SitesBLAST
Comparing WP_011384888.1 AMB_RS12610 bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA 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)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
52% identity, 98% coverage: 3:1024/1039 of query aligns to 8:983/983 of 3hazA
- active site: N652 (= N689), K675 (= K712), E752 (= E789), C786 (= C823), E878 (= E919), A960 (= A1001)
- binding flavin-adenine dinucleotide: D272 (= D286), A273 (= A287), Q306 (= Q320), R333 (= R347), V335 (= V349), K336 (= K350), G337 (= G351), A338 (= A352), Y339 (= Y353), W340 (= W354), F358 (= F372), T359 (= T373), R360 (≠ T374), K361 (= K375), T364 (= T378), A387 (= A401), T388 (= T402), H389 (= H403), N390 (= N404), Y435 (= Y446), S460 (= S471), F461 (= F472)
- binding nicotinamide-adenine-dinucleotide: I648 (= I685), S649 (= S686), P650 (= P687), W651 (= W688), N652 (= N689), I657 (= I694), K675 (= K712), P676 (= P713), A677 (= A714), G708 (≠ P745), G711 (= G748), A712 (≠ E749), T726 (= T763), G727 (= G764), S728 (= S765), V731 (≠ T768), I735 (= I772), E752 (= E789), T753 (= T790), C786 (= C823), E878 (= E919), F880 (= F921), F948 (= F989)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
51% identity, 98% coverage: 3:1023/1039 of query aligns to 8:973/973 of 6bsnA
- active site: N643 (= N689), E743 (= E789), A777 (≠ C823), A951 (= A1001)
- binding dihydroflavine-adenine dinucleotide: D269 (= D286), A270 (= A287), Q303 (= Q320), R330 (= R347), V332 (= V349), K333 (= K350), G334 (= G351), A335 (= A352), Y336 (= Y353), W337 (= W354), F355 (= F372), T356 (= T373), R357 (≠ T374), K358 (= K375), T361 (= T378), A384 (= A401), T385 (= T402), H386 (= H403), N387 (= N404), Y432 (= Y446), S457 (= S471), F458 (= F472)
- binding proline: M630 (≠ L676), W642 (= W688), F644 (= F690), G718 (= G764), R776 (= R822), S778 (= S824), F871 (= F921), I930 (= I980), G931 (= G981), A932 (= A982), F939 (= F989), A958 (≠ I1008), R959 (= R1009), A961 (≠ G1011)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1015/1218 of 6x9dA
- active site: N692 (= N689), K715 (= K712), E795 (= E789), C829 (= C823), E925 (= E919), A1007 (= A1001)
- binding flavin-adenine dinucleotide: D291 (= D286), A292 (= A287), V323 (≠ A318), Q325 (= Q320), R352 (= R347), V354 (= V349), K355 (= K350), G356 (= G351), A357 (= A352), Y358 (= Y353), W359 (= W354), F377 (= F372), T378 (= T373), R379 (≠ T374), K380 (= K375), T383 (= T378), A406 (= A401), T407 (= T402), H408 (= H403), N409 (= N404), Q432 (= Q424), C433 (≠ R425), E477 (= E465), S483 (= S471), F484 (= F472)
- binding 4-hydroxyproline: E659 (= E642), F693 (= F690), I697 (= I694), R828 (= R822), S830 (= S824), G987 (= G981), A988 (= A982), F995 (= F989)
- binding nicotinamide-adenine-dinucleotide: I688 (= I685), S689 (= S686), P690 (= P687), W691 (= W688), N692 (= N689), I697 (= I694), K715 (= K712), A717 (= A714), E718 (≠ P715), G748 (≠ P745), G751 (= G748), A752 (≠ E749), T766 (= T763), G767 (= G764), S768 (= S765), V771 (≠ T768), E795 (= E789), T796 (= T790), C829 (= C823), E925 (= E919), F927 (= F921), F995 (= F989)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1014/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D286), A291 (= A287), V322 (≠ A318), Q324 (= Q320), R351 (= R347), V353 (= V349), K354 (= K350), G355 (= G351), A356 (= A352), Y357 (= Y353), W358 (= W354), F376 (= F372), T377 (= T373), R378 (≠ T374), K379 (= K375), T382 (= T378), A405 (= A401), T406 (= T402), H407 (= H403), N408 (= N404), C432 (≠ R425), L433 (= L426), E476 (= E465), S482 (= S471), F483 (= F472)
- binding nicotinamide-adenine-dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), I696 (= I694), K714 (= K712), E717 (≠ P715), G747 (≠ P745), G750 (= G748), T765 (= T763), G766 (= G764), S767 (= S765), V770 (≠ T768), I774 (= I772), E794 (= E789), T795 (= T790), C828 (= C823), E924 (= E919), F926 (= F921), F994 (= F989)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K245), Y457 (= Y446), Y469 (= Y458), R472 (= R461), R473 (= R462)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K245), D290 (= D286), Y457 (= Y446), Y469 (= Y458), R472 (= R461), R473 (= R462)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1014/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), I696 (= I694), K714 (= K712), A716 (= A714), E717 (≠ P715), G747 (≠ P745), G750 (= G748), A751 (≠ E749), T765 (= T763), G766 (= G764), S767 (= S765), V770 (≠ T768), E794 (= E789), T795 (= T790), C828 (= C823), E924 (= E919), F926 (= F921), F994 (= F989)
- 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 (= D286), A291 (= A287), V322 (≠ A318), Q324 (= Q320), V353 (= V349), K354 (= K350), G355 (= G351), A356 (= A352), W358 (= W354), F376 (= F372), T377 (= T373), R378 (≠ T374), K379 (= K375), T382 (= T378), A405 (= A401), T406 (= T402), H407 (= H403), N408 (= N404), Q431 (= Q424), C432 (≠ R425), L433 (= L426), Y457 (= Y446), E476 (= E465)
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)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1014/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), K714 (= K712), E717 (≠ P715), G747 (≠ P745), G750 (= G748), A751 (≠ E749), F764 (= F762), G766 (= G764), S767 (= S765), V770 (≠ T768), T795 (= T790), G796 (= G791), C828 (= C823), E924 (= E919), F926 (= F921)
- 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 (= K245), D290 (= D286), A291 (= A287), V322 (≠ A318), Q324 (= Q320), R351 (= R347), V353 (= V349), K354 (= K350), G355 (= G351), A356 (= A352), Y357 (= Y353), W358 (= W354), F376 (= F372), T377 (= T373), R378 (≠ T374), K379 (= K375), T382 (= T378), A405 (= A401), T406 (= T402), H407 (= H403), N408 (= N404), Q431 (= Q424), C432 (≠ R425), L433 (= L426), Y457 (= Y446), S482 (= S471), F483 (= F472)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1011/1214 of 6x9aA
- active site: N688 (= N689), K711 (= K712), E791 (= E789), C825 (= C823), E921 (= E919), A1003 (= A1001)
- binding flavin-adenine dinucleotide: D287 (= D286), A288 (= A287), V319 (≠ A318), R348 (= R347), V350 (= V349), K351 (= K350), G352 (= G351), A353 (= A352), Y354 (= Y353), W355 (= W354), F373 (= F372), T374 (= T373), R375 (≠ T374), K376 (= K375), T379 (= T378), A402 (= A401), T403 (= T402), H404 (= H403), N405 (= N404), C429 (≠ R425), E473 (= E465), S479 (= S471), F480 (= F472)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ R542), T556 (≠ S543), E655 (= E642), F689 (= F690), R725 (= R726), S826 (= S824), G983 (= G981), A984 (= A982), F991 (= F989)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1013/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D286), A290 (= A287), V321 (≠ A318), Q323 (= Q320), R350 (= R347), V352 (= V349), K353 (= K350), G354 (= G351), A355 (= A352), Y356 (= Y353), W357 (= W354), F375 (= F372), T376 (= T373), R377 (≠ T374), K378 (= K375), T381 (= T378), A404 (= A401), T405 (= T402), H406 (= H403), N407 (= N404), C431 (≠ R425), L432 (= L426), E475 (= E465), S481 (= S471), F482 (= F472)
- binding nicotinamide-adenine-dinucleotide: I686 (= I685), S687 (= S686), P688 (= P687), W689 (= W688), N690 (= N689), I695 (= I694), K713 (= K712), A715 (= A714), E716 (≠ P715), G746 (≠ P745), G749 (= G748), A750 (≠ E749), T764 (= T763), G765 (= G764), S766 (= S765), V769 (≠ T768), E793 (= E789), T794 (= T790), C827 (= C823), E923 (= E919), F925 (= F921), F993 (= F989)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y446), Y468 (= Y458), R471 (= R461), R472 (= R462)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1013/1216 of 6x99A
- active site: N690 (= N689), K713 (= K712), E793 (= E789), C827 (= C823), E923 (= E919), A1005 (= A1001)
- binding d-proline: W557 (≠ R542), T558 (≠ S543), E657 (= E642), F691 (= F690), R727 (= R726), R826 (= R822), S828 (= S824), G985 (= G981), A986 (= A982), F993 (= F989)
- binding flavin-adenine dinucleotide: D289 (= D286), A290 (= A287), V321 (≠ A318), R350 (= R347), V352 (= V349), K353 (= K350), G354 (= G351), A355 (= A352), Y356 (= Y353), W357 (= W354), F375 (= F372), T376 (= T373), R377 (≠ T374), K378 (= K375), T381 (= T378), A404 (= A401), T405 (= T402), H406 (= H403), N407 (= N404), Q430 (= Q424), C431 (≠ R425), Y456 (= Y446), E475 (= E465), S481 (= S471), F482 (= F472)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1011/1214 of 6x9bA
- active site: N688 (= N689), K711 (= K712), E791 (= E789), C825 (= C823), E921 (= E919), A1003 (= A1001)
- binding flavin-adenine dinucleotide: D287 (= D286), A288 (= A287), V319 (≠ A318), R348 (= R347), V350 (= V349), K351 (= K350), G352 (= G351), A353 (= A352), Y354 (= Y353), W355 (= W354), F373 (= F372), T374 (= T373), R375 (≠ T374), K376 (= K375), T379 (= T378), A402 (= A401), T403 (= T402), H404 (= H403), N405 (= N404), Q428 (= Q424), C429 (≠ R425), Y454 (= Y446), E473 (= E465), S479 (= S471), F480 (= F472)
- binding nicotinamide-adenine-dinucleotide: I684 (= I685), S685 (= S686), P686 (= P687), W687 (= W688), N688 (= N689), I693 (= I694), K711 (= K712), A713 (= A714), E714 (≠ P715), G744 (≠ P745), G747 (= G748), A748 (≠ E749), T762 (= T763), G763 (= G764), S764 (= S765), V767 (≠ T768), I771 (= I772), E791 (= E789), T792 (= T790), C825 (= C823), E921 (= E919), F923 (= F921)
- binding (4R)-4-hydroxy-D-proline: E655 (= E642), F689 (= F690), S826 (= S824), G983 (= G981), A984 (= A982), F991 (= F989)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 7:1010/1209 of 6x9cA
- active site: N687 (= N689), K710 (= K712), E790 (= E789), C824 (= C823), E920 (= E919), A1002 (= A1001)
- binding dihydroflavine-adenine dinucleotide: D286 (= D286), A287 (= A287), V318 (≠ A318), Q320 (= Q320), R347 (= R347), V349 (= V349), K350 (= K350), G351 (= G351), A352 (= A352), Y353 (= Y353), W354 (= W354), F372 (= F372), T373 (= T373), R374 (≠ T374), K375 (= K375), T378 (= T378), A401 (= A401), T402 (= T402), H403 (= H403), N404 (= N404), Q427 (= Q424), C428 (≠ R425), E472 (= E465), S478 (= S471), F479 (= F472)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I685), S684 (= S686), P685 (= P687), W686 (= W688), N687 (= N689), K710 (= K712), E713 (≠ P715), G743 (≠ P745), G746 (= G748), A747 (≠ E749), F760 (= F762), G762 (= G764), S763 (= S765), V766 (≠ T768), E920 (= E919), F922 (= F921)
- binding proline: R823 (= R822), C824 (= C823), S825 (= S824), G982 (= G981), A983 (= A982), F990 (= F989)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:1006/1207 of 5kf6A
- active site: N683 (= N689), K706 (= K712), E786 (= E789), C820 (= C823), E916 (= E919), A998 (= A1001)
- binding flavin-adenine dinucleotide: D282 (= D286), A283 (= A287), V314 (≠ A318), Q316 (= Q320), R343 (= R347), V345 (= V349), K346 (= K350), G347 (= G351), A348 (= A352), Y349 (= Y353), W350 (= W354), F368 (= F372), T369 (= T373), R370 (≠ T374), K371 (= K375), T374 (= T378), A397 (= A401), T398 (= T402), H399 (= H403), N400 (= N404), Q423 (= Q424), C424 (≠ R425), L425 (= L426), E468 (= E465), S474 (= S471), F475 (= F472)
- binding nicotinamide-adenine-dinucleotide: I679 (= I685), S680 (= S686), P681 (= P687), W682 (= W688), N683 (= N689), I688 (= I694), K706 (= K712), A708 (= A714), E709 (≠ P715), G739 (≠ P745), G742 (= G748), A743 (≠ E749), F756 (= F762), T757 (= T763), G758 (= G764), S759 (= S765), V762 (≠ T768), I766 (= I772), E786 (= E789), T787 (= T790), C820 (= C823), E916 (= E919), F918 (= F921), F986 (= F989)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K245), D282 (= D286), Y449 (= Y446), R464 (= R461), R465 (= R462)
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)
49% identity, 97% coverage: 3:1009/1039 of query aligns to 8:996/1197 of 6ufpA
- active site: N673 (= N689), K696 (= K712), E776 (= E789), C810 (= C823), E906 (= E919), A988 (= A1001)
- binding dihydroflavine-adenine dinucleotide: D285 (= D286), A286 (= A287), V317 (≠ A318), Q319 (= Q320), R346 (= R347), V348 (= V349), K349 (= K350), G350 (= G351), A351 (= A352), W353 (= W354), F371 (= F372), T372 (= T373), R373 (≠ T374), K374 (= K375), T377 (= T378), A400 (= A401), T401 (= T402), H402 (= H403), N403 (= N404), Q426 (= Q424), C427 (≠ R425), L428 (= L426), S464 (= S471)
- binding nicotinamide-adenine-dinucleotide: I669 (= I685), P671 (= P687), W672 (= W688), N673 (= N689), I678 (= I694), K696 (= K712), E699 (≠ P715), G729 (≠ P745), G732 (= G748), F746 (= F762), T747 (= T763), G748 (= G764), S749 (= S765), V752 (≠ T768), E776 (= E789), T777 (= T790), C810 (= C823), E906 (= E919), F908 (= F921)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K245), D285 (= D286), Y439 (= Y446), Y451 (= Y458), R454 (= R461), R455 (= R462)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
50% identity, 47% coverage: 15:500/1039 of query aligns to 1:487/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K245), Y433 (= Y446), R448 (= R461), R449 (= R462)
- binding flavin-adenine dinucleotide: D263 (= D286), A264 (= A287), V295 (≠ A318), Q297 (= Q320), R324 (= R347), V326 (= V349), K327 (= K350), G328 (= G351), A329 (= A352), Y330 (= Y353), W331 (= W354), Y349 (≠ F372), T350 (= T373), R351 (≠ T374), K352 (= K375), T355 (= T378), A378 (= A401), T379 (= T402), H380 (= H403), N381 (= N404), C405 (≠ R425), L406 (= L426), E452 (= E465), S458 (= S471)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
50% identity, 47% coverage: 15:500/1039 of query aligns to 1:483/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D286), A260 (= A287), V291 (≠ A318), Q293 (= Q320), R320 (= R347), V322 (= V349), K323 (= K350), G324 (= G351), A325 (= A352), Y326 (= Y353), W327 (= W354), Y345 (≠ F372), T346 (= T373), R347 (≠ T374), K348 (= K375), T351 (= T378), A374 (= A401), T375 (= T402), H376 (= H403), N377 (= N404), C401 (≠ R425), L402 (= L426), E448 (= E465), S454 (= S471)
- binding cyclopropanecarboxylic acid: K218 (= K245), Y429 (= Y446), Y441 (= Y458), R444 (= R461), R445 (= R462)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
50% identity, 47% coverage: 15:500/1039 of query aligns to 1:483/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D286), A260 (= A287), V291 (≠ A318), Q293 (= Q320), R320 (= R347), V322 (= V349), K323 (= K350), G324 (= G351), A325 (= A352), Y326 (= Y353), W327 (= W354), Y345 (≠ F372), T346 (= T373), R347 (≠ T374), K348 (= K375), T351 (= T378), A374 (= A401), T375 (= T402), H376 (= H403), N377 (= N404), C401 (≠ R425), L402 (= L426), E448 (= E465), S454 (= S471)
- binding cyclobutanecarboxylic acid: K218 (= K245), L402 (= L426), Y429 (= Y446), Y441 (= Y458), R444 (= R461), R445 (= R462)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
50% identity, 47% coverage: 15:500/1039 of query aligns to 1:483/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D286), A260 (= A287), V291 (≠ A318), Q293 (= Q320), R320 (= R347), V322 (= V349), K323 (= K350), G324 (= G351), A325 (= A352), Y326 (= Y353), W327 (= W354), Y345 (≠ F372), T346 (= T373), R347 (≠ T374), K348 (= K375), T351 (= T378), A374 (= A401), T375 (= T402), H376 (= H403), N377 (= N404), C401 (≠ R425), L402 (= L426), E448 (= E465), S454 (= S471)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K245), Y326 (= Y353), Y429 (= Y446), Y441 (= Y458), R444 (= R461), R445 (= R462)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
49% identity, 47% coverage: 15:500/1039 of query aligns to 2:475/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A287), V283 (≠ A318), Q285 (= Q320), R312 (= R347), V314 (= V349), K315 (= K350), G316 (= G351), A317 (= A352), Y318 (= Y353), W319 (= W354), Y337 (≠ F372), T338 (= T373), R339 (≠ T374), K340 (= K375), T343 (= T378), A366 (= A401), T367 (= T402), H368 (= H403), N369 (= N404), C393 (≠ R425), L394 (= L426), E440 (= E465), S446 (= S471), F447 (= F472)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K245), Y421 (= Y446), R436 (= R461), R437 (= R462)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
32% identity, 84% coverage: 150:1024/1039 of query aligns to 68:954/959 of 5ur2B
- active site: N618 (= N689), K641 (= K712), E722 (= E789), C756 (= C823), E851 (= E919), T931 (≠ A1001)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K245), D215 (= D286), M216 (≠ A287), Q249 (= Q320), V278 (= V349), K279 (= K350), G280 (= G351), A281 (= A352), W283 (= W354), Y300 (≠ F372), T301 (= T373), N302 (≠ T374), K303 (= K375), S306 (≠ T378), A329 (= A401), S330 (≠ T402), H331 (= H403), N332 (= N404), Q356 (= Q424), M357 (≠ R425), L358 (= L426), Y379 (= Y446), E398 (= E465), E403 (≠ S470), W405 (≠ F472)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
47% identity, 47% coverage: 15:500/1039 of query aligns to 1:453/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D286), A230 (= A287), V261 (≠ A318), Q263 (= Q320), R290 (= R347), V292 (= V349), K293 (= K350), G294 (= G351), A295 (= A352), Y296 (= Y353), W297 (= W354), Y315 (≠ F372), T316 (= T373), R317 (≠ T374), K318 (= K375), T321 (= T378), A344 (= A401), T345 (= T402), H346 (= H403), N347 (= N404), Q370 (= Q424), C371 (≠ R425), L372 (= L426), E418 (= E465), S424 (= S471)
Query Sequence
>WP_011384888.1 AMB_RS12610 bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA
MIFTAPLPAPDPERQAIHRAAGTSEADLVSGLSAGIPLEDEARRRIVNRAVNLVDGARRN
RRTLGLDGLLNEYRLSTREGVVLMCLAEALLRIPDDHTVDLLIKDKIASADWDGHLGHSP
SVFVNASTWALVLGDRLLHLEEDGRAVLGRMAGRLGEAVVRRALRHAMGLMGRQFVLGRT
IAEALDNARAWEARGYRHSFDMLGEAARCEQAAQDYLRAYAGAIEALGRHAKGAGPIAGP
GLSVKLSALHPRFEMAQRQRVLGELVPRLRDLCHRARDAGIGLTIDAEEADRLDISLDVM
EAALADPALDGWDGFGMAVQAYQKRARPVIAWAGALAARRQQRLMIRLVKGAYWDGEVKR
AQERGLGGFPVFTTKEATDVSYLACAADLLARPDLFYPQFATHNAHTAAAVMEMTGGAGD
WEFQRLHGMGEALYAQLVPEFPCRTYAPVGSHQELLPYLVRRLLENGANSSFVSRLADEE
IPAHVVAADPLAALGRITPQLVAEPSALFGPSRRNSGGLDLSSPAVLAQLDLALAAVATP
ERSAPIVDGRERENQAAKPVLDPADHRRVVGEVVDASPADVEAALASARAAFPAWDDLGG
EARASILERAADRLEADRARFMALAIREAGKTIPDALSEVREAVDFLRFYAAEARARFSQ
PVRLPGPVGESNELMLGGRGVFACISPWNFPLAIFVGQVAAALAAGNAVVAKPAPQTPLM
AAAAVRLLHQAGVPPQALHLVPGGPAIGEALTVNPLVDAIAFTGSTATARHINRLRAAMD
GPLAPLIAETGGLNAMIVDSSALPEQVVADCLESAFRSAGQRCSALRVAFIQREAWTRIQ
PLLAGAMAELSLGDPALLSTDVGPVIDEASRRRLLAHGGRLRHAGRMIGQSACPPDCRVG
TFFAPMAHQLDNLDLLQSEVFGPILHVIPWEAGRLEQVLDCVAATSYGLTLGIHSRIDAT
IAQVIARARIGNIYVNRTMIGAVVGSQPFGGLGLSGTGAKAGGPNTLIRYGVERCLSVNT
AAAGGDVALMAGPQRHGTK
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