SitesBLAST
Comparing N515DRAFT_4232 N515DRAFT_4232 L-proline dehydrogenase /delta-1-pyrroline-5-carboxylate dehydrogenase 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)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
52% identity, 95% coverage: 44:1064/1074 of query aligns to 8:983/983 of 3hazA
- active site: N652 (= N727), K675 (= K750), E752 (= E828), C786 (= C862), E878 (= E959), A960 (= A1041)
- binding flavin-adenine dinucleotide: D272 (= D318), A273 (= A319), Q306 (= Q352), R333 (= R379), V335 (= V381), K336 (= K382), G337 (= G383), A338 (= A384), Y339 (= Y385), W340 (= W386), F358 (≠ Y404), T359 (= T405), R360 (= R406), K361 (= K407), T364 (= T410), A387 (= A434), T388 (= T435), H389 (= H436), N390 (= N437), Y435 (= Y482), S460 (= S507), F461 (= F508)
- binding nicotinamide-adenine-dinucleotide: I648 (= I723), S649 (= S724), P650 (= P725), W651 (= W726), N652 (= N727), I657 (= I732), K675 (= K750), P676 (= P751), A677 (= A752), G708 (= G783), G711 (= G787), A712 (= A788), T726 (= T802), G727 (= G803), S728 (= S804), V731 (≠ T807), I735 (= I811), E752 (= E828), T753 (= T829), C786 (= C862), E878 (= E959), F880 (= F961), F948 (= F1029)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1014/1216 of 6x99A
- active site: N690 (= N727), K713 (= K750), E793 (= E828), C827 (= C862), E923 (= E959), A1005 (= A1041)
- binding d-proline: W557 (= W580), T558 (= T581), E657 (= E680), F691 (= F728), R727 (≠ Q764), R826 (= R861), S828 (= S863), G985 (= G1021), A986 (= A1022), F993 (= F1029)
- binding flavin-adenine dinucleotide: D289 (= D318), A290 (= A319), V321 (= V350), R350 (= R379), V352 (= V381), K353 (= K382), G354 (= G383), A355 (= A384), Y356 (= Y385), W357 (= W386), F375 (≠ Y404), T376 (= T405), R377 (= R406), K378 (= K407), T381 (= T410), A404 (= A434), T405 (= T435), H406 (= H436), N407 (= N437), Q430 (= Q456), C431 (≠ R457), Y456 (= Y482), E475 (= E501), S481 (= S507), F482 (= F508)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1016/1218 of 6x9dA
- active site: N692 (= N727), K715 (= K750), E795 (= E828), C829 (= C862), E925 (= E959), A1007 (= A1041)
- binding flavin-adenine dinucleotide: D291 (= D318), A292 (= A319), V323 (= V350), Q325 (= Q352), R352 (= R379), V354 (= V381), K355 (= K382), G356 (= G383), A357 (= A384), Y358 (= Y385), W359 (= W386), F377 (≠ Y404), T378 (= T405), R379 (= R406), K380 (= K407), T383 (= T410), A406 (= A434), T407 (= T435), H408 (= H436), N409 (= N437), Q432 (= Q456), C433 (≠ R457), E477 (= E501), S483 (= S507), F484 (= F508)
- binding 4-hydroxyproline: E659 (= E680), F693 (= F728), I697 (= I732), R828 (= R861), S830 (= S863), G987 (= G1021), A988 (= A1022), F995 (= F1029)
- binding nicotinamide-adenine-dinucleotide: I688 (= I723), S689 (= S724), P690 (= P725), W691 (= W726), N692 (= N727), I697 (= I732), K715 (= K750), A717 (= A752), E718 (= E753), G748 (= G783), G751 (= G787), A752 (= A788), T766 (= T802), G767 (= G803), S768 (= S804), V771 (≠ T807), E795 (= E828), T796 (= T829), C829 (= C862), E925 (= E959), F927 (= F961), F995 (= F1029)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
52% identity, 95% coverage: 44:1063/1074 of query aligns to 8:973/973 of 6bsnA
- active site: N643 (= N727), E743 (= E828), A777 (≠ C862), A951 (= A1041)
- binding dihydroflavine-adenine dinucleotide: D269 (= D318), A270 (= A319), Q303 (= Q352), R330 (= R379), V332 (= V381), K333 (= K382), G334 (= G383), A335 (= A384), Y336 (= Y385), W337 (= W386), F355 (≠ Y404), T356 (= T405), R357 (= R406), K358 (= K407), T361 (= T410), A384 (= A434), T385 (= T435), H386 (= H436), N387 (= N437), Y432 (= Y482), S457 (= S507), F458 (= F508)
- binding proline: M630 (≠ L714), W642 (= W726), F644 (= F728), G718 (= G803), R776 (= R861), S778 (= S863), F871 (= F961), I930 (= I1020), G931 (= G1021), A932 (= A1022), F939 (= F1029), A958 (≠ F1048), R959 (= R1049), A961 (= A1051)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1012/1214 of 6x9bA
- active site: N688 (= N727), K711 (= K750), E791 (= E828), C825 (= C862), E921 (= E959), A1003 (= A1041)
- binding flavin-adenine dinucleotide: D287 (= D318), A288 (= A319), V319 (= V350), R348 (= R379), V350 (= V381), K351 (= K382), G352 (= G383), A353 (= A384), Y354 (= Y385), W355 (= W386), F373 (≠ Y404), T374 (= T405), R375 (= R406), K376 (= K407), T379 (= T410), A402 (= A434), T403 (= T435), H404 (= H436), N405 (= N437), Q428 (= Q456), C429 (≠ R457), Y454 (= Y482), E473 (= E501), S479 (= S507), F480 (= F508)
- binding nicotinamide-adenine-dinucleotide: I684 (= I723), S685 (= S724), P686 (= P725), W687 (= W726), N688 (= N727), I693 (= I732), K711 (= K750), A713 (= A752), E714 (= E753), G744 (= G783), G747 (= G787), A748 (= A788), T762 (= T802), G763 (= G803), S764 (= S804), V767 (≠ T807), I771 (= I811), E791 (= E828), T792 (= T829), C825 (= C862), E921 (= E959), F923 (= F961)
- binding (4R)-4-hydroxy-D-proline: E655 (= E680), F689 (= F728), S826 (= S863), G983 (= G1021), A984 (= A1022), F991 (= F1029)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 18:1011/1209 of 6x9cA
- active site: N687 (= N727), K710 (= K750), E790 (= E828), C824 (= C862), E920 (= E959), A1002 (= A1041)
- binding dihydroflavine-adenine dinucleotide: D286 (= D318), A287 (= A319), V318 (= V350), Q320 (= Q352), R347 (= R379), V349 (= V381), K350 (= K382), G351 (= G383), A352 (= A384), Y353 (= Y385), W354 (= W386), F372 (≠ Y404), T373 (= T405), R374 (= R406), K375 (= K407), T378 (= T410), A401 (= A434), T402 (= T435), H403 (= H436), N404 (= N437), Q427 (= Q456), C428 (≠ R457), E472 (= E501), S478 (= S507), F479 (= F508)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I723), S684 (= S724), P685 (= P725), W686 (= W726), N687 (= N727), K710 (= K750), E713 (= E753), G743 (= G783), G746 (= G787), A747 (= A788), F760 (= F801), G762 (= G803), S763 (= S804), V766 (≠ T807), E920 (= E959), F922 (= F961)
- binding proline: R823 (= R861), C824 (= C862), S825 (= S863), G982 (= G1021), A983 (= A1022), F990 (= F1029)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1015/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D318), A291 (= A319), V322 (= V350), Q324 (= Q352), R351 (= R379), V353 (= V381), K354 (= K382), G355 (= G383), A356 (= A384), Y357 (= Y385), W358 (= W386), F376 (≠ Y404), T377 (= T405), R378 (= R406), K379 (= K407), T382 (= T410), A405 (= A434), T406 (= T435), H407 (= H436), N408 (= N437), C432 (≠ R457), L433 (= L458), E476 (= E501), S482 (= S507), F483 (= F508)
- binding nicotinamide-adenine-dinucleotide: I687 (= I723), S688 (= S724), P689 (= P725), W690 (= W726), N691 (= N727), I696 (= I732), K714 (= K750), E717 (= E753), G747 (= G783), G750 (= G787), T765 (= T802), G766 (= G803), S767 (= S804), V770 (≠ T807), I774 (= I811), E794 (= E828), T795 (= T829), C828 (= C862), E924 (= E959), F926 (= F961), F994 (= F1029)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K277), Y457 (= Y482), Y469 (= Y494), R472 (= R497), R473 (= R498)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K277), D290 (= D318), Y457 (= Y482), Y469 (= Y494), R472 (= R497), R473 (= R498)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1015/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I723), S688 (= S724), P689 (= P725), W690 (= W726), N691 (= N727), I696 (= I732), K714 (= K750), A716 (= A752), E717 (= E753), G747 (= G783), G750 (= G787), A751 (= A788), T765 (= T802), G766 (= G803), S767 (= S804), V770 (≠ T807), E794 (= E828), T795 (= T829), C828 (= C862), E924 (= E959), F926 (= F961), F994 (= F1029)
- 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 (= D318), A291 (= A319), V322 (= V350), Q324 (= Q352), V353 (= V381), K354 (= K382), G355 (= G383), A356 (= A384), W358 (= W386), F376 (≠ Y404), T377 (= T405), R378 (= R406), K379 (= K407), T382 (= T410), A405 (= A434), T406 (= T435), H407 (= H436), N408 (= N437), Q431 (= Q456), C432 (≠ R457), L433 (= L458), Y457 (= Y482), E476 (= E501)
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
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1012/1214 of 6x9aA
- active site: N688 (= N727), K711 (= K750), E791 (= E828), C825 (= C862), E921 (= E959), A1003 (= A1041)
- binding flavin-adenine dinucleotide: D287 (= D318), A288 (= A319), V319 (= V350), R348 (= R379), V350 (= V381), K351 (= K382), G352 (= G383), A353 (= A384), Y354 (= Y385), W355 (= W386), F373 (≠ Y404), T374 (= T405), R375 (= R406), K376 (= K407), T379 (= T410), A402 (= A434), T403 (= T435), H404 (= H436), N405 (= N437), C429 (≠ R457), E473 (= E501), S479 (= S507), F480 (= F508)
- binding (4S)-4-hydroxy-D-proline: W555 (= W580), T556 (= T581), E655 (= E680), F689 (= F728), R725 (≠ Q764), S826 (= S863), G983 (= G1021), A984 (= A1022), F991 (= F1029)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1015/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I723), S688 (= S724), P689 (= P725), W690 (= W726), N691 (= N727), K714 (= K750), E717 (= E753), G747 (= G783), G750 (= G787), A751 (= A788), F764 (= F801), G766 (= G803), S767 (= S804), V770 (≠ T807), T795 (= T829), G796 (= G830), C828 (= C862), E924 (= E959), F926 (= F961)
- 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 (= K277), D290 (= D318), A291 (= A319), V322 (= V350), Q324 (= Q352), R351 (= R379), V353 (= V381), K354 (= K382), G355 (= G383), A356 (= A384), Y357 (= Y385), W358 (= W386), F376 (≠ Y404), T377 (= T405), R378 (= R406), K379 (= K407), T382 (= T410), A405 (= A434), T406 (= T435), H407 (= H436), N408 (= N437), Q431 (= Q456), C432 (≠ R457), L433 (= L458), Y457 (= Y482), S482 (= S507), F483 (= F508)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1014/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D318), A290 (= A319), V321 (= V350), Q323 (= Q352), R350 (= R379), V352 (= V381), K353 (= K382), G354 (= G383), A355 (= A384), Y356 (= Y385), W357 (= W386), F375 (≠ Y404), T376 (= T405), R377 (= R406), K378 (= K407), T381 (= T410), A404 (= A434), T405 (= T435), H406 (= H436), N407 (= N437), C431 (≠ R457), L432 (= L458), E475 (= E501), S481 (= S507), F482 (= F508)
- binding nicotinamide-adenine-dinucleotide: I686 (= I723), S687 (= S724), P688 (= P725), W689 (= W726), N690 (= N727), I695 (= I732), K713 (= K750), A715 (= A752), E716 (= E753), G746 (= G783), G749 (= G787), A750 (= A788), T764 (= T802), G765 (= G803), S766 (= S804), V769 (≠ T807), E793 (= E828), T794 (= T829), C827 (= C862), E923 (= E959), F925 (= F961), F993 (= F1029)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y482), Y468 (= Y494), R471 (= R497), R472 (= R498)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
53% identity, 94% coverage: 41:1050/1074 of query aligns to 19:1007/1207 of 5kf6A
- active site: N683 (= N727), K706 (= K750), E786 (= E828), C820 (= C862), E916 (= E959), A998 (= A1041)
- binding flavin-adenine dinucleotide: D282 (= D318), A283 (= A319), V314 (= V350), Q316 (= Q352), R343 (= R379), V345 (= V381), K346 (= K382), G347 (= G383), A348 (= A384), Y349 (= Y385), W350 (= W386), F368 (≠ Y404), T369 (= T405), R370 (= R406), K371 (= K407), T374 (= T410), A397 (= A434), T398 (= T435), H399 (= H436), N400 (= N437), Q423 (= Q456), C424 (≠ R457), L425 (= L458), E468 (= E501), S474 (= S507), F475 (= F508)
- binding nicotinamide-adenine-dinucleotide: I679 (= I723), S680 (= S724), P681 (= P725), W682 (= W726), N683 (= N727), I688 (= I732), K706 (= K750), A708 (= A752), E709 (= E753), G739 (= G783), G742 (= G787), A743 (= A788), F756 (= F801), T757 (= T802), G758 (= G803), S759 (= S804), V762 (≠ T807), I766 (= I811), E786 (= E828), T787 (= T829), C820 (= C862), E916 (= E959), F918 (= F961), F986 (= F1029)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K277), D282 (= D318), Y449 (= Y482), R464 (= R497), R465 (= R498)
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)
52% identity, 94% coverage: 41:1050/1074 of query aligns to 19:997/1197 of 6ufpA
- active site: N673 (= N727), K696 (= K750), E776 (= E828), C810 (= C862), E906 (= E959), A988 (= A1041)
- binding dihydroflavine-adenine dinucleotide: D285 (= D318), A286 (= A319), V317 (= V350), Q319 (= Q352), R346 (= R379), V348 (= V381), K349 (= K382), G350 (= G383), A351 (= A384), W353 (= W386), F371 (≠ Y404), T372 (= T405), R373 (= R406), K374 (= K407), T377 (= T410), A400 (= A434), T401 (= T435), H402 (= H436), N403 (= N437), Q426 (= Q456), C427 (≠ R457), L428 (= L458), S464 (= S507)
- binding nicotinamide-adenine-dinucleotide: I669 (= I723), P671 (= P725), W672 (= W726), N673 (= N727), I678 (= I732), K696 (= K750), E699 (= E753), G729 (= G783), G732 (= G787), F746 (= F801), T747 (= T802), G748 (= G803), S749 (= S804), V752 (≠ T807), E776 (= E828), T777 (= T829), C810 (= C862), E906 (= E959), F908 (= F961)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K277), D285 (= D318), Y439 (= Y482), Y451 (= Y494), R454 (= R497), R455 (= R498)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
53% identity, 47% coverage: 40:544/1074 of query aligns to 4:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K277), Y433 (= Y482), R448 (= R497), R449 (= R498)
- binding flavin-adenine dinucleotide: D263 (= D318), A264 (= A319), V295 (= V350), Q297 (= Q352), R324 (= R379), V326 (= V381), K327 (= K382), G328 (= G383), A329 (= A384), Y330 (= Y385), W331 (= W386), Y349 (= Y404), T350 (= T405), R351 (= R406), K352 (= K407), T355 (= T410), A378 (= A434), T379 (= T435), H380 (= H436), N381 (= N437), C405 (≠ R457), L406 (= L458), E452 (= E501), S458 (= S507)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
53% identity, 47% coverage: 40:544/1074 of query aligns to 4:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D318), A260 (= A319), V291 (= V350), Q293 (= Q352), R320 (= R379), V322 (= V381), K323 (= K382), G324 (= G383), A325 (= A384), Y326 (= Y385), W327 (= W386), Y345 (= Y404), T346 (= T405), R347 (= R406), K348 (= K407), T351 (= T410), A374 (= A434), T375 (= T435), H376 (= H436), N377 (= N437), C401 (≠ R457), L402 (= L458), E448 (= E501), S454 (= S507)
- binding cyclopropanecarboxylic acid: K218 (= K277), Y429 (= Y482), Y441 (= Y494), R444 (= R497), R445 (= R498)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
53% identity, 47% coverage: 40:544/1074 of query aligns to 4:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D318), A260 (= A319), V291 (= V350), Q293 (= Q352), R320 (= R379), V322 (= V381), K323 (= K382), G324 (= G383), A325 (= A384), Y326 (= Y385), W327 (= W386), Y345 (= Y404), T346 (= T405), R347 (= R406), K348 (= K407), T351 (= T410), A374 (= A434), T375 (= T435), H376 (= H436), N377 (= N437), C401 (≠ R457), L402 (= L458), E448 (= E501), S454 (= S507)
- binding cyclobutanecarboxylic acid: K218 (= K277), L402 (= L458), Y429 (= Y482), Y441 (= Y494), R444 (= R497), R445 (= R498)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
53% identity, 47% coverage: 40:544/1074 of query aligns to 4:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D318), A260 (= A319), V291 (= V350), Q293 (= Q352), R320 (= R379), V322 (= V381), K323 (= K382), G324 (= G383), A325 (= A384), Y326 (= Y385), W327 (= W386), Y345 (= Y404), T346 (= T405), R347 (= R406), K348 (= K407), T351 (= T410), A374 (= A434), T375 (= T435), H376 (= H436), N377 (= N437), C401 (≠ R457), L402 (= L458), E448 (= E501), S454 (= S507)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K277), Y326 (= Y385), Y429 (= Y482), Y441 (= Y494), R444 (= R497), R445 (= R498)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
52% identity, 47% coverage: 40:544/1074 of query aligns to 5:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A319), V283 (= V350), Q285 (= Q352), R312 (= R379), V314 (= V381), K315 (= K382), G316 (= G383), A317 (= A384), Y318 (= Y385), W319 (= W386), Y337 (= Y404), T338 (= T405), R339 (= R406), K340 (= K407), T343 (= T410), A366 (= A434), T367 (= T435), H368 (= H436), N369 (= N437), C393 (≠ R457), L394 (= L458), E440 (= E501), S446 (= S507), F447 (= F508)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K277), Y421 (= Y482), R436 (= R497), R437 (= R498)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
50% identity, 47% coverage: 40:544/1074 of query aligns to 4:466/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D318), A229 (= A319), V260 (= V350), Q262 (= Q352), V291 (= V381), K292 (= K382), G293 (= G383), A294 (= A384), Y295 (= Y385), W296 (= W386), Y314 (= Y404), T315 (= T405), R316 (= R406), K317 (= K407), T320 (= T410), A343 (= A434), T344 (= T435), H345 (= H436), N346 (= N437), C370 (≠ R457), L371 (= L458), E417 (= E501), S423 (= S507), F424 (= F508)
- binding proline: K187 (= K277), L371 (= L458), Y410 (= Y494), R413 (= R497), R414 (= R498)
3e2qA Crystal structure reduced puta86-630 mutant y540s complexed with trans-4-hydroxy-l-proline (see paper)
50% identity, 47% coverage: 40:544/1074 of query aligns to 4:466/468 of 3e2qA
- binding flavin-adenine dinucleotide: D228 (= D318), A229 (= A319), V260 (= V350), Q262 (= Q352), V291 (= V381), K292 (= K382), G293 (= G383), A294 (= A384), Y295 (= Y385), W296 (= W386), Y314 (= Y404), T315 (= T405), R316 (= R406), K317 (= K407), T320 (= T410), A343 (= A434), T344 (= T435), H345 (= H436), N346 (= N437), Q369 (= Q456), C370 (≠ R457), L371 (= L458), E417 (= E501), S423 (= S507), F424 (= F508)
- binding 4-hydroxyproline: D143 (= D233), K187 (= K277), D228 (= D318), Y410 (= Y494), R413 (= R497), R414 (= R498)
Query Sequence
>N515DRAFT_4232 N515DRAFT_4232 L-proline dehydrogenase /delta-1-pyrroline-5-carboxylate dehydrogenase
MRPFCHNTYNCGIPCASPAHRHPVTQPILSPELPTGAEPARARITAAWLRDETEAVNDLL
VQASLPPVEREKVIDLAADLVTRVRARAKDQSAVESFMRQYDLSSEEGVLLMCVAEALLR
IPDKATADKLIRDKLGDANWKKHLGQSESLFVNASTWGLMLTGKLVNLAGDIRHDFTGAL
RRLVGRAGEPAIRLAVRQAMRIMGHQFVMGRTIGEALDRCAQKEYAVYRYSYDMLGESAL
TSETAERYQQDYRNAIAAIGARGPFANHTDAPSISVKLSALHPRYEVAKRELARRDLTAK
LLELSQLAMKHGIALSVDAEEADRLELSLDILGDVFAHPSLAGWNGLGIVVQAYSKRTPF
VIDWLIETARGSGRRWYVRLVKGAYWDAEVKRAQENGLPGYPVYTRKPNTDVSYLACARK
LFDAGIELIYPQFATHNAHTIAAVHHLAKGRPYEYQRLHGMGTDLYAEVIGAQNLNVPCR
VYAPVGTHEDLLPYLVRRLLENGANTSFVNRVVDESLPVRELVADPCETVRSFASIPHPR
IPLPVNLYGELRKNSMGVNFSNDNELKALAETVNAKSGPWTATPLVPGATSAGATVQVTN
PADRRQVVGSYVSADSATVEKALANAVAAQHGWDRLPAASRAAILEHAAEQLEARRGEFI
ALCVREAGKGLPDAIAEIREAADFLRYYATMARRYFGQPEQLPGPTGESNQLFLNGRGVF
VCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTSLIGHAAVQLLHEAGVPADVLQYLP
GDGATVGAALTRDPRVAGVAFTGSTETAWAINRALAARNAPIAALIAETGGQNAMIADSS
ALPEQIVKDAVSSAFQSAGQRCSAARVLYVQEDIADKVCAMLAGAMAELKVGDPAQLSTD
VGPVIDEDARKILVDHAARMDQEAKKIGEVALDPATTGNGTFFAPRAYEIPGLATLTREI
FGPVLHVIRWKGSELDKVVDEINATGYGLTLGIHSRIDDTVEFIQSRARVGNCYVNRNQI
GAVVGVQPFGGEGLSGTGPKAGGPHYLFRFAGERTLTINTTAAGGNASLLTIGE
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