SitesBLAST
Comparing CCNA_00846 CCNA_00846 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)
51% identity, 98% coverage: 14:1021/1029 of query aligns to 15:983/983 of 3hazA
- active site: N652 (= N688), K675 (= K711), E752 (= E789), C786 (= C823), E878 (= E916), A960 (= A998)
- binding flavin-adenine dinucleotide: D272 (= D278), A273 (= A279), Q306 (= Q312), R333 (= R339), V335 (= V341), K336 (= K342), G337 (= G343), A338 (= A344), Y339 (= Y345), W340 (= W346), F358 (= F364), T359 (= T365), R360 (≠ T366), K361 (= K367), T364 (= T370), A387 (= A393), T388 (= T394), H389 (= H395), N390 (= N396), Y435 (= Y442), S460 (= S467), F461 (= F468)
- binding nicotinamide-adenine-dinucleotide: I648 (= I684), S649 (= S685), P650 (= P686), W651 (= W687), N652 (= N688), I657 (= I693), K675 (= K711), P676 (= P712), A677 (= A713), G708 (= G744), G711 (= G748), A712 (= A749), T726 (= T763), G727 (= G764), S728 (≠ G765), V731 (≠ T768), I735 (= I772), E752 (= E789), T753 (= T790), C786 (= C823), E878 (= E916), F880 (= F918), F948 (= F986)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
50% identity, 98% coverage: 14:1019/1029 of query aligns to 15:972/973 of 6bsnA
- active site: N643 (= N688), E743 (= E789), A777 (≠ C823), A951 (= A998)
- binding dihydroflavine-adenine dinucleotide: D269 (= D278), A270 (= A279), Q303 (= Q312), R330 (= R339), V332 (= V341), K333 (= K342), G334 (= G343), A335 (= A344), Y336 (= Y345), W337 (= W346), F355 (= F364), T356 (= T365), R357 (≠ T366), K358 (= K367), T361 (= T370), A384 (= A393), T385 (= T394), H386 (= H395), N387 (= N396), Y432 (= Y442), S457 (= S467), F458 (= F468)
- binding proline: M630 (≠ L675), W642 (= W687), F644 (= F689), G718 (= G764), R776 (= R822), S778 (= S824), F871 (= F918), I930 (≠ T977), G931 (= G978), A932 (= A979), F939 (= F986), A958 (≠ L1005), R959 (= R1006), A961 (= A1008)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1038/1218 of 6x9dA
- active site: N692 (= N688), K715 (= K711), E795 (= E789), C829 (= C823), E925 (= E916), A1007 (= A998)
- binding flavin-adenine dinucleotide: D291 (= D278), A292 (= A279), V323 (≠ A310), Q325 (= Q312), R352 (= R339), V354 (= V341), K355 (= K342), G356 (= G343), A357 (= A344), Y358 (= Y345), W359 (= W346), F377 (= F364), T378 (= T365), R379 (≠ T366), K380 (= K367), T383 (= T370), A406 (= A393), T407 (= T394), H408 (= H395), N409 (= N396), Q432 (= Q417), C433 (≠ R418), E477 (= E461), S483 (= S467), F484 (= F468)
- binding 4-hydroxyproline: E659 (= E641), F693 (= F689), I697 (= I693), R828 (= R822), S830 (= S824), G987 (= G978), A988 (= A979), F995 (= F986)
- binding nicotinamide-adenine-dinucleotide: I688 (= I684), S689 (= S685), P690 (= P686), W691 (= W687), N692 (= N688), I697 (= I693), K715 (= K711), A717 (= A713), E718 (= E714), G748 (= G744), G751 (= G748), A752 (= A749), T766 (= T763), G767 (= G764), S768 (≠ G765), V771 (≠ T768), E795 (= E789), T796 (= T790), C829 (= C823), E925 (= E916), F927 (= F918), F995 (= F986)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1036/1216 of 6x99A
- active site: N690 (= N688), K713 (= K711), E793 (= E789), C827 (= C823), E923 (= E916), A1005 (= A998)
- binding d-proline: W557 (≠ L540), T558 (≠ S541), E657 (= E641), F691 (= F689), R727 (≠ K725), R826 (= R822), S828 (= S824), G985 (= G978), A986 (= A979), F993 (= F986)
- binding flavin-adenine dinucleotide: D289 (= D278), A290 (= A279), V321 (≠ A310), R350 (= R339), V352 (= V341), K353 (= K342), G354 (= G343), A355 (= A344), Y356 (= Y345), W357 (= W346), F375 (= F364), T376 (= T365), R377 (≠ T366), K378 (= K367), T381 (= T370), A404 (= A393), T405 (= T394), H406 (= H395), N407 (= N396), Q430 (= Q417), C431 (≠ R418), Y456 (= Y442), E475 (= E461), S481 (= S467), F482 (= F468)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1034/1214 of 6x9aA
- active site: N688 (= N688), K711 (= K711), E791 (= E789), C825 (= C823), E921 (= E916), A1003 (= A998)
- binding flavin-adenine dinucleotide: D287 (= D278), A288 (= A279), V319 (≠ A310), R348 (= R339), V350 (= V341), K351 (= K342), G352 (= G343), A353 (= A344), Y354 (= Y345), W355 (= W346), F373 (= F364), T374 (= T365), R375 (≠ T366), K376 (= K367), T379 (= T370), A402 (= A393), T403 (= T394), H404 (= H395), N405 (= N396), C429 (≠ R418), E473 (= E461), S479 (= S467), F480 (= F468)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ L540), T556 (≠ S541), E655 (= E641), F689 (= F689), R725 (≠ K725), S826 (= S824), G983 (= G978), A984 (= A979), F991 (= F986)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1037/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D278), A291 (= A279), V322 (≠ A310), Q324 (= Q312), R351 (= R339), V353 (= V341), K354 (= K342), G355 (= G343), A356 (= A344), Y357 (= Y345), W358 (= W346), F376 (= F364), T377 (= T365), R378 (≠ T366), K379 (= K367), T382 (= T370), A405 (= A393), T406 (= T394), H407 (= H395), N408 (= N396), C432 (≠ R418), L433 (= L419), E476 (= E461), S482 (= S467), F483 (= F468)
- binding nicotinamide-adenine-dinucleotide: I687 (= I684), S688 (= S685), P689 (= P686), W690 (= W687), N691 (= N688), I696 (= I693), K714 (= K711), E717 (= E714), G747 (= G744), G750 (= G748), T765 (= T763), G766 (= G764), S767 (≠ G765), V770 (≠ T768), I774 (= I772), E794 (= E789), T795 (= T790), C828 (= C823), E924 (= E916), F926 (= F918), F994 (= F986)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K237), Y457 (= Y442), Y469 (= Y454), R472 (= R457), R473 (= R458)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K237), D290 (= D278), Y457 (= Y442), Y469 (= Y454), R472 (= R457), R473 (= R458)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1037/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I684), S688 (= S685), P689 (= P686), W690 (= W687), N691 (= N688), I696 (= I693), K714 (= K711), A716 (= A713), E717 (= E714), G747 (= G744), G750 (= G748), A751 (= A749), T765 (= T763), G766 (= G764), S767 (≠ G765), V770 (≠ T768), E794 (= E789), T795 (= T790), C828 (= C823), E924 (= E916), F926 (= F918), F994 (= F986)
- 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 (= D278), A291 (= A279), V322 (≠ A310), Q324 (= Q312), V353 (= V341), K354 (= K342), G355 (= G343), A356 (= A344), W358 (= W346), F376 (= F364), T377 (= T365), R378 (≠ T366), K379 (= K367), T382 (= T370), A405 (= A393), T406 (= T394), H407 (= H395), N408 (= N396), Q431 (= Q417), C432 (≠ R418), L433 (= L419), Y457 (= Y442), E476 (= E461)
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
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1037/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I684), S688 (= S685), P689 (= P686), W690 (= W687), N691 (= N688), K714 (= K711), E717 (= E714), G747 (= G744), G750 (= G748), A751 (= A749), F764 (= F762), G766 (= G764), S767 (≠ G765), V770 (≠ T768), T795 (= T790), G796 (= G791), C828 (= C823), E924 (= E916), F926 (= F918)
- 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 (= K237), D290 (= D278), A291 (= A279), V322 (≠ A310), Q324 (= Q312), R351 (= R339), V353 (= V341), K354 (= K342), G355 (= G343), A356 (= A344), Y357 (= Y345), W358 (= W346), F376 (= F364), T377 (= T365), R378 (≠ T366), K379 (= K367), T382 (= T370), A405 (= A393), T406 (= T394), H407 (= H395), N408 (= N396), Q431 (= Q417), C432 (≠ R418), L433 (= L419), Y457 (= Y442), S482 (= S467), F483 (= F468)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1034/1214 of 6x9bA
- active site: N688 (= N688), K711 (= K711), E791 (= E789), C825 (= C823), E921 (= E916), A1003 (= A998)
- binding flavin-adenine dinucleotide: D287 (= D278), A288 (= A279), V319 (≠ A310), R348 (= R339), V350 (= V341), K351 (= K342), G352 (= G343), A353 (= A344), Y354 (= Y345), W355 (= W346), F373 (= F364), T374 (= T365), R375 (≠ T366), K376 (= K367), T379 (= T370), A402 (= A393), T403 (= T394), H404 (= H395), N405 (= N396), Q428 (= Q417), C429 (≠ R418), Y454 (= Y442), E473 (= E461), S479 (= S467), F480 (= F468)
- binding nicotinamide-adenine-dinucleotide: I684 (= I684), S685 (= S685), P686 (= P686), W687 (= W687), N688 (= N688), I693 (= I693), K711 (= K711), A713 (= A713), E714 (= E714), G744 (= G744), G747 (= G748), A748 (= A749), T762 (= T763), G763 (= G764), S764 (≠ G765), V767 (≠ T768), I771 (= I772), E791 (= E789), T792 (= T790), C825 (= C823), E921 (= E916), F923 (= F918)
- binding (4R)-4-hydroxy-D-proline: E655 (= E641), F689 (= F689), S826 (= S824), G983 (= G978), A984 (= A979), F991 (= F986)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 20:1033/1209 of 6x9cA
- active site: N687 (= N688), K710 (= K711), E790 (= E789), C824 (= C823), E920 (= E916), A1002 (= A998)
- binding dihydroflavine-adenine dinucleotide: D286 (= D278), A287 (= A279), V318 (≠ A310), Q320 (= Q312), R347 (= R339), V349 (= V341), K350 (= K342), G351 (= G343), A352 (= A344), Y353 (= Y345), W354 (= W346), F372 (= F364), T373 (= T365), R374 (≠ T366), K375 (= K367), T378 (= T370), A401 (= A393), T402 (= T394), H403 (= H395), N404 (= N396), Q427 (= Q417), C428 (≠ R418), E472 (= E461), S478 (= S467), F479 (= F468)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I684), S684 (= S685), P685 (= P686), W686 (= W687), N687 (= N688), K710 (= K711), E713 (= E714), G743 (= G744), G746 (= G748), A747 (= A749), F760 (= F762), G762 (= G764), S763 (≠ G765), V766 (≠ T768), E920 (= E916), F922 (= F918)
- binding proline: R823 (= R822), C824 (= C823), S825 (= S824), G982 (= G978), A983 (= A979), F990 (= F986)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1036/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D278), A290 (= A279), V321 (≠ A310), Q323 (= Q312), R350 (= R339), V352 (= V341), K353 (= K342), G354 (= G343), A355 (= A344), Y356 (= Y345), W357 (= W346), F375 (= F364), T376 (= T365), R377 (≠ T366), K378 (= K367), T381 (= T370), A404 (= A393), T405 (= T394), H406 (= H395), N407 (= N396), C431 (≠ R418), L432 (= L419), E475 (= E461), S481 (= S467), F482 (= F468)
- binding nicotinamide-adenine-dinucleotide: I686 (= I684), S687 (= S685), P688 (= P686), W689 (= W687), N690 (= N688), I695 (= I693), K713 (= K711), A715 (= A713), E716 (= E714), G746 (= G744), G749 (= G748), A750 (= A749), T764 (= T763), G765 (= G764), S766 (≠ G765), V769 (≠ T768), E793 (= E789), T794 (= T790), C827 (= C823), E923 (= E916), F925 (= F918), F993 (= F986)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y442), Y468 (= Y454), R471 (= R457), R472 (= R458)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1029/1207 of 5kf6A
- active site: N683 (= N688), K706 (= K711), E786 (= E789), C820 (= C823), E916 (= E916), A998 (= A998)
- binding flavin-adenine dinucleotide: D282 (= D278), A283 (= A279), V314 (≠ A310), Q316 (= Q312), R343 (= R339), V345 (= V341), K346 (= K342), G347 (= G343), A348 (= A344), Y349 (= Y345), W350 (= W346), F368 (= F364), T369 (= T365), R370 (≠ T366), K371 (= K367), T374 (= T370), A397 (= A393), T398 (= T394), H399 (= H395), N400 (= N396), Q423 (= Q417), C424 (≠ R418), L425 (= L419), E468 (= E461), S474 (= S467), F475 (= F468)
- binding nicotinamide-adenine-dinucleotide: I679 (= I684), S680 (= S685), P681 (= P686), W682 (= W687), N683 (= N688), I688 (= I693), K706 (= K711), A708 (= A713), E709 (= E714), G739 (= G744), G742 (= G748), A743 (= A749), F756 (= F762), T757 (= T763), G758 (= G764), S759 (≠ G765), V762 (≠ T768), I766 (= I772), E786 (= E789), T787 (= T790), C820 (= C823), E916 (= E916), F918 (= F918), F986 (= F986)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K237), D282 (= D278), Y449 (= Y442), R464 (= R457), R465 (= R458)
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)
47% identity, 100% coverage: 6:1029/1029 of query aligns to 21:1019/1197 of 6ufpA
- active site: N673 (= N688), K696 (= K711), E776 (= E789), C810 (= C823), E906 (= E916), A988 (= A998)
- binding dihydroflavine-adenine dinucleotide: D285 (= D278), A286 (= A279), V317 (≠ A310), Q319 (= Q312), R346 (= R339), V348 (= V341), K349 (= K342), G350 (= G343), A351 (= A344), W353 (= W346), F371 (= F364), T372 (= T365), R373 (≠ T366), K374 (= K367), T377 (= T370), A400 (= A393), T401 (= T394), H402 (= H395), N403 (= N396), Q426 (= Q417), C427 (≠ R418), L428 (= L419), S464 (= S467)
- binding nicotinamide-adenine-dinucleotide: I669 (= I684), P671 (= P686), W672 (= W687), N673 (= N688), I678 (= I693), K696 (= K711), E699 (= E714), G729 (= G744), G732 (= G748), F746 (= F762), T747 (= T763), G748 (= G764), S749 (≠ G765), V752 (≠ T768), E776 (= E789), T777 (= T790), C810 (= C823), E906 (= E916), F908 (= F918)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K237), D285 (= D278), Y439 (= Y442), Y451 (= Y454), R454 (= R457), R455 (= R458)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
49% identity, 45% coverage: 44:503/1029 of query aligns to 48:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K237), Y433 (= Y442), R448 (= R457), R449 (= R458)
- binding flavin-adenine dinucleotide: D263 (= D278), A264 (= A279), V295 (≠ A310), Q297 (= Q312), R324 (= R339), V326 (= V341), K327 (= K342), G328 (= G343), A329 (= A344), Y330 (= Y345), W331 (= W346), Y349 (≠ F364), T350 (= T365), R351 (≠ T366), K352 (= K367), T355 (= T370), A378 (= A393), T379 (= T394), H380 (= H395), N381 (= N396), C405 (≠ R418), L406 (= L419), E452 (= E461), S458 (= S467)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
49% identity, 45% coverage: 44:503/1029 of query aligns to 48:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D278), A260 (= A279), V291 (≠ A310), Q293 (= Q312), R320 (= R339), V322 (= V341), K323 (= K342), G324 (= G343), A325 (= A344), Y326 (= Y345), W327 (= W346), Y345 (≠ F364), T346 (= T365), R347 (≠ T366), K348 (= K367), T351 (= T370), A374 (= A393), T375 (= T394), H376 (= H395), N377 (= N396), C401 (≠ R418), L402 (= L419), E448 (= E461), S454 (= S467)
- binding cyclopropanecarboxylic acid: K218 (= K237), Y429 (= Y442), Y441 (= Y454), R444 (= R457), R445 (= R458)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
49% identity, 45% coverage: 44:503/1029 of query aligns to 48:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D278), A260 (= A279), V291 (≠ A310), Q293 (= Q312), R320 (= R339), V322 (= V341), K323 (= K342), G324 (= G343), A325 (= A344), Y326 (= Y345), W327 (= W346), Y345 (≠ F364), T346 (= T365), R347 (≠ T366), K348 (= K367), T351 (= T370), A374 (= A393), T375 (= T394), H376 (= H395), N377 (= N396), C401 (≠ R418), L402 (= L419), E448 (= E461), S454 (= S467)
- binding cyclobutanecarboxylic acid: K218 (= K237), L402 (= L419), Y429 (= Y442), Y441 (= Y454), R444 (= R457), R445 (= R458)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
49% identity, 45% coverage: 44:503/1029 of query aligns to 48:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D278), A260 (= A279), V291 (≠ A310), Q293 (= Q312), R320 (= R339), V322 (= V341), K323 (= K342), G324 (= G343), A325 (= A344), Y326 (= Y345), W327 (= W346), Y345 (≠ F364), T346 (= T365), R347 (≠ T366), K348 (= K367), T351 (= T370), A374 (= A393), T375 (= T394), H376 (= H395), N377 (= N396), C401 (≠ R418), L402 (= L419), E448 (= E461), S454 (= S467)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K237), Y326 (= Y345), Y429 (= Y442), Y441 (= Y454), R444 (= R457), R445 (= R458)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
48% identity, 45% coverage: 44:503/1029 of query aligns to 49:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A279), V283 (≠ A310), Q285 (= Q312), R312 (= R339), V314 (= V341), K315 (= K342), G316 (= G343), A317 (= A344), Y318 (= Y345), W319 (= W346), Y337 (≠ F364), T338 (= T365), R339 (≠ T366), K340 (= K367), T343 (= T370), A366 (= A393), T367 (= T394), H368 (= H395), N369 (= N396), C393 (≠ R418), L394 (= L419), E440 (= E461), S446 (= S467), F447 (= F468)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K237), Y421 (= Y442), R436 (= R457), R437 (= R458)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
31% identity, 86% coverage: 145:1025/1029 of query aligns to 68:958/959 of 5ur2B
- active site: N618 (= N688), K641 (= K711), E722 (= E789), C756 (= C823), E851 (= E916), T931 (≠ A998)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K237), D215 (= D278), M216 (≠ A279), Q249 (= Q312), V278 (= V341), K279 (= K342), G280 (= G343), A281 (= A344), W283 (= W346), Y300 (≠ F364), T301 (= T365), N302 (≠ T366), K303 (= K367), S306 (≠ T370), A329 (= A393), S330 (≠ T394), H331 (= H395), N332 (= N396), Q356 (= Q417), M357 (≠ R418), L358 (= L419), Y379 (= Y442), E398 (= E461), E403 (≠ T466), W405 (≠ F468)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
46% identity, 45% coverage: 44:503/1029 of query aligns to 48:466/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D278), A229 (= A279), V260 (≠ A310), Q262 (= Q312), V291 (= V341), K292 (= K342), G293 (= G343), A294 (= A344), Y295 (= Y345), W296 (= W346), Y314 (≠ F364), T315 (= T365), R316 (≠ T366), K317 (= K367), T320 (= T370), A343 (= A393), T344 (= T394), H345 (= H395), N346 (= N396), C370 (≠ R418), L371 (= L419), E417 (= E461), S423 (= S467), F424 (= F468)
- binding proline: K187 (= K237), L371 (= L419), Y410 (= Y454), R413 (= R457), R414 (= R458)
Query Sequence
>CCNA_00846 CCNA_00846 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase
MTDWDSLDAGKYRDEAAVIADLLAAKPLSSEDRAAVRAEAEALVRGARRSVRKQGVVESF
LQEFSLGTREGLALMCLAEALLRTPDDDTRDKLIAEKIGSADWASHLGGSDSLFVNASTW
GLMLTGKIVEPDETARNDMPGFIKKLAGRLGEPVIRAAVGQAIRIMGEQFVLGRTIEAAI
KRAAAEGDMCSFDMLGEGARTAADAARYEKAYADAIETVGKLSNGAGPEAGHGVSVKLSA
LCPRYEATHEDRVWEELYPRTLRLAKIAARHNLNFTIDAEEADRLALSLKLLDKLCREPE
LGDWTGLGLAVQAYQKRCGEVIARLKALSEETGRRLMVRLVKGAYWDSEIKRAQVAGRPD
YPVFTTKPATDLSYLVNAKALIEAAPHLYAQFATHNAHTLAAVVRMAKNTGVKIEHQRLH
GMGEALYKAADDLYDGITLRAYAPVGGHEDLLPYLVRRLLENGANTSFVHALLDERVPVE
KVVTDPIDTVEAHPDRHAKIPTPINVYGERRVNSAGLDLSVKADRERLSAAVAAQDGVTL
SAGPLVGGKVVAGGAPLPLIAPANDQKTVGVVSEAQSAQIDEAFKLARAAQPAWDRAGGV
ARAQVLRAMGDALEANIERLIALLSREAGKTLSDGIAEVREAVDFCRYYAMLAEDQFGEA
EILKGPVGETNSLRLAGRGVFVCISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIA
FEAVKLYHAAGLDPRLLALLPGRGETVGAALTSHEDLDGVAFTGGTDTAWRINQTLAARQ
GPIVPFIAETGGLNGMFVDTTAQREQVIDDVIVSAFGSAGQRCSALRLLFLPHDTADHII
EGLKGAMDALVLGDPALAVTDVGPVIDAEAKDALDKHLVRLKSDAKVLHALAAPAGGTFF
APVLAEIPTADFLEREVFGPVLHVVRYKPENLEKVAGALAARRYGLTLGIHSRIESFAAD
VQRLVPAGNAYVNRSMTGAVVGVQPFGGEGLSGTGPKAGGPHALLRFAVERALSVNITAQ
GGDPALLNL
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