SitesBLAST
Comparing WP_011767475.1 NCBI__GCF_000061505.1:WP_011767475.1 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)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1218/1218 of 6x9dA
- active site: N692 (= N699), K715 (= K722), E795 (= E801), C829 (= C835), E925 (= E931), A1007 (= A1013)
- binding flavin-adenine dinucleotide: D291 (= D294), A292 (= A295), V323 (= V326), Q325 (= Q328), R352 (= R355), V354 (= V357), K355 (= K358), G356 (= G359), A357 (= A360), Y358 (= Y361), W359 (= W362), F377 (≠ Y380), T378 (= T381), R379 (= R382), K380 (= K383), T383 (= T386), A406 (= A409), T407 (= T410), H408 (= H411), N409 (= N412), Q432 (= Q438), C433 (= C439), E477 (= E483), S483 (= S489), F484 (= F490)
- binding 4-hydroxyproline: E659 (= E668), F693 (= F700), I697 (= I704), R828 (= R834), S830 (= S836), G987 (= G993), A988 (= A994), F995 (= F1001)
- binding nicotinamide-adenine-dinucleotide: I688 (= I695), S689 (= S696), P690 (= P697), W691 (= W698), N692 (= N699), I697 (= I704), K715 (= K722), A717 (= A724), E718 (≠ L725), G748 (= G756), G751 (= G759), A752 (≠ Q760), T766 (= T774), G767 (= G775), S768 (= S776), V771 (= V779), E795 (= E801), T796 (= T802), C829 (= C835), E925 (= E931), F927 (= F933), F995 (= F1001)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D294), A291 (= A295), V322 (= V326), Q324 (= Q328), R351 (= R355), V353 (= V357), K354 (= K358), G355 (= G359), A356 (= A360), Y357 (= Y361), W358 (= W362), F376 (≠ Y380), T377 (= T381), R378 (= R382), K379 (= K383), T382 (= T386), A405 (= A409), T406 (= T410), H407 (= H411), N408 (= N412), C432 (= C439), L433 (= L440), E476 (= E483), S482 (= S489), F483 (= F490)
- binding nicotinamide-adenine-dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), I696 (= I704), K714 (= K722), E717 (≠ L725), G747 (= G756), G750 (= G759), T765 (= T774), G766 (= G775), S767 (= S776), V770 (= V779), I774 (≠ L783), E794 (= E801), T795 (= T802), C828 (= C835), E924 (= E931), F926 (= F933), F994 (= F1001)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K253), Y457 (= Y464), Y469 (= Y476), R472 (= R479), R473 (= R480)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K253), D290 (= D294), Y457 (= Y464), Y469 (= Y476), R472 (= R479), R473 (= R480)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), I696 (= I704), K714 (= K722), A716 (= A724), E717 (≠ L725), G747 (= G756), G750 (= G759), A751 (≠ Q760), T765 (= T774), G766 (= G775), S767 (= S776), V770 (= V779), E794 (= E801), T795 (= T802), C828 (= C835), E924 (= E931), F926 (= F933), F994 (= F1001)
- 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 (= D294), A291 (= A295), V322 (= V326), Q324 (= Q328), V353 (= V357), K354 (= K358), G355 (= G359), A356 (= A360), W358 (= W362), F376 (≠ Y380), T377 (= T381), R378 (= R382), K379 (= K383), T382 (= T386), A405 (= A409), T406 (= T410), H407 (= H411), N408 (= N412), Q431 (= Q438), C432 (= C439), L433 (= L440), Y457 (= Y464), E476 (= E483), G1217 (= G1221)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D294), A290 (= A295), V321 (= V326), Q323 (= Q328), R350 (= R355), V352 (= V357), K353 (= K358), G354 (= G359), A355 (= A360), Y356 (= Y361), W357 (= W362), F375 (≠ Y380), T376 (= T381), R377 (= R382), K378 (= K383), T381 (= T386), A404 (= A409), T405 (= T410), H406 (= H411), N407 (= N412), C431 (= C439), L432 (= L440), E475 (= E483), S481 (= S489), F482 (= F490)
- binding nicotinamide-adenine-dinucleotide: I686 (= I695), S687 (= S696), P688 (= P697), W689 (= W698), N690 (= N699), I695 (= I704), K713 (= K722), A715 (= A724), E716 (≠ L725), G746 (= G756), G749 (= G759), A750 (≠ Q760), T764 (= T774), G765 (= G775), S766 (= S776), V769 (= V779), E793 (= E801), T794 (= T802), C827 (= C835), E923 (= E931), F925 (= F933), F993 (= F1001)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y464), Y468 (= Y476), R471 (= R479), R472 (= R480)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1214/1214 of 6x9bA
- active site: N688 (= N699), K711 (= K722), E791 (= E801), C825 (= C835), E921 (= E931), A1003 (= A1013)
- binding flavin-adenine dinucleotide: D287 (= D294), A288 (= A295), V319 (= V326), R348 (= R355), V350 (= V357), K351 (= K358), G352 (= G359), A353 (= A360), Y354 (= Y361), W355 (= W362), F373 (≠ Y380), T374 (= T381), R375 (= R382), K376 (= K383), T379 (= T386), A402 (= A409), T403 (= T410), H404 (= H411), N405 (= N412), Q428 (= Q438), C429 (= C439), Y454 (= Y464), E473 (= E483), S479 (= S489), F480 (= F490)
- binding nicotinamide-adenine-dinucleotide: I684 (= I695), S685 (= S696), P686 (= P697), W687 (= W698), N688 (= N699), I693 (= I704), K711 (= K722), A713 (= A724), E714 (≠ L725), G744 (= G756), G747 (= G759), A748 (≠ Q760), T762 (= T774), G763 (= G775), S764 (= S776), V767 (= V779), I771 (≠ L783), E791 (= E801), T792 (= T802), C825 (= C835), E921 (= E931), F923 (= F933)
- binding (4R)-4-hydroxy-D-proline: E655 (= E668), F689 (= F700), S826 (= S836), G983 (= G993), A984 (= A994), F991 (= F1001)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
55% identity, 99% coverage: 14:1220/1221 of query aligns to 18:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), K714 (= K722), E717 (≠ L725), G747 (= G756), G750 (= G759), A751 (≠ Q760), F764 (= F773), G766 (= G775), S767 (= S776), V770 (= V779), T795 (= T802), G796 (= G803), C828 (= C835), E924 (= E931), F926 (= F933)
- 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 (= K253), D290 (= D294), A291 (= A295), V322 (= V326), Q324 (= Q328), R351 (= R355), V353 (= V357), K354 (= K358), G355 (= G359), A356 (= A360), Y357 (= Y361), W358 (= W362), F376 (≠ Y380), T377 (= T381), R378 (= R382), K379 (= K383), T382 (= T386), A405 (= A409), T406 (= T410), H407 (= H411), N408 (= N412), Q431 (= Q438), C432 (= C439), L433 (= L440), Y457 (= Y464), S482 (= S489), F483 (= F490)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1216/1216 of 6x99A
- active site: N690 (= N699), K713 (= K722), E793 (= E801), C827 (= C835), E923 (= E931), A1005 (= A1013)
- binding d-proline: W557 (≠ R563), T558 (≠ R564), E657 (= E668), F691 (= F700), R727 (≠ E736), R826 (= R834), S828 (= S836), G985 (= G993), A986 (= A994), F993 (= F1001)
- binding flavin-adenine dinucleotide: D289 (= D294), A290 (= A295), V321 (= V326), R350 (= R355), V352 (= V357), K353 (= K358), G354 (= G359), A355 (= A360), Y356 (= Y361), W357 (= W362), F375 (≠ Y380), T376 (= T381), R377 (= R382), K378 (= K383), T381 (= T386), A404 (= A409), T405 (= T410), H406 (= H411), N407 (= N412), Q430 (= Q438), C431 (= C439), Y456 (= Y464), E475 (= E483), S481 (= S489), F482 (= F490)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1221/1221 of query aligns to 18:1214/1214 of 6x9aA
- active site: N688 (= N699), K711 (= K722), E791 (= E801), C825 (= C835), E921 (= E931), A1003 (= A1013)
- binding flavin-adenine dinucleotide: D287 (= D294), A288 (= A295), V319 (= V326), R348 (= R355), V350 (= V357), K351 (= K358), G352 (= G359), A353 (= A360), Y354 (= Y361), W355 (= W362), F373 (≠ Y380), T374 (= T381), R375 (= R382), K376 (= K383), T379 (= T386), A402 (= A409), T403 (= T410), H404 (= H411), N405 (= N412), C429 (= C439), E473 (= E483), S479 (= S489), F480 (= F490)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ R563), T556 (≠ R564), E655 (= E668), F689 (= F700), R725 (≠ E736), S826 (= S836), G983 (= G993), A984 (= A994), F991 (= F1001)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
55% identity, 99% coverage: 14:1217/1221 of query aligns to 17:1209/1209 of 6x9cA
- active site: N687 (= N699), K710 (= K722), E790 (= E801), C824 (= C835), E920 (= E931), A1002 (= A1013)
- binding dihydroflavine-adenine dinucleotide: D286 (= D294), A287 (= A295), V318 (= V326), Q320 (= Q328), R347 (= R355), V349 (= V357), K350 (= K358), G351 (= G359), A352 (= A360), Y353 (= Y361), W354 (= W362), F372 (≠ Y380), T373 (= T381), R374 (= R382), K375 (= K383), T378 (= T386), A401 (= A409), T402 (= T410), H403 (= H411), N404 (= N412), Q427 (= Q438), C428 (= C439), E472 (= E483), S478 (= S489), F479 (= F490)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I695), S684 (= S696), P685 (= P697), W686 (= W698), N687 (= N699), K710 (= K722), E713 (≠ L725), G743 (= G756), G746 (= G759), A747 (≠ Q760), F760 (= F773), G762 (= G775), S763 (= S776), V766 (= V779), E920 (= E931), F922 (= F933)
- binding proline: R823 (= R834), C824 (= C835), S825 (= S836), G982 (= G993), A983 (= A994), F990 (= F1001)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
55% identity, 99% coverage: 14:1218/1221 of query aligns to 18:1206/1207 of 5kf6A
- active site: N683 (= N699), K706 (= K722), E786 (= E801), C820 (= C835), E916 (= E931), A998 (= A1013)
- binding flavin-adenine dinucleotide: D282 (= D294), A283 (= A295), V314 (= V326), Q316 (= Q328), R343 (= R355), V345 (= V357), K346 (= K358), G347 (= G359), A348 (= A360), Y349 (= Y361), W350 (= W362), F368 (≠ Y380), T369 (= T381), R370 (= R382), K371 (= K383), T374 (= T386), A397 (= A409), T398 (= T410), H399 (= H411), N400 (= N412), Q423 (= Q438), C424 (= C439), L425 (= L440), E468 (= E483), S474 (= S489), F475 (= F490)
- binding nicotinamide-adenine-dinucleotide: I679 (= I695), S680 (= S696), P681 (= P697), W682 (= W698), N683 (= N699), I688 (= I704), K706 (= K722), A708 (= A724), E709 (≠ L725), G739 (= G756), G742 (= G759), A743 (≠ Q760), F756 (= F773), T757 (= T774), G758 (= G775), S759 (= S776), V762 (= V779), I766 (≠ L783), E786 (= E801), T787 (= T802), C820 (= C835), E916 (= E931), F918 (= F933), F986 (= F1001)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K253), D282 (= D294), Y449 (= Y464), R464 (= R479), R465 (= R480)
6ufpA Structure of proline utilization a with the fad covalently modified by l-thiazolidine-2-carboxylate and three cysteines (cys46, cys470, cys638) modified to s,s-(2-hydroxyethyl)thiocysteine (see paper)
55% identity, 99% coverage: 14:1218/1221 of query aligns to 18:1196/1197 of 6ufpA
- active site: N673 (= N699), K696 (= K722), E776 (= E801), C810 (= C835), E906 (= E931), A988 (= A1013)
- binding dihydroflavine-adenine dinucleotide: D285 (= D294), A286 (= A295), V317 (= V326), Q319 (= Q328), R346 (= R355), V348 (= V357), K349 (= K358), G350 (= G359), A351 (= A360), W353 (= W362), F371 (≠ Y380), T372 (= T381), R373 (= R382), K374 (= K383), T377 (= T386), A400 (= A409), T401 (= T410), H402 (= H411), N403 (= N412), Q426 (= Q438), C427 (= C439), L428 (= L440), S464 (= S489)
- binding nicotinamide-adenine-dinucleotide: I669 (= I695), P671 (= P697), W672 (= W698), N673 (= N699), I678 (= I704), K696 (= K722), E699 (≠ L725), G729 (= G756), G732 (= G759), F746 (= F773), T747 (= T774), G748 (= G775), S749 (= S776), V752 (= V779), E776 (= E801), T777 (= T802), C810 (= C835), E906 (= E931), F908 (= F933)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K253), D285 (= D294), Y439 (= Y464), Y451 (= Y476), R454 (= R479), R455 (= R480)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
50% identity, 80% coverage: 48:1022/1221 of query aligns to 34:969/983 of 3hazA
- active site: N652 (= N699), K675 (= K722), E752 (= E801), C786 (= C835), E878 (= E931), A960 (= A1013)
- binding flavin-adenine dinucleotide: D272 (= D294), A273 (= A295), Q306 (= Q328), R333 (= R355), V335 (= V357), K336 (= K358), G337 (= G359), A338 (= A360), Y339 (= Y361), W340 (= W362), F358 (≠ Y380), T359 (= T381), R360 (= R382), K361 (= K383), T364 (= T386), A387 (= A409), T388 (= T410), H389 (= H411), N390 (= N412), Y435 (= Y464), S460 (= S489), F461 (= F490)
- binding nicotinamide-adenine-dinucleotide: I648 (= I695), S649 (= S696), P650 (= P697), W651 (= W698), N652 (= N699), I657 (= I704), K675 (= K722), P676 (= P723), A677 (= A724), G708 (= G756), G711 (= G759), A712 (≠ Q760), T726 (= T774), G727 (= G775), S728 (= S776), V731 (= V779), I735 (≠ L783), E752 (= E801), T753 (= T802), C786 (= C835), E878 (= E931), F880 (= F933), F948 (= F1001)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
50% identity, 80% coverage: 48:1022/1221 of query aligns to 34:960/973 of 6bsnA
- active site: N643 (= N699), E743 (= E801), A777 (≠ C835), A951 (= A1013)
- binding dihydroflavine-adenine dinucleotide: D269 (= D294), A270 (= A295), Q303 (= Q328), R330 (= R355), V332 (= V357), K333 (= K358), G334 (= G359), A335 (= A360), Y336 (= Y361), W337 (= W362), F355 (≠ Y380), T356 (= T381), R357 (= R382), K358 (= K383), T361 (= T386), A384 (= A409), T385 (= T410), H386 (= H411), N387 (= N412), Y432 (= Y464), S457 (= S489), F458 (= F490)
- binding proline: M630 (vs. gap), W642 (= W698), F644 (= F700), G718 (= G775), R776 (= R834), S778 (= S836), F871 (= F933), I930 (≠ V992), G931 (= G993), A932 (= A994), F939 (= F1001), A958 (≠ H1020), R959 (= R1021)
Sites not aligning to the query:
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
59% identity, 42% coverage: 15:526/1221 of query aligns to 5:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K253), Y433 (= Y464), R448 (= R479), R449 (= R480)
- binding flavin-adenine dinucleotide: D263 (= D294), A264 (= A295), V295 (= V326), Q297 (= Q328), R324 (= R355), V326 (= V357), K327 (= K358), G328 (= G359), A329 (= A360), Y330 (= Y361), W331 (= W362), Y349 (= Y380), T350 (= T381), R351 (= R382), K352 (= K383), T355 (= T386), A378 (= A409), T379 (= T410), H380 (= H411), N381 (= N412), C405 (= C439), L406 (= L440), E452 (= E483), S458 (= S489)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
59% identity, 42% coverage: 15:526/1221 of query aligns to 5:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D294), A260 (= A295), V291 (= V326), Q293 (= Q328), R320 (= R355), V322 (= V357), K323 (= K358), G324 (= G359), A325 (= A360), Y326 (= Y361), W327 (= W362), Y345 (= Y380), T346 (= T381), R347 (= R382), K348 (= K383), T351 (= T386), A374 (= A409), T375 (= T410), H376 (= H411), N377 (= N412), C401 (= C439), L402 (= L440), E448 (= E483), S454 (= S489)
- binding cyclopropanecarboxylic acid: K218 (= K253), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
59% identity, 42% coverage: 15:526/1221 of query aligns to 5:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D294), A260 (= A295), V291 (= V326), Q293 (= Q328), R320 (= R355), V322 (= V357), K323 (= K358), G324 (= G359), A325 (= A360), Y326 (= Y361), W327 (= W362), Y345 (= Y380), T346 (= T381), R347 (= R382), K348 (= K383), T351 (= T386), A374 (= A409), T375 (= T410), H376 (= H411), N377 (= N412), C401 (= C439), L402 (= L440), E448 (= E483), S454 (= S489)
- binding cyclobutanecarboxylic acid: K218 (= K253), L402 (= L440), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
59% identity, 42% coverage: 15:526/1221 of query aligns to 5:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D294), A260 (= A295), V291 (= V326), Q293 (= Q328), R320 (= R355), V322 (= V357), K323 (= K358), G324 (= G359), A325 (= A360), Y326 (= Y361), W327 (= W362), Y345 (= Y380), T346 (= T381), R347 (= R382), K348 (= K383), T351 (= T386), A374 (= A409), T375 (= T410), H376 (= H411), N377 (= N412), C401 (= C439), L402 (= L440), E448 (= E483), S454 (= S489)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K253), Y326 (= Y361), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
58% identity, 42% coverage: 15:526/1221 of query aligns to 6:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A295), V283 (= V326), Q285 (= Q328), R312 (= R355), V314 (= V357), K315 (= K358), G316 (= G359), A317 (= A360), Y318 (= Y361), W319 (= W362), Y337 (= Y380), T338 (= T381), R339 (= R382), K340 (= K383), T343 (= T386), A366 (= A409), T367 (= T410), H368 (= H411), N369 (= N412), C393 (= C439), L394 (= L440), E440 (= E483), S446 (= S489), F447 (= F490)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K253), Y421 (= Y464), R436 (= R479), R437 (= R480)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
56% identity, 42% coverage: 15:526/1221 of query aligns to 5:467/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D294), A230 (= A295), V261 (= V326), Q263 (= Q328), R290 (= R355), V292 (= V357), K293 (= K358), G294 (= G359), A295 (= A360), Y296 (= Y361), W297 (= W362), Y315 (= Y380), T316 (= T381), R317 (= R382), K318 (= K383), T321 (= T386), A344 (= A409), T345 (= T410), H346 (= H411), N347 (= N412), Q370 (= Q438), C371 (= C439), L372 (= L440), E418 (= E483), S424 (= S489)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
55% identity, 42% coverage: 15:526/1221 of query aligns to 5:466/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D294), A229 (= A295), V260 (= V326), Q262 (= Q328), V291 (= V357), K292 (= K358), G293 (= G359), A294 (= A360), Y295 (= Y361), W296 (= W362), Y314 (= Y380), T315 (= T381), R316 (= R382), K317 (= K383), T320 (= T386), A343 (= A409), T344 (= T410), H345 (= H411), N346 (= N412), C370 (= C439), L371 (= L440), E417 (= E483), S423 (= S489), F424 (= F490)
- binding proline: K187 (= K253), L371 (= L440), Y410 (= Y476), R413 (= R479), R414 (= R480)
Query Sequence
>WP_011767475.1 NCBI__GCF_000061505.1:WP_011767475.1
MRFDADVPEAPGALRAAITAATRRDEADCVHALVAELQQRRARLGLDDAAVEARAAALVV
DVRRRRRGAGGVDQLMHEFSLSTQEGVALMCLAEALLRIPDHATADRLIRDKIGQGDWRT
HLGHSESLFVNAATWGLLISGRLVATRSERALGSALSRLLARGGEPVVRRGVDFAMRLLG
QQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAA
GHGPRAGPGISIKLSALHPRYCRAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEADR
LELSLDLFEALVADPLLAGWDGLGFVVQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGA
YWDSEIKRAQVEGQAGYPVYTRKAHTDLAYLVCAARLLAEAGAVYPQFATHNARTVAEVH
EMAQCVGAGGTLPAYEFQCLHGMGESLYDSVVGGARLGVPCRIYAPVGSHRTLLPYLVRR
LLENGANSSFVNRIVDDSMPVAALAADPLQAVLAGDVTPHPSIPLPAGLYGPERRNSAGL
DLASDAVLAALEAALVARAGEPRRAQPLLGSGKLDEAAARQRARPVCNPADHADIVGSVV
EALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWG
NAVAEVREAVDFCRYYAQQVVTLPAPTQAAPLVCISPWNFPLAIFVGQLSAALAAGRCVL
AKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVA
RGLARWLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRV
LCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGV
FRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRLIASINATGYG
LTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLH
RLLGTAQLDPAALGLVAPAEPAAALGVLAAWARQRGDSALAARCAEDGARSLAGCHCALP
GPTGEANTLRFVGRGVVLCVADSAPALLAQLAAALATGNSALFEAGAAAYRVAAELPSAL
GGWLGVRGHGPDPVFAVALFDGDTEAEWLLRRRLAERPGPLVAVLRADGAGRYPLHRLVA
ERVVSINTAAAGGNAALMTLG
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