ P326), N302 (≠ S327), K303 (= K328), S306 (= S331), A329 (= A356), S330 (≠ G357), H331 (= H358), N332 (= N359), Q356 (≠ E382), M357 (= M383), L358 (= L384), Y379 (= Y405), E398 (= E427), E403 (= E432), W405 (≠ F434)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
29% identity, 72% coverage: 115:959/1180 of query aligns to 82:950/977 of 4nmaA
- active site: N629 (= N642), K652 (= K665), E733 (= E738), C767 (= C772), E863 (= E870), A943 (= A952)
- binding flavin-adenine dinucleotide: D226 (= D237), M227 (= M238), Q258 (= Q270), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), Y291 (≠ N307), W292 (≠ L308), W309 (≠ L325), T310 (≠ P326), I311 (≠ S327), K312 (= K328), S315 (= S331), A338 (= A356), S339 (≠ G357), H340 (= H358), N341 (= N359), Q365 (≠ E382), L367 (= L384), E407 (= E427), S413 (≠ N433), F414 (= F434)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K194), Y388 (= Y405), Y400 (= Y420), R403 (= R423), R404 (= R424)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
29% identity, 72% coverage: 113:959/1180 of query aligns to 80:952/979 of 4nmdA
- active site: N631 (= N642), K654 (= K665), E735 (= E738), C769 (= C772), E865 (= E870), A945 (= A952)
- binding dihydroflavine-adenine dinucleotide: D226 (= D237), M227 (= M238), V256 (= V268), Q258 (= Q270), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), W292 (≠ L308), W309 (≠ L325), T310 (≠ P326), I311 (≠ S327), K312 (= K328), S315 (= S331), A338 (= A356), S339 (≠ G357), H340 (= H358), N341 (= N359), Q365 (≠ E382), V366 (≠ M383), L367 (= L384), Y388 (= Y405), F414 (= F434)
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
28% identity, 72% coverage: 113:959/1180 of query aligns to 79:952/979 of 4nmfB
- active site: N631 (= N642), K654 (= K665), E735 (= E738), C769 (= C772), E865 (= E870), A945 (= A952)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K194), Y290 (≠ N307), Y387 (= Y405), Y399 (= Y420), R402 (= R423), R403 (= R424)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K194), L366 (= L384), Y399 (= Y420), R402 (= R423)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K194), D225 (= D237), M226 (= M238), V255 (= V268), Q257 (= Q270), R284 (= R301), V286 (= V303), K287 (= K304), G288 (= G305), A289 (= A306), W291 (≠ L308), W308 (≠ L325), T309 (≠ P326), I310 (≠ S327), K311 (= K328), S314 (= S331), A337 (= A356), S338 (≠ G357), H339 (= H358), N340 (= N359), Q364 (≠ E382), L366 (= L384), Y387 (= Y405), E406 (= E427), E411 (= E432), S412 (≠ N433), F413 (= F434)
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
28% identity, 72% coverage: 113:959/1180 of query aligns to 76:946/973 of 4nmfA
- active site: N625 (= N642), K648 (= K665), E729 (= E738), C763 (= C772), E859 (= E870), A939 (= A952)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K194), Y287 (≠ N307), Y384 (= Y405), Y396 (= Y420), R399 (= R423), R400 (= R424)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K194), D222 (= D237), M223 (= M238), V252 (= V268), Q254 (= Q270), R281 (= R301), V283 (= V303), K284 (= K304), G285 (= G305), A286 (= A306), W288 (≠ L308), W305 (≠ L325), T306 (≠ P326), I307 (≠ S327), K308 (= K328), S311 (= S331), A334 (= A356), S335 (≠ G357), H336 (= H358), N337 (= N359), Q361 (≠ E382), V362 (≠ M383), L363 (= L384), Y384 (= Y405), E403 (= E427), E408 (= E432), F410 (= F434)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
29% identity, 72% coverage: 115:959/1180 of query aligns to 79:945/972 of 4nmeA
- active site: N624 (= N642), K647 (= K665), E728 (= E738), C762 (= C772), E858 (= E870), A938 (= A952)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K194), D224 (= D237), M225 (= M238), V254 (= V268), Q256 (= Q270), R283 (= R301), V285 (= V303), K286 (= K304), G287 (= G305), A288 (= A306), W290 (≠ L308), W307 (≠ L325), T308 (≠ P326), I309 (≠ S327), K310 (= K328), S313 (= S331), A336 (= A356), S337 (≠ G357), H338 (= H358), N339 (= N359), Q363 (≠ E382), L365 (= L384), Y383 (= Y405), E402 (= E427), F409 (= F434)
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
28% identity, 72% coverage: 115:959/1180 of query aligns to 81:953/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D237), M227 (= M238), V256 (= V268), Q258 (= Q270), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), Y291 (≠ N307), W292 (≠ L308), W309 (≠ L325), T310 (≠ P326), I311 (≠ S327), K312 (= K328), S315 (= S331), A338 (= A356), S339 (≠ G357), H340 (= H358), N341 (= N359), L367 (= L384), Y388 (= Y405), E407 (= E427), S413 (≠ N433), F414 (= F434)
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
28% identity, 74% coverage: 91:959/1180 of query aligns to 51:915/941 of 4nmcA
- active site: N594 (= N642), K617 (= K665), E698 (= E738), C732 (= C772), E828 (= E870), A908 (= A952)
- binding flavin-adenine dinucleotide: D215 (= D237), M216 (= M238), V245 (= V268), Q247 (= Q270), R274 (= R301), V276 (= V303), K277 (= K304), G278 (= G305), A279 (= A306), W281 (≠ L308), W298 (≠ L325), T299 (≠ P326), I300 (≠ S327), K301 (= K328), S304 (= S331), A327 (= A356), S328 (≠ G357), H329 (= H358), N330 (= N359), L356 (= L384), Y377 (= Y405)
9e5wA Proline utilization a (puta) from sinorhizobium meliloti inactivated by n-propargylglycine (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 243:1018/1212 of 9e5wA
- binding nicotinamide-adenine-dinucleotide: I684 (≠ A638), S685 (≠ P639), P686 (= P640), W687 (= W641), N688 (= N642), I693 (= I647), K711 (= K665), A713 (= A667), E714 (≠ P668), G744 (= G699), G747 (= G702), A748 (≠ R703), T762 (= T717), G763 (= G718), S764 (≠ A719), V767 (≠ T722), I771 (≠ F726), E791 (= E738), T792 (= T739), C825 (= C772), E921 (= E870), F923 (= F872), F991 (= F938)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K246 (= K194), D287 (= D237), A288 (≠ M238), V319 (= V268), Q321 (= Q270), R348 (= R301), V350 (= V303), K351 (= K304), G352 (= G305), A353 (= A306), W355 (vs. gap), F373 (≠ L325), T374 (≠ P326), R375 (≠ S327), K376 (= K328), T379 (≠ S331), A402 (= A356), T403 (≠ G357), H404 (= H358), N405 (= N359), Q428 (≠ E382), C429 (≠ M383), L430 (= L384), Y454 (= Y405), S479 (≠ N433)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 245:1020/1216 of 6x99A
- active site: N690 (= N642), K713 (= K665), E793 (= E738), C827 (= C772), E923 (= E870), A1005 (= A952)
- binding d-proline: W557 (≠ G519), T558 (≠ Q520), E657 (= E606), F691 (= F643), R727 (≠ E679), R826 (≠ K771), S828 (= S773), G985 (= G930), A986 (= A931), F993 (= F938)
- binding flavin-adenine dinucleotide: D289 (= D237), A290 (≠ M238), V321 (= V268), R350 (= R301), V352 (= V303), K353 (= K304), G354 (= G305), A355 (= A306), Y356 (vs. gap), W357 (vs. gap), F375 (≠ L325), T376 (≠ P326), R377 (≠ S327), K378 (= K328), T381 (≠ S331), A404 (= A356), T405 (≠ G357), H406 (= H358), N407 (= N359), Q430 (≠ E382), C431 (≠ M383), Y456 (= Y405), E475 (= E427), S481 (≠ N433), F482 (= F434)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 238:1013/1207 of 5kf6A
- active site: N683 (= N642), K706 (= K665), E786 (= E738), C820 (= C772), E916 (= E870), A998 (= A952)
- binding flavin-adenine dinucleotide: D282 (= D237), A283 (≠ M238), V314 (= V268), Q316 (= Q270), R343 (= R301), V345 (= V303), K346 (= K304), G347 (= G305), A348 (= A306), Y349 (vs. gap), W350 (vs. gap), F368 (≠ L325), T369 (≠ P326), R370 (≠ S327), K371 (= K328), T374 (≠ S331), A397 (= A356), T398 (≠ G357), H399 (= H358), N400 (= N359), Q423 (≠ E382), C424 (≠ M383), L425 (= L384), E468 (= E427), S474 (≠ N433), F475 (= F434)
- binding nicotinamide-adenine-dinucleotide: I679 (≠ A638), S680 (≠ P639), P681 (= P640), W682 (= W641), N683 (= N642), I688 (= I647), K706 (= K665), A708 (= A667), E709 (≠ P668), G739 (= G699), G742 (= G702), A743 (≠ R703), F756 (≠ L716), T757 (= T717), G758 (= G718), S759 (≠ A719), V762 (≠ T722), I766 (≠ F726), E786 (= E738), T787 (= T739), C820 (= C772), E916 (= E870), F918 (= F872), F986 (= F938)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K194), D282 (= D237), Y449 (= Y405), R464 (= R423), R465 (= R424)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 245:1020/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D237), A290 (≠ M238), V321 (= V268), Q323 (= Q270), R350 (= R301), V352 (= V303), K353 (= K304), G354 (= G305), A355 (= A306), Y356 (vs. gap), W357 (vs. gap), F375 (≠ L325), T376 (≠ P326), R377 (≠ S327), K378 (= K328), T381 (≠ S331), A404 (= A356), T405 (≠ G357), H406 (= H358), N407 (= N359), C431 (≠ M383), L432 (= L384), E475 (= E427), S481 (≠ N433), F482 (= F434)
- binding nicotinamide-adenine-dinucleotide: I686 (≠ A638), S687 (≠ P639), P688 (= P640), W689 (= W641), N690 (= N642), I695 (= I647), K713 (= K665), A715 (= A667), E716 (≠ P668), G746 (= G699), G749 (= G702), A750 (≠ R703), T764 (= T717), G765 (= G718), S766 (≠ A719), V769 (≠ T722), E793 (= E738), T794 (= T739), C827 (= C772), E923 (= E870), F925 (= F872), F993 (= F938)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y405), Y468 (= Y420), R471 (= R423), R472 (= R424)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 246:1021/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D237), A291 (≠ M238), V322 (= V268), Q324 (= Q270), R351 (= R301), V353 (= V303), K354 (= K304), G355 (= G305), A356 (= A306), Y357 (vs. gap), W358 (vs. gap), F376 (≠ L325), T377 (≠ P326), R378 (≠ S327), K379 (= K328), T382 (≠ S331), A405 (= A356), T406 (≠ G357), H407 (= H358), N408 (= N359), C432 (≠ M383), L433 (= L384), E476 (= E427), S482 (≠ N433), F483 (= F434)
- binding nicotinamide-adenine-dinucleotide: I687 (≠ A638), S688 (≠ P639), P689 (= P640), W690 (= W641), N691 (= N642), I696 (= I647), K714 (= K665), E717 (≠ P668), G747 (= G699), G750 (= G702), T765 (= T717), G766 (= G718), S767 (≠ A719), V770 (≠ T722), I774 (≠ F726), E794 (= E738), T795 (= T739), C828 (= C772), E924 (= E870), F926 (= F872), F994 (= F938)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K194), Y457 (= Y405), Y469 (= Y420), R472 (= R423), R473 (= R424)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K194), D290 (= D237), Y457 (= Y405), Y469 (= Y420), R472 (= R423), R473 (= R424)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 246:1021/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (≠ A638), S688 (≠ P639), P689 (= P640), W690 (= W641), N691 (= N642), I696 (= I647), K714 (= K665), A716 (= A667), E717 (≠ P668), G747 (= G699), G750 (= G702), A751 (≠ R703), T765 (= T717), G766 (= G718), S767 (≠ A719), V770 (≠ T722), E794 (= E738), T795 (= T739), C828 (= C772), E924 (= E870), F926 (= F872), F994 (= F938)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[5-(1,3-dithiolan-2-yl)-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: D290 (= D237), A291 (≠ M238), V322 (= V268), Q324 (= Q270), V353 (= V303), K354 (= K304), G355 (= G305), A356 (= A306), W358 (vs. gap), F376 (≠ L325), T377 (≠ P326), R378 (≠ S327), K379 (= K328), T382 (≠ S331), A405 (= A356), T406 (≠ G357), H407 (= H358), N408 (= N359), Q431 (≠ E382), C432 (≠ M383), L433 (= L384), Y457 (= Y405), E476 (= E427)
Sites not aligning to the query:
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[5-(1,3-dithiolan-2-yl)-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: 1217
9dl6A Bifunctional protein PutA (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 247:1022/1218 of 9dl6A
- binding (3S)-piperidine-3-carboxylic acid: E659 (= E606), F693 (= F643), R828 (≠ K771), C829 (= C772), S830 (= S773), G987 (= G930), A988 (= A931)
- binding flavin-adenine dinucleotide: D291 (= D237), A292 (≠ M238), V323 (= V268), R352 (= R301), V354 (= V303), K355 (= K304), G356 (= G305), A357 (= A306), W359 (vs. gap), F377 (≠ L325), T378 (≠ P326), R379 (≠ S327), K380 (= K328), T383 (≠ S331), A406 (= A356), T407 (≠ G357), H408 (= H358), N409 (= N359), Q432 (≠ E382), C433 (≠ M383), Y458 (= Y405), E477 (= E427), S483 (≠ N433), F484 (= F434)
- binding (3R)-piperidine-3-carboxylic acid: E659 (= E606), F693 (= F643), I697 (= I647), R828 (≠ K771), C829 (= C772), S830 (= S773), G987 (= G930), A988 (= A931), F995 (= F938)
- binding nicotinamide-adenine-dinucleotide: I688 (≠ A638), S689 (≠ P639), P690 (= P640), W691 (= W641), N692 (= N642), I697 (= I647), K715 (= K665), A717 (= A667), E718 (≠ P668), G748 (= G699), G751 (= G702), A752 (≠ R703), T766 (= T717), G767 (= G718), S768 (≠ A719), V771 (≠ T722), I775 (≠ F726), E795 (= E738), T796 (= T739), C829 (= C772), E925 (= E870), F927 (= F872), F995 (= F938)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 247:1022/1218 of 6x9dA
- active site: N692 (= N642), K715 (= K665), E795 (= E738), C829 (= C772), E925 (= E870), A1007 (= A952)
- binding flavin-adenine dinucleotide: D291 (= D237), A292 (≠ M238), V323 (= V268), Q325 (= Q270), R352 (= R301), V354 (= V303), K355 (= K304), G356 (= G305), A357 (= A306), Y358 (vs. gap), W359 (vs. gap), F377 (≠ L325), T378 (≠ P326), R379 (≠ S327), K380 (= K328), T383 (≠ S331), A406 (= A356), T407 (≠ G357), H408 (= H358), N409 (= N359), Q432 (≠ E382), C433 (≠ M383), E477 (= E427), S483 (≠ N433), F484 (= F434)
- binding 4-hydroxyproline: E659 (= E606), F693 (= F643), I697 (= I647), R828 (≠ K771), S830 (= S773), G987 (= G930), A988 (= A931), F995 (= F938)
- binding nicotinamide-adenine-dinucleotide: I688 (≠ A638), S689 (≠ P639), P690 (= P640), W691 (= W641), N692 (= N642), I697 (= I647), K715 (= K665), A717 (= A667), E718 (≠ P668), G748 (= G699), G751 (= G702), A752 (≠ R703), T766 (= T717), G767 (= G718), S768 (≠ A719), V771 (≠ T722), E795 (= E738), T796 (= T739), C829 (= C772), E925 (= E870), F927 (= F872), F995 (= F938)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 242:1017/1209 of 6x9cA
- active site: N687 (= N642), K710 (= K665), E790 (= E738), C824 (= C772), E920 (= E870), A1002 (= A952)
- binding dihydroflavine-adenine dinucleotide: D286 (= D237), A287 (≠ M238), V318 (= V268), Q320 (= Q270), R347 (= R301), V349 (= V303), K350 (= K304), G351 (= G305), A352 (= A306), Y353 (vs. gap), W354 (vs. gap), F372 (≠ L325), T373 (≠ P326), R374 (≠ S327), K375 (= K328), T378 (≠ S331), A401 (= A356), T402 (≠ G357), H403 (= H358), N404 (= N359), Q427 (≠ E382), C428 (≠ M383), E472 (= E427), S478 (≠ N433), F479 (= F434)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (≠ A638), S684 (≠ P639), P685 (= P640), W686 (= W641), N687 (= N642), K710 (= K665), E713 (≠ P668), G743 (= G699), G746 (= G702), A747 (≠ R703), F760 (≠ L716), G762 (= G718), S763 (≠ A719), V766 (≠ T722), E920 (= E870), F922 (= F872)
- binding proline: R823 (≠ K771), C824 (= C772), S825 (= S773), G982 (= G930), A983 (= A931), F990 (= F938)
9e0cA Bifunctional protein PutA (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 245:1020/1216 of 9e0cA
- binding (1-benzofuran-5-yl)methanol: K248 (= K194), D289 (= D237), Y356 (vs. gap), Y456 (= Y405)
- binding flavin-adenine dinucleotide: D289 (= D237), A290 (≠ M238), V321 (= V268), R350 (= R301), V352 (= V303), K353 (= K304), G354 (= G305), A355 (= A306), Y356 (vs. gap), W357 (vs. gap), F375 (≠ L325), T376 (≠ P326), R377 (≠ S327), K378 (= K328), T381 (≠ S331), A404 (= A356), T405 (≠ G357), H406 (= H358), N407 (= N359), Q430 (≠ E382), C431 (≠ M383), E475 (= E427), S481 (≠ N433), F482 (= F434)
- binding nicotinamide-adenine-dinucleotide: I686 (≠ A638), S687 (≠ P639), P688 (= P640), W689 (= W641), N690 (= N642), I695 (= I647), K713 (= K665), A715 (= A667), E716 (≠ P668), G746 (= G699), G749 (= G702), A750 (≠ R703), F763 (≠ L716), T764 (= T717), G765 (= G718), S766 (≠ A719), V769 (≠ T722), I773 (≠ F726), E793 (= E738), T794 (= T739), C827 (= C772), E923 (= E870), F925 (= F872), F993 (= F938)
9dl2A Structure of proline utilization a complexed with 2,3-dihydro-1,4- benzodioxine-5-carboxylic acid (see paper)
30% identity, 66% coverage: 191:969/1180 of query aligns to 245:1020/1216 of 9dl2A
- binding 2,3-dihydro-1,4-benzodioxine-5-carboxylic acid: E657 (= E606), F691 (= F643), A694 (= A646), R826 (≠ K771), S828 (= S773), G985 (= G930), A986 (= A931), F993 (= F938)
- binding flavin-adenine dinucleotide: D289 (= D237), A290 (≠ M238), V321 (= V268), R350 (= R301), V352 (= V303), K353 (= K304), G354 (= G305), A355 (= A306), Y356 (vs. gap), W357 (vs. gap), F375 (≠ L325), T376 (≠ P326), R377 (≠ S327), K378 (= K328), T381 (≠ S331), A404 (= A356), T405 (≠ G357), H406 (= H358), N407 (= N359), Q430 (≠ E382), C431 (≠ M383), E475 (= E427), N476 (= N428), S481 (≠ N433), F482 (= F434)
- binding nicotinamide-adenine-dinucleotide: I686 (≠ A638), S687 (≠ P639), P688 (= P640), W689 (= W641), N690 (= N642), I695 (= I647), K713 (= K665), A715 (= A667), E716 (≠ P668), G746 (= G699), G749 (= G702), F763 (≠ L716), T764 (= T717), G765 (= G718), S766 (≠ A719), V769 (≠ T722), I773 (≠ F726), E793 (= E738), T794 (= T739), C827 (= C772), E923 (= E870), F925 (= F872), F993 (= F938)
Query Sequence
>WP_104912863.1 NCBI__GCF_002950575.1:WP_104912863.1
MSLTVSKSNTAQVSTKGVRGAKTLSDDCVELVHQWLDRAATLHKKPHASSQRLADLLKDP
DGPAFALGFVDRVLRPEDLTVAARALRELGQKPPAFLTGILRWLLMVGSWFAPLLPAIVV
PIARKALKTLIGHLIIDASDASLERTLKRLTKRGDQLNINLLGEAVLGAGEATKRLEGIE
RLIERRDVTYVSVKVSSVVAQLSMWSYDQTVERVVEKLVPLYEKAAATNPPTFINLDMEE
YRDLEMTLDVFQRVLGRESLHHYYGGIVMQAYLPEALDAMKRLSAFATERVAKGGAQLKV
RVVKGANLQMEQVDAALHDWPVAVLPSKQESDTNYKRVLEWSLSPERAKAIRIGVAGHNL
FDLAFSHLLATSRGVREHVDFEMLVGMAPDQADAVRETVGPLILYTPVVHSHEFDAAVGY
LVRRLDENASPENFMSAVFDLHDHSDVFAREEARFRASLDAMTQKAPTPSRTQDRTLETR
PRTLPAVDEFHNEPDTDLALPANQEWARGIYRHAASLEGQAAGLDTLQGGLISDDLGPID
GRIEIDSIVEKMRRGGKKWAARGAEGRGKILLKAAAELGVRRGEIMSVMMQEAGKTLAES
DPEISEAIDFARYYASQAVEMEQLNGAKFTPVGLTMVAPPWNFPVAIPTGSVTSALAAGS
AVIIKPAPQVRRCAAVMVEALWAAGVPKDVLHLADVSEGELGRALISHQGVDRVILTGAF
ETAALFRSWRADLPVLAETSGKNALVITPSADIDLAVADLVKSAFGHAGQKCSAASLVIL
VGSVAKSERFWRQLEDAVNTLDVGWPDARPETTMNPIIEPPGAKLRQGLTELGAGEEWLA
EPRQLDDTERLWSPGVRLGVRPGSTFHQTEYFGPLLGVMTARTLQDAVEYQNSVEYGLTA
GIHSLDPDEVSYWLDHVHAGNLYVNRGITGAIVRRQPFGGWKKSSVGPTAKAGGPNYLFG
LGSLTSAPVNRDLVGSVEDIAPEFLEVVAAAGETLTPEERESLTHALLSDQHAYSHHYGA
SVDVSEVGVERNVFRYRPFEAVVRASSLTPLVDVLRVVLAGLRTGSVVHLSSSDSLPDPV
MRVLGSPSGNRPALASVHVESELEFVERVRRNPPQRIRLLGGNANVMYVHFDGSPAVAVW
DDEVTQSGRVEMLPFVREQAVSITGHRFGAPDPRFLSLPV
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