SitesBLAST
Comparing RR42_RS20125 FitnessBrowser__Cup4G11:RR42_RS20125 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)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1218/1218 of 6x9dA
- active site: N692 (= N787), K715 (= K810), E795 (= E891), C829 (= C925), E925 (= E1025), A1007 (= A1107)
- binding flavin-adenine dinucleotide: D291 (= D374), A292 (= A375), V323 (= V406), Q325 (= Q408), R352 (= R435), V354 (= V437), K355 (= K438), G356 (= G439), A357 (= A440), Y358 (= Y441), W359 (= W442), F377 (≠ Y460), T378 (= T461), R379 (= R462), K380 (= K463), T383 (= T466), A406 (= A489), T407 (= T490), H408 (= H491), N409 (= N492), Q432 (= Q515), C433 (= C516), E477 (= E563), S483 (= S569), F484 (= F570)
- binding 4-hydroxyproline: E659 (= E753), F693 (= F788), I697 (= I792), R828 (= R924), S830 (= S926), G987 (= G1087), A988 (= A1088), F995 (= F1095)
- binding nicotinamide-adenine-dinucleotide: I688 (= I783), S689 (= S784), P690 (= P785), W691 (= W786), N692 (= N787), I697 (= I792), K715 (= K810), A717 (= A812), E718 (= E813), G748 (= G843), G751 (= G847), A752 (= A848), T766 (= T862), G767 (= G863), S768 (= S864), V771 (= V867), E795 (= E891), T796 (= T892), C829 (= C925), E925 (= E1025), F927 (= F1027), F995 (= F1095)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D374), A291 (= A375), V322 (= V406), Q324 (= Q408), R351 (= R435), V353 (= V437), K354 (= K438), G355 (= G439), A356 (= A440), Y357 (= Y441), W358 (= W442), F376 (≠ Y460), T377 (= T461), R378 (= R462), K379 (= K463), T382 (= T466), A405 (= A489), T406 (= T490), H407 (= H491), N408 (= N492), C432 (= C516), L433 (= L517), E476 (= E563), S482 (= S569), F483 (= F570)
- binding nicotinamide-adenine-dinucleotide: I687 (= I783), S688 (= S784), P689 (= P785), W690 (= W786), N691 (= N787), I696 (= I792), K714 (= K810), E717 (= E813), G747 (= G843), G750 (= G847), T765 (= T862), G766 (= G863), S767 (= S864), V770 (= V867), I774 (≠ L871), E794 (= E891), T795 (= T892), C828 (= C925), E924 (= E1025), F926 (= F1027), F994 (= F1095)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K333), Y457 (= Y544), Y469 (= Y556), R472 (= R559), R473 (= R560)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K333), D290 (= D374), Y457 (= Y544), Y469 (= Y556), R472 (= R559), R473 (= R560)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I783), S688 (= S784), P689 (= P785), W690 (= W786), N691 (= N787), I696 (= I792), K714 (= K810), A716 (= A812), E717 (= E813), G747 (= G843), G750 (= G847), A751 (= A848), T765 (= T862), G766 (= G863), S767 (= S864), V770 (= V867), E794 (= E891), T795 (= T892), C828 (= C925), E924 (= E1025), F926 (= F1027), F994 (= F1095)
- 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 (= D374), A291 (= A375), V322 (= V406), Q324 (= Q408), V353 (= V437), K354 (= K438), G355 (= G439), A356 (= A440), W358 (= W442), F376 (≠ Y460), T377 (= T461), R378 (= R462), K379 (= K463), T382 (= T466), A405 (= A489), T406 (= T490), H407 (= H491), N408 (= N492), Q431 (= Q515), C432 (= C516), L433 (= L517), Y457 (= Y544), E476 (= E563), G1217 (= G1333)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D374), A290 (= A375), V321 (= V406), Q323 (= Q408), R350 (= R435), V352 (= V437), K353 (= K438), G354 (= G439), A355 (= A440), Y356 (= Y441), W357 (= W442), F375 (≠ Y460), T376 (= T461), R377 (= R462), K378 (= K463), T381 (= T466), A404 (= A489), T405 (= T490), H406 (= H491), N407 (= N492), C431 (= C516), L432 (= L517), E475 (= E563), S481 (= S569), F482 (= F570)
- binding nicotinamide-adenine-dinucleotide: I686 (= I783), S687 (= S784), P688 (= P785), W689 (= W786), N690 (= N787), I695 (= I792), K713 (= K810), A715 (= A812), E716 (= E813), G746 (= G843), G749 (= G847), A750 (= A848), T764 (= T862), G765 (= G863), S766 (= S864), V769 (= V867), E793 (= E891), T794 (= T892), C827 (= C925), E923 (= E1025), F925 (= F1027), F993 (= F1095)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y544), Y468 (= Y556), R471 (= R559), R472 (= R560)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1216/1216 of 6x99A
- active site: N690 (= N787), K713 (= K810), E793 (= E891), C827 (= C925), E923 (= E1025), A1005 (= A1107)
- binding d-proline: W557 (≠ V649), T558 (≠ S650), E657 (= E753), F691 (= F788), R727 (= R824), R826 (= R924), S828 (= S926), G985 (= G1087), A986 (= A1088), F993 (= F1095)
- binding flavin-adenine dinucleotide: D289 (= D374), A290 (= A375), V321 (= V406), R350 (= R435), V352 (= V437), K353 (= K438), G354 (= G439), A355 (= A440), Y356 (= Y441), W357 (= W442), F375 (≠ Y460), T376 (= T461), R377 (= R462), K378 (= K463), T381 (= T466), A404 (= A489), T405 (= T490), H406 (= H491), N407 (= N492), Q430 (= Q515), C431 (= C516), Y456 (= Y544), E475 (= E563), S481 (= S569), F482 (= F570)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
62% identity, 94% coverage: 81:1332/1333 of query aligns to 4:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I783), S688 (= S784), P689 (= P785), W690 (= W786), N691 (= N787), K714 (= K810), E717 (= E813), G747 (= G843), G750 (= G847), A751 (= A848), F764 (= F861), G766 (= G863), S767 (= S864), V770 (= V867), T795 (= T892), G796 (= G893), C828 (= C925), E924 (= E1025), F926 (= F1027)
- 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 (= K333), D290 (= D374), A291 (= A375), V322 (= V406), Q324 (= Q408), R351 (= R435), V353 (= V437), K354 (= K438), G355 (= G439), A356 (= A440), Y357 (= Y441), W358 (= W442), F376 (≠ Y460), T377 (= T461), R378 (= R462), K379 (= K463), T382 (= T466), A405 (= A489), T406 (= T490), H407 (= H491), N408 (= N492), Q431 (= Q515), C432 (= C516), L433 (= L517), Y457 (= Y544), S482 (= S569), F483 (= F570)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1214/1214 of 6x9aA
- active site: N688 (= N787), K711 (= K810), E791 (= E891), C825 (= C925), E921 (= E1025), A1003 (= A1107)
- binding flavin-adenine dinucleotide: D287 (= D374), A288 (= A375), V319 (= V406), R348 (= R435), V350 (= V437), K351 (= K438), G352 (= G439), A353 (= A440), Y354 (= Y441), W355 (= W442), F373 (≠ Y460), T374 (= T461), R375 (= R462), K376 (= K463), T379 (= T466), A402 (= A489), T403 (= T490), H404 (= H491), N405 (= N492), C429 (= C516), E473 (= E563), S479 (= S569), F480 (= F570)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ V649), T556 (≠ S650), E655 (= E753), F689 (= F788), R725 (= R824), S826 (= S926), G983 (= G1087), A984 (= A1088), F991 (= F1095)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1333/1333 of query aligns to 4:1214/1214 of 6x9bA
- active site: N688 (= N787), K711 (= K810), E791 (= E891), C825 (= C925), E921 (= E1025), A1003 (= A1107)
- binding flavin-adenine dinucleotide: D287 (= D374), A288 (= A375), V319 (= V406), R348 (= R435), V350 (= V437), K351 (= K438), G352 (= G439), A353 (= A440), Y354 (= Y441), W355 (= W442), F373 (≠ Y460), T374 (= T461), R375 (= R462), K376 (= K463), T379 (= T466), A402 (= A489), T403 (= T490), H404 (= H491), N405 (= N492), Q428 (= Q515), C429 (= C516), Y454 (= Y544), E473 (= E563), S479 (= S569), F480 (= F570)
- binding nicotinamide-adenine-dinucleotide: I684 (= I783), S685 (= S784), P686 (= P785), W687 (= W786), N688 (= N787), I693 (= I792), K711 (= K810), A713 (= A812), E714 (= E813), G744 (= G843), G747 (= G847), A748 (= A848), T762 (= T862), G763 (= G863), S764 (= S864), V767 (= V867), I771 (≠ L871), E791 (= E891), T792 (= T892), C825 (= C925), E921 (= E1025), F923 (= F1027)
- binding (4R)-4-hydroxy-D-proline: E655 (= E753), F689 (= F788), S826 (= S926), G983 (= G1087), A984 (= A1088), F991 (= F1095)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
62% identity, 94% coverage: 81:1329/1333 of query aligns to 3:1209/1209 of 6x9cA
- active site: N687 (= N787), K710 (= K810), E790 (= E891), C824 (= C925), E920 (= E1025), A1002 (= A1107)
- binding dihydroflavine-adenine dinucleotide: D286 (= D374), A287 (= A375), V318 (= V406), Q320 (= Q408), R347 (= R435), V349 (= V437), K350 (= K438), G351 (= G439), A352 (= A440), Y353 (= Y441), W354 (= W442), F372 (≠ Y460), T373 (= T461), R374 (= R462), K375 (= K463), T378 (= T466), A401 (= A489), T402 (= T490), H403 (= H491), N404 (= N492), Q427 (= Q515), C428 (= C516), E472 (= E563), S478 (= S569), F479 (= F570)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I783), S684 (= S784), P685 (= P785), W686 (= W786), N687 (= N787), K710 (= K810), E713 (= E813), G743 (= G843), G746 (= G847), A747 (= A848), F760 (= F861), G762 (= G863), S763 (= S864), V766 (= V867), E920 (= E1025), F922 (= F1027)
- binding proline: R823 (= R924), C824 (= C925), S825 (= S926), G982 (= G1087), A983 (= A1088), F990 (= F1095)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
61% identity, 94% coverage: 81:1330/1333 of query aligns to 4:1206/1207 of 5kf6A
- active site: N683 (= N787), K706 (= K810), E786 (= E891), C820 (= C925), E916 (= E1025), A998 (= A1107)
- binding flavin-adenine dinucleotide: D282 (= D374), A283 (= A375), V314 (= V406), Q316 (= Q408), R343 (= R435), V345 (= V437), K346 (= K438), G347 (= G439), A348 (= A440), Y349 (= Y441), W350 (= W442), F368 (≠ Y460), T369 (= T461), R370 (= R462), K371 (= K463), T374 (= T466), A397 (= A489), T398 (= T490), H399 (= H491), N400 (= N492), Q423 (= Q515), C424 (= C516), L425 (= L517), E468 (= E563), S474 (= S569), F475 (= F570)
- binding nicotinamide-adenine-dinucleotide: I679 (= I783), S680 (= S784), P681 (= P785), W682 (= W786), N683 (= N787), I688 (= I792), K706 (= K810), A708 (= A812), E709 (= E813), G739 (= G843), G742 (= G847), A743 (= A848), F756 (= F861), T757 (= T862), G758 (= G863), S759 (= S864), V762 (= V867), I766 (≠ L871), E786 (= E891), T787 (= T892), C820 (= C925), E916 (= E1025), F918 (= F1027), F986 (= F1095)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K333), D282 (= D374), Y449 (= Y544), R464 (= R559), R465 (= R560)
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)
61% identity, 94% coverage: 81:1330/1333 of query aligns to 4:1196/1197 of 6ufpA
- active site: N673 (= N787), K696 (= K810), E776 (= E891), C810 (= C925), E906 (= E1025), A988 (= A1107)
- binding dihydroflavine-adenine dinucleotide: D285 (= D374), A286 (= A375), V317 (= V406), Q319 (= Q408), R346 (= R435), V348 (= V437), K349 (= K438), G350 (= G439), A351 (= A440), W353 (= W442), F371 (≠ Y460), T372 (= T461), R373 (= R462), K374 (= K463), T377 (= T466), A400 (= A489), T401 (= T490), H402 (= H491), N403 (= N492), Q426 (= Q515), C427 (= C516), L428 (= L517), S464 (= S569)
- binding nicotinamide-adenine-dinucleotide: I669 (= I783), P671 (= P785), W672 (= W786), N673 (= N787), I678 (= I792), K696 (= K810), E699 (= E813), G729 (= G843), G732 (= G847), F746 (= F861), T747 (= T862), G748 (= G863), S749 (= S864), V752 (= V867), E776 (= E891), T777 (= T892), C810 (= C925), E906 (= E1025), F908 (= F1027)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K333), D285 (= D374), Y439 (= Y544), Y451 (= Y556), R454 (= R559), R455 (= R560)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
47% identity, 76% coverage: 99:1116/1333 of query aligns to 8:960/973 of 6bsnA
- active site: N643 (= N787), E743 (= E891), A777 (≠ C925), A951 (= A1107)
- binding dihydroflavine-adenine dinucleotide: D269 (= D374), A270 (= A375), Q303 (= Q408), R330 (= R435), V332 (= V437), K333 (= K438), G334 (= G439), A335 (= A440), Y336 (= Y441), W337 (= W442), F355 (≠ Y460), T356 (= T461), R357 (= R462), K358 (= K463), T361 (= T466), A384 (= A489), T385 (= T490), H386 (= H491), N387 (= N492), Y432 (= Y544), S457 (= S569), F458 (= F570)
- binding proline: M630 (vs. gap), W642 (= W786), F644 (= F788), G718 (= G863), R776 (= R924), S778 (= S926), F871 (= F1027), I930 (≠ V1086), G931 (= G1087), A932 (= A1088), F939 (= F1095), A958 (≠ H1114), R959 (= R1115)
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
47% identity, 76% coverage: 99:1116/1333 of query aligns to 8:969/983 of 3hazA
- active site: N652 (= N787), K675 (= K810), E752 (= E891), C786 (= C925), E878 (= E1025), A960 (= A1107)
- binding flavin-adenine dinucleotide: D272 (= D374), A273 (= A375), Q306 (= Q408), R333 (= R435), V335 (= V437), K336 (= K438), G337 (= G439), A338 (= A440), Y339 (= Y441), W340 (= W442), F358 (≠ Y460), T359 (= T461), R360 (= R462), K361 (= K463), T364 (= T466), A387 (= A489), T388 (= T490), H389 (= H491), N390 (= N492), Y435 (= Y544), S460 (= S569), F461 (= F570)
- binding nicotinamide-adenine-dinucleotide: I648 (= I783), S649 (= S784), P650 (= P785), W651 (= W786), N652 (= N787), I657 (= I792), K675 (= K810), P676 (= P811), A677 (= A812), G708 (= G843), G711 (= G847), A712 (= A848), T726 (= T862), G727 (= G863), S728 (= S864), V731 (= V867), I735 (≠ L871), E752 (= E891), T753 (= T892), C786 (= C925), E878 (= E1025), F880 (= F1027), F948 (= F1095)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
80% identity, 39% coverage: 92:613/1333 of query aligns to 1:502/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K333), Y433 (= Y544), R448 (= R559), R449 (= R560)
- binding flavin-adenine dinucleotide: D263 (= D374), A264 (= A375), V295 (= V406), Q297 (= Q408), R324 (= R435), V326 (= V437), K327 (= K438), G328 (= G439), A329 (= A440), Y330 (= Y441), W331 (= W442), Y349 (= Y460), T350 (= T461), R351 (= R462), K352 (= K463), T355 (= T466), A378 (= A489), T379 (= T490), H380 (= H491), N381 (= N492), C405 (= C516), L406 (= L517), E452 (= E563), S458 (= S569)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
79% identity, 39% coverage: 92:613/1333 of query aligns to 1:498/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D374), A260 (= A375), V291 (= V406), Q293 (= Q408), R320 (= R435), V322 (= V437), K323 (= K438), G324 (= G439), A325 (= A440), Y326 (= Y441), W327 (= W442), Y345 (= Y460), T346 (= T461), R347 (= R462), K348 (= K463), T351 (= T466), A374 (= A489), T375 (= T490), H376 (= H491), N377 (= N492), C401 (= C516), L402 (= L517), E448 (= E563), S454 (= S569)
- binding cyclopropanecarboxylic acid: K218 (= K333), Y429 (= Y544), Y441 (= Y556), R444 (= R559), R445 (= R560)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
79% identity, 39% coverage: 92:613/1333 of query aligns to 1:498/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D374), A260 (= A375), V291 (= V406), Q293 (= Q408), R320 (= R435), V322 (= V437), K323 (= K438), G324 (= G439), A325 (= A440), Y326 (= Y441), W327 (= W442), Y345 (= Y460), T346 (= T461), R347 (= R462), K348 (= K463), T351 (= T466), A374 (= A489), T375 (= T490), H376 (= H491), N377 (= N492), C401 (= C516), L402 (= L517), E448 (= E563), S454 (= S569)
- binding cyclobutanecarboxylic acid: K218 (= K333), L402 (= L517), Y429 (= Y544), Y441 (= Y556), R444 (= R559), R445 (= R560)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
79% identity, 39% coverage: 92:613/1333 of query aligns to 1:498/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D374), A260 (= A375), V291 (= V406), Q293 (= Q408), R320 (= R435), V322 (= V437), K323 (= K438), G324 (= G439), A325 (= A440), Y326 (= Y441), W327 (= W442), Y345 (= Y460), T346 (= T461), R347 (= R462), K348 (= K463), T351 (= T466), A374 (= A489), T375 (= T490), H376 (= H491), N377 (= N492), C401 (= C516), L402 (= L517), E448 (= E563), S454 (= S569)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K333), Y326 (= Y441), Y429 (= Y544), Y441 (= Y556), R444 (= R559), R445 (= R560)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
78% identity, 39% coverage: 91:613/1333 of query aligns to 1:490/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A375), V283 (= V406), Q285 (= Q408), R312 (= R435), V314 (= V437), K315 (= K438), G316 (= G439), A317 (= A440), Y318 (= Y441), W319 (= W442), Y337 (= Y460), T338 (= T461), R339 (= R462), K340 (= K463), T343 (= T466), A366 (= A489), T367 (= T490), H368 (= H491), N369 (= N492), C393 (= C516), L394 (= L517), E440 (= E563), S446 (= S569), F447 (= F570)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K333), Y421 (= Y544), R436 (= R559), R437 (= R560)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
74% identity, 39% coverage: 92:613/1333 of query aligns to 1:468/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D374), A230 (= A375), V261 (= V406), Q263 (= Q408), R290 (= R435), V292 (= V437), K293 (= K438), G294 (= G439), A295 (= A440), Y296 (= Y441), W297 (= W442), Y315 (= Y460), T316 (= T461), R317 (= R462), K318 (= K463), T321 (= T466), A344 (= A489), T345 (= T490), H346 (= H491), N347 (= N492), Q370 (= Q515), C371 (= C516), L372 (= L517), E418 (= E563), S424 (= S569)
1tiwA Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) complexed with l-tetrahydro-2-furoic acid (see paper)
72% identity, 39% coverage: 91:613/1333 of query aligns to 1:458/459 of 1tiwA
- binding flavin-adenine dinucleotide: D219 (= D374), A220 (= A375), V251 (= V406), Q253 (= Q408), R280 (= R435), V282 (= V437), K283 (= K438), G284 (= G439), A285 (= A440), Y286 (= Y441), W287 (= W442), Y305 (= Y460), T306 (= T461), R307 (= R462), K308 (= K463), T311 (= T466), A334 (= A489), T335 (= T490), H336 (= H491), N337 (= N492), Q360 (= Q515), C361 (= C516), L362 (= L517), E408 (= E563), S414 (= S569)
- binding tetrahydrofuran-2-carboxylic acid: K178 (= K333), D219 (= D374), Y389 (= Y544), R404 (= R559), R405 (= R560)
Query Sequence
>RR42_RS20125 FitnessBrowser__Cup4G11:RR42_RS20125
MATTTLGVKLDDASRERLKRVAQSIDRTPHWLIKQAIFTYLEQVERGNIPHETSAAGTGS
EGAADGADAFDGAASDGAIQPFLEFAQSVQPQSVLRAAITAAYRRPESECVPVLLEQARL
PHQQAEAALAMARTLATRLRERKVGTGREGLVQGLIQEFSLSSQEGVALMCLAEALLRIP
DKATRDALIRDKISGANWQSHLGQSPSVFVNAATWGLLFTGKLVATHTEAGLSKALTRII
GKGGEPLIRKGVDMAMRLMGEQFVTGETISEALANARKYEAEGFRYSYDMLGEAAMTEAD
AQRYLASYEQAINAIGQASRGRGIYEGPGISIKLSALHPRYSRAQHERVIGELYGRLKSL
TLLARQYDIGINIDAEEADRLEISLDLLERLCFEPELAGWNGIGFVVQGYQKRCPFVIDY
LIDLARRSRHRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYVACARKLLSV
PDVIYPQFATHNAHTLAAIYQIAGHNYYPGQYEFQCLHGMGEPLYDQVVGPLADGKFNRP
CRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADDTISLDELVADPVAVVEQMHADEG
ALGLPHPRIAQPRTLYGESRANSAGIDLSNEHRLASLSSALLAGTSEAVSAVPLLGTEAA
AGEDVNQPAPVRNPSDQRDVVGHVTEASMAEVEAALQAAVNAAPIWQATPADVRAAALER
AAELMEAQMQSLMGIIVREAGKTFSNAIAEVREAVDFLRYYAAQVRETFSSDTHRPLGPV
VCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLREAGVPAGAVQLLP
GRGETVGAALVGDARVKGVMFTGSTEVARLLQRSVAGRLDAAGRPVPLIAETGGQNAMIV
DSSALAEQVVGDVVNSAFDSAGQRCSALRVLCLQEEVADRVLEMLKGAMDELTMGNPDRL
STDVGPVIDEEARGNIVRHIDAMRAKGRRVHQADPNGALSAACRNGTFVSPTLIELDSIE
ELQREVFGPVLHVVRYPRAGLDTLLAQINGTGYGLTMGIHTRIDETIEHIVERAEVGNLY
VNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLSVCPLDAVARVVRASDTVGGADE
TGPVRRTLTETLATLKEWAQRESAALPGLVAACERFAAASAAGLSVTLPGPTGERNTYTL
LPRAAVLCLAQQETDLAVQLAAVLAAGSQAVWVESPMARALFARLPKAVQSRVRLVADWS
AGDTGFDAVLHHGDSDQLRAVCEQLATRPGPIISVQGLAHGEPNIAIERLLIERSLSVNT
AAAGGNASLMTIG
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