SitesBLAST
Comparing 352642 FitnessBrowser__Btheta:352642 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)
5ux5A Structure of proline utilization a (puta) from corynebacterium freiburgense (see paper)
35% identity, 93% coverage: 70:1099/1106 of query aligns to 24:963/963 of 5ux5A
- active site: C617 (= C743), K792 (= K920)
- binding flavin-adenine dinucleotide: D138 (= D192), M139 (= M193), R202 (= R256), V204 (= V258), K205 (= K259), G206 (= G260), A207 (≠ C261), L209 (= L263), T228 (≠ S282), K229 (= K283), V232 (= V286), S257 (= S312), N259 (= N314), E282 (= E337), M283 (= M338), N328 (= N388)
- binding nicotinamide-adenine-dinucleotide: S484 (= S611), W486 (= W613), K510 (= K637), A512 (= A639), E543 (≠ R669), G547 (≠ L673), G563 (= G689), A564 (≠ G690), T567 (= T693), F571 (≠ I697), F713 (= F841)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
29% identity, 79% coverage: 60:932/1106 of query aligns to 72:942/959 of 5ur2B
- active site: N618 (= N614), K641 (= K637), E722 (= E709), C756 (= C743), E851 (= E839), T931 (≠ A921)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K141), D215 (= D192), M216 (= M193), Q249 (= Q225), V278 (= V258), K279 (= K259), G280 (= G260), A281 (≠ C261), W283 (≠ L263), Y300 (≠ R280), T301 (≠ P281), N302 (≠ S282), K303 (= K283), S306 (≠ V286), A329 (= A311), S330 (= S312), H331 (= H313), N332 (= N314), Q356 (≠ E337), M357 (= M338), L358 (= L339), Y379 (= Y360), E398 (= E382), E403 (≠ D387), W405 (≠ F389)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
27% identity, 84% coverage: 2:932/1106 of query aligns to 43:954/977 of 4nmaA
- active site: N629 (= N614), K652 (= K637), E733 (= E709), C767 (= C743), E863 (= E839), A943 (= A921)
- binding flavin-adenine dinucleotide: D226 (= D192), M227 (= M193), Q258 (= Q225), R285 (= R256), V287 (= V258), K288 (= K259), G289 (= G260), A290 (≠ C261), Y291 (≠ N262), W292 (≠ L263), W309 (≠ R280), T310 (≠ P281), I311 (≠ S282), K312 (= K283), S315 (≠ V286), A338 (= A311), S339 (= S312), H340 (= H313), N341 (= N314), Q365 (≠ E337), L367 (= L339), E407 (= E382), S413 (≠ N388), F414 (= F389)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K141), Y388 (= Y360), Y400 (= Y375), R403 (= R378), R404 (= R379)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
29% identity, 79% coverage: 58:932/1106 of query aligns to 73:956/979 of 4nmdA
- active site: N631 (= N614), K654 (= K637), E735 (= E709), C769 (= C743), E865 (= E839), A945 (= A921)
- binding dihydroflavine-adenine dinucleotide: D226 (= D192), M227 (= M193), V256 (= V223), Q258 (= Q225), R285 (= R256), V287 (= V258), K288 (= K259), G289 (= G260), A290 (≠ C261), W292 (≠ L263), W309 (≠ R280), T310 (≠ P281), I311 (≠ S282), K312 (= K283), S315 (≠ V286), A338 (= A311), S339 (= S312), H340 (= H313), N341 (= N314), Q365 (≠ E337), V366 (≠ M338), L367 (= L339), Y388 (= Y360), F414 (= F389)
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, 79% coverage: 58:932/1106 of query aligns to 72:956/979 of 4nmfB
- active site: N631 (= N614), K654 (= K637), E735 (= E709), C769 (= C743), E865 (= E839), A945 (= A921)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K141), Y290 (≠ N262), Y387 (= Y360), Y399 (= Y375), R402 (= R378), R403 (= R379)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K141), L366 (= L339), Y399 (= Y375), R402 (= R378)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K141), D225 (= D192), M226 (= M193), V255 (= V223), Q257 (= Q225), R284 (= R256), V286 (= V258), K287 (= K259), G288 (= G260), A289 (≠ C261), W291 (≠ L263), W308 (≠ R280), T309 (≠ P281), I310 (≠ S282), K311 (= K283), S314 (≠ V286), A337 (= A311), S338 (= S312), H339 (= H313), N340 (= N314), Q364 (≠ E337), L366 (= L339), Y387 (= Y360), E406 (= E382), E411 (≠ D387), S412 (≠ N388), F413 (= F389)
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, 79% coverage: 58:932/1106 of query aligns to 69:950/973 of 4nmfA
- active site: N625 (= N614), K648 (= K637), E729 (= E709), C763 (= C743), E859 (= E839), A939 (= A921)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K141), Y287 (≠ N262), Y384 (= Y360), Y396 (= Y375), R399 (= R378), R400 (= R379)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K141), D222 (= D192), M223 (= M193), V252 (= V223), Q254 (= Q225), R281 (= R256), V283 (= V258), K284 (= K259), G285 (= G260), A286 (≠ C261), W288 (≠ L263), W305 (≠ R280), T306 (≠ P281), I307 (≠ S282), K308 (= K283), S311 (≠ V286), A334 (= A311), S335 (= S312), H336 (= H313), N337 (= N314), Q361 (≠ E337), V362 (≠ M338), L363 (= L339), Y384 (= Y360), E403 (= E382), E408 (≠ D387), F410 (= F389)
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
28% identity, 79% coverage: 58:932/1106 of query aligns to 75:957/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D192), M227 (= M193), V256 (= V223), Q258 (= Q225), R285 (= R256), V287 (= V258), K288 (= K259), G289 (= G260), A290 (≠ C261), Y291 (≠ N262), W292 (≠ L263), W309 (≠ R280), T310 (≠ P281), I311 (≠ S282), K312 (= K283), S315 (≠ V286), A338 (= A311), S339 (= S312), H340 (= H313), N341 (= N314), L367 (= L339), Y388 (= Y360), E407 (= E382), S413 (≠ N388), F414 (= F389)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
28% identity, 79% coverage: 58:932/1106 of query aligns to 73:949/972 of 4nmeA
- active site: N624 (= N614), K647 (= K637), E728 (= E709), C762 (= C743), E858 (= E839), A938 (= A921)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K141), D224 (= D192), M225 (= M193), V254 (= V223), Q256 (= Q225), R283 (= R256), V285 (= V258), K286 (= K259), G287 (= G260), A288 (≠ C261), W290 (≠ L263), W307 (≠ R280), T308 (≠ P281), I309 (≠ S282), K310 (= K283), S313 (≠ V286), A336 (= A311), S337 (= S312), H338 (= H313), N339 (= N314), Q363 (≠ E337), L365 (= L339), Y383 (= Y360), E402 (= E382), F409 (= F389)
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
26% identity, 84% coverage: 6:932/1106 of query aligns to 18:919/941 of 4nmcA
- active site: N594 (= N614), K617 (= K637), E698 (= E709), C732 (= C743), E828 (= E839), A908 (= A921)
- binding flavin-adenine dinucleotide: D215 (= D192), M216 (= M193), V245 (= V223), Q247 (= Q225), R274 (= R256), V276 (= V258), K277 (= K259), G278 (= G260), A279 (≠ C261), W281 (≠ L263), W298 (≠ R280), T299 (≠ P281), I300 (≠ S282), K301 (= K283), S304 (≠ V286), A327 (= A311), S328 (= S312), H329 (= H313), N330 (= N314), L356 (= L339), Y377 (= Y360)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
27% identity, 78% coverage: 71:930/1106 of query aligns to 148:960/973 of 6bsnA
- active site: N643 (= N614), E743 (= E709), A777 (≠ C743), A951 (= A921)
- binding dihydroflavine-adenine dinucleotide: D269 (= D192), A270 (≠ M193), Q303 (= Q225), R330 (= R256), V332 (= V258), K333 (= K259), G334 (= G260), A335 (≠ C261), Y336 (≠ N262), W337 (≠ L263), F355 (≠ R280), T356 (≠ P281), R357 (≠ S282), K358 (= K283), T361 (≠ V286), A384 (= A311), T385 (≠ S312), H386 (= H313), N387 (= N314), Y432 (= Y360), S457 (≠ N388), F458 (= F389)
- binding proline: M630 (= M601), W642 (= W613), F644 (= F615), G718 (= G689), R776 (≠ K742), S778 (= S744), F871 (= F841), I930 (≠ T898), G931 (= G899), A932 (= A900), F939 (= F907), A958 (≠ T928), R959 (≠ C929)
Sites not aligning to the query:
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 242:1007/1209 of 6x9cA
- active site: N687 (= N614), K710 (= K637), E790 (= E709), C824 (= C743), E920 (= E839), A1002 (= A921)
- binding dihydroflavine-adenine dinucleotide: D286 (= D192), A287 (≠ M193), V318 (= V223), Q320 (= Q225), R347 (= R256), V349 (= V258), K350 (= K259), G351 (= G260), A352 (≠ C261), Y353 (≠ N262), W354 (≠ L263), F372 (≠ R280), T373 (≠ P281), R374 (≠ S282), K375 (= K283), T378 (≠ V286), A401 (= A311), T402 (≠ S312), H403 (= H313), N404 (= N314), Q427 (≠ E337), C428 (≠ M338), E472 (= E382), S478 (≠ N388), F479 (= F389)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I610), S684 (= S611), P685 (= P612), W686 (= W613), N687 (= N614), K710 (= K637), E713 (≠ T640), G743 (≠ R670), G746 (≠ L673), A747 (≠ K674), F760 (≠ L687), G762 (= G689), S763 (≠ G690), V766 (≠ T693), E920 (= E839), F922 (= F841)
- binding proline: R823 (≠ K742), C824 (= C743), S825 (= S744), G982 (= G899), A983 (= A900), F990 (= F907)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 243:1008/1214 of 6x9bA
- active site: N688 (= N614), K711 (= K637), E791 (= E709), C825 (= C743), E921 (= E839), A1003 (= A921)
- binding flavin-adenine dinucleotide: D287 (= D192), A288 (≠ M193), V319 (= V223), R348 (= R256), V350 (= V258), K351 (= K259), G352 (= G260), A353 (≠ C261), Y354 (≠ N262), W355 (≠ L263), F373 (≠ R280), T374 (≠ P281), R375 (≠ S282), K376 (= K283), T379 (≠ V286), A402 (= A311), T403 (≠ S312), H404 (= H313), N405 (= N314), Q428 (≠ E337), C429 (≠ M338), Y454 (= Y360), E473 (= E382), S479 (≠ N388), F480 (= F389)
- binding nicotinamide-adenine-dinucleotide: I684 (= I610), S685 (= S611), P686 (= P612), W687 (= W613), N688 (= N614), I693 (= I619), K711 (= K637), A713 (= A639), E714 (≠ T640), G744 (≠ R670), G747 (≠ L673), A748 (≠ K674), T762 (= T688), G763 (= G689), S764 (≠ G690), V767 (≠ T693), I771 (vs. gap), E791 (= E709), T792 (= T710), C825 (= C743), E921 (= E839), F923 (= F841)
- binding (4R)-4-hydroxy-D-proline: E655 (= E578), F689 (= F615), S826 (= S744), G983 (= G899), A984 (= A900), F991 (= F907)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 243:1008/1214 of 6x9aA
- active site: N688 (= N614), K711 (= K637), E791 (= E709), C825 (= C743), E921 (= E839), A1003 (= A921)
- binding flavin-adenine dinucleotide: D287 (= D192), A288 (≠ M193), V319 (= V223), R348 (= R256), V350 (= V258), K351 (= K259), G352 (= G260), A353 (≠ C261), Y354 (≠ N262), W355 (≠ L263), F373 (≠ R280), T374 (≠ P281), R375 (≠ S282), K376 (= K283), T379 (≠ V286), A402 (= A311), T403 (≠ S312), H404 (= H313), N405 (= N314), C429 (≠ M338), E473 (= E382), S479 (≠ N388), F480 (= F389)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ P475), T556 (≠ E476), E655 (= E578), F689 (= F615), R725 (≠ K651), S826 (= S744), G983 (= G899), A984 (= A900), F991 (= F907)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 238:1003/1207 of 5kf6A
- active site: N683 (= N614), K706 (= K637), E786 (= E709), C820 (= C743), E916 (= E839), A998 (= A921)
- binding flavin-adenine dinucleotide: D282 (= D192), A283 (≠ M193), V314 (= V223), Q316 (= Q225), R343 (= R256), V345 (= V258), K346 (= K259), G347 (= G260), A348 (≠ C261), Y349 (≠ N262), W350 (≠ L263), F368 (≠ R280), T369 (≠ P281), R370 (≠ S282), K371 (= K283), T374 (≠ V286), A397 (= A311), T398 (≠ S312), H399 (= H313), N400 (= N314), Q423 (≠ E337), C424 (≠ M338), L425 (= L339), E468 (= E382), S474 (≠ N388), F475 (= F389)
- binding nicotinamide-adenine-dinucleotide: I679 (= I610), S680 (= S611), P681 (= P612), W682 (= W613), N683 (= N614), I688 (= I619), K706 (= K637), A708 (= A639), E709 (≠ T640), G739 (≠ R670), G742 (≠ L673), A743 (≠ K674), F756 (≠ L687), T757 (= T688), G758 (= G689), S759 (≠ G690), V762 (≠ T693), I766 (vs. gap), E786 (= E709), T787 (= T710), C820 (= C743), E916 (= E839), F918 (= F841), F986 (= F907)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K141), D282 (= D192), Y449 (= Y360), R464 (= R378), R465 (= R379)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 246:1011/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I610), S688 (= S611), P689 (= P612), W690 (= W613), N691 (= N614), K714 (= K637), E717 (≠ T640), G747 (≠ R670), G750 (≠ L673), A751 (≠ K674), F764 (≠ L687), G766 (= G689), S767 (≠ G690), V770 (≠ T693), T795 (= T710), G796 (= G711), C828 (= C743), E924 (= E839), F926 (= F841)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-5-[(2R)-tetrahydrothiophen-2-yl]-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl}-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name): K249 (= K141), D290 (= D192), A291 (≠ M193), V322 (= V223), Q324 (= Q225), R351 (= R256), V353 (= V258), K354 (= K259), G355 (= G260), A356 (≠ C261), Y357 (≠ N262), W358 (≠ L263), F376 (≠ R280), T377 (≠ P281), R378 (≠ S282), K379 (= K283), T382 (≠ V286), A405 (= A311), T406 (≠ S312), H407 (= H313), N408 (= N314), Q431 (≠ E337), C432 (≠ M338), L433 (= L339), Y457 (= Y360), S482 (≠ N388), F483 (= F389)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 245:1010/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D192), A290 (≠ M193), V321 (= V223), Q323 (= Q225), R350 (= R256), V352 (= V258), K353 (= K259), G354 (= G260), A355 (≠ C261), Y356 (≠ N262), W357 (≠ L263), F375 (≠ R280), T376 (≠ P281), R377 (≠ S282), K378 (= K283), T381 (≠ V286), A404 (= A311), T405 (≠ S312), H406 (= H313), N407 (= N314), C431 (≠ M338), L432 (= L339), E475 (= E382), S481 (≠ N388), F482 (= F389)
- binding nicotinamide-adenine-dinucleotide: I686 (= I610), S687 (= S611), P688 (= P612), W689 (= W613), N690 (= N614), I695 (= I619), K713 (= K637), A715 (= A639), E716 (≠ T640), G746 (≠ R670), G749 (≠ L673), A750 (≠ K674), T764 (= T688), G765 (= G689), S766 (≠ G690), V769 (≠ T693), E793 (= E709), T794 (= T710), C827 (= C743), E923 (= E839), F925 (= F841), F993 (= F907)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y360), Y468 (= Y375), R471 (= R378), R472 (= R379)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 247:1012/1218 of 6x9dA
- active site: N692 (= N614), K715 (= K637), E795 (= E709), C829 (= C743), E925 (= E839), A1007 (= A921)
- binding flavin-adenine dinucleotide: D291 (= D192), A292 (≠ M193), V323 (= V223), Q325 (= Q225), R352 (= R256), V354 (= V258), K355 (= K259), G356 (= G260), A357 (≠ C261), Y358 (≠ N262), W359 (≠ L263), F377 (≠ R280), T378 (≠ P281), R379 (≠ S282), K380 (= K283), T383 (≠ V286), A406 (= A311), T407 (≠ S312), H408 (= H313), N409 (= N314), Q432 (≠ E337), C433 (≠ M338), E477 (= E382), S483 (≠ N388), F484 (= F389)
- binding 4-hydroxyproline: E659 (= E578), F693 (= F615), I697 (= I619), R828 (≠ K742), S830 (= S744), G987 (= G899), A988 (= A900), F995 (= F907)
- binding nicotinamide-adenine-dinucleotide: I688 (= I610), S689 (= S611), P690 (= P612), W691 (= W613), N692 (= N614), I697 (= I619), K715 (= K637), A717 (= A639), E718 (≠ T640), G748 (≠ R670), G751 (≠ L673), A752 (≠ K674), T766 (= T688), G767 (= G689), S768 (≠ G690), V771 (≠ T693), E795 (= E709), T796 (= T710), C829 (= C743), E925 (= E839), F927 (= F841), F995 (= F907)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 246:1011/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D192), A291 (≠ M193), V322 (= V223), Q324 (= Q225), R351 (= R256), V353 (= V258), K354 (= K259), G355 (= G260), A356 (≠ C261), Y357 (≠ N262), W358 (≠ L263), F376 (≠ R280), T377 (≠ P281), R378 (≠ S282), K379 (= K283), T382 (≠ V286), A405 (= A311), T406 (≠ S312), H407 (= H313), N408 (= N314), C432 (≠ M338), L433 (= L339), E476 (= E382), S482 (≠ N388), F483 (= F389)
- binding nicotinamide-adenine-dinucleotide: I687 (= I610), S688 (= S611), P689 (= P612), W690 (= W613), N691 (= N614), I696 (= I619), K714 (= K637), E717 (≠ T640), G747 (≠ R670), G750 (≠ L673), T765 (= T688), G766 (= G689), S767 (≠ G690), V770 (≠ T693), I774 (vs. gap), E794 (= E709), T795 (= T710), C828 (= C743), E924 (= E839), F926 (= F841), F994 (= F907)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K141), Y457 (= Y360), Y469 (= Y375), R472 (= R378), R473 (= R379)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K141), D290 (= D192), Y457 (= Y360), Y469 (= Y375), R472 (= R378), R473 (= R379)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 246:1011/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I610), S688 (= S611), P689 (= P612), W690 (= W613), N691 (= N614), I696 (= I619), K714 (= K637), A716 (= A639), E717 (≠ T640), G747 (≠ R670), G750 (≠ L673), A751 (≠ K674), T765 (= T688), G766 (= G689), S767 (≠ G690), V770 (≠ T693), E794 (= E709), T795 (= T710), C828 (= C743), E924 (= E839), F926 (= F841), F994 (= F907)
- 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 (= D192), A291 (≠ M193), V322 (= V223), Q324 (= Q225), V353 (= V258), K354 (= K259), G355 (= G260), A356 (≠ C261), W358 (≠ L263), F376 (≠ R280), T377 (≠ P281), R378 (≠ S282), K379 (= K283), T382 (≠ V286), A405 (= A311), T406 (≠ S312), H407 (= H313), N408 (= N314), Q431 (≠ E337), C432 (≠ M338), L433 (= L339), Y457 (= Y360), E476 (= E382)
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
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
28% identity, 71% coverage: 138:926/1106 of query aligns to 245:1010/1216 of 6x99A
- active site: N690 (= N614), K713 (= K637), E793 (= E709), C827 (= C743), E923 (= E839), A1005 (= A921)
- binding d-proline: W557 (≠ P475), T558 (≠ E476), E657 (= E578), F691 (= F615), R727 (≠ K651), R826 (≠ K742), S828 (= S744), G985 (= G899), A986 (= A900), F993 (= F907)
- binding flavin-adenine dinucleotide: D289 (= D192), A290 (≠ M193), V321 (= V223), R350 (= R256), V352 (= V258), K353 (= K259), G354 (= G260), A355 (≠ C261), Y356 (≠ N262), W357 (≠ L263), F375 (≠ R280), T376 (≠ P281), R377 (≠ S282), K378 (= K283), T381 (≠ V286), A404 (= A311), T405 (≠ S312), H406 (= H313), N407 (= N314), Q430 (≠ E337), C431 (≠ M338), Y456 (= Y360), E475 (= E382), S481 (≠ N388), F482 (= F389)
Query Sequence
>352642 FitnessBrowser__Btheta:352642
MVQRPQDKKFLVKMLDESSQIRDRRILAKRIKTLLDQYGVPEFLNKRDSFLFKMYQAFGH
HFDFIAIPIIKKRLRMNTSQVIINEARPQLTKHLAIRAKEKIGQNVNLLGEVVLGNGEAD
HRYHHYLKALESPDINYISVKISGIYAQTHALNYEESFPELISRMSALYQKAIDFPYTDE
EGVRRSKFINLDMEEYKDTHFTLRLFKTVLSLPQFKNYSAGIVVQAYLPDAYDFQTELIE
FAKARVAEGGAPIKMRLVKGCNLEMETVISSLRGWPNPIRPSKEEVDANYLHLLERALMP
ENARVLHLGVASHNLFSIAYAYLLAQKYGTAEYMTFEMLEGMANHLWRAQSMLGNRVILY
TPVVKNEHFLNAVSYLVRRMDENTAPDNFLTHSFNLRPNTKEWDFLAKQFEDAYAMKDQL
SHVSPRTQNRNLPYTPVPPADVLKNEPDTDFDLPQNQEWVRSIFSKWKKDGTEQPEIIPL
QIGAETVVCESRYPYTDRCQDDEVCICEMSQADSAQVEKIIEIAEADPAGWRKTTLEERH
RIMYEAANRLADMRGDLIGCMCAVTGKTVIEGDVEVSEAVDYARFYTTAMKKFAALDDVE
MKPKGTILVISPWNFPCAIPVGGIVAGLAGGNTVILKPATVAAPVAWMFAKAFWDAGVPK
EALQVIITRREALKVLTTAPAIKHIILTGGTDTAQNIAKANPTTPLSAETGGKNVIILTA
SGDRDHAIMNIVTSAFGNAGQKCSACSLLLVERSVYEDENFRSKLKDAATSLKTGSVWNA
GNIVGPMITNKNDKLLQAFNLEPGESWLVPPRFIDRREYILAPTVKWGVKPESFSFRTEL
FGPLLSVACIENLEEGIRLVNGLDYGLTSGLQSLDEKEQKLWKNSVMAGNLYINRGITGA
IVNRQPFGGMKLSAFGGGIKAGGPNYCTCFLEITDKPDSRTDYRQSYAKAYQEEFSKPRD
VNRLYGEQNLFRYLPLKNMILRLFPKDTDEEATMIAHAARICRTPLTISFGPTDDRSSRL
AGLGCTLRKESLEDFLKELPEYERVRTCSPDIPDVMYERAAETNKYIATAPPVKQGRIEL
IHYIKEQSIAFEYHRYGSISEVPPCE
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