SitesBLAST
Comparing SMc02181 SMc02181 bifunctional proline dehydrogenase/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)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1218/1218 of 6x9dA
- active site: N692 (= N707), K715 (= K730), E795 (= E810), C829 (= C844), E925 (= E940), A1007 (= A1022)
- binding flavin-adenine dinucleotide: D291 (= D306), A292 (= A307), V323 (= V338), Q325 (= Q340), R352 (= R367), V354 (= V369), K355 (= K370), G356 (= G371), A357 (= A372), Y358 (= Y373), W359 (= W374), F377 (= F392), T378 (= T393), R379 (= R394), K380 (= K395), T383 (= T398), A406 (= A421), T407 (= T422), H408 (= H423), N409 (= N424), Q432 (= Q447), C433 (= C448), E477 (= E492), S483 (= S498), F484 (= F499)
- binding 4-hydroxyproline: E659 (= E674), F693 (= F708), I697 (= I712), R828 (= R843), S830 (= S845), G987 (= G1002), A988 (= A1003), F995 (= F1010)
- binding nicotinamide-adenine-dinucleotide: I688 (= I703), S689 (= S704), P690 (= P705), W691 (= W706), N692 (= N707), I697 (= I712), K715 (= K730), A717 (= A732), E718 (= E733), G748 (= G763), G751 (= G766), A752 (= A767), T766 (= T781), G767 (= G782), S768 (= S783), V771 (= V786), E795 (= E810), T796 (= T811), C829 (= C844), E925 (= E940), F927 (= F942), F995 (= F1010)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), R351 (= R367), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), Y357 (= Y373), W358 (= W374), F376 (= F392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), C432 (= C448), L433 (= L449), E476 (= E492), S482 (= S498), F483 (= F499)
- binding nicotinamide-adenine-dinucleotide: I687 (= I703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), I696 (= I712), K714 (= K730), E717 (= E733), G747 (= G763), G750 (= G766), T765 (= T781), G766 (= G782), S767 (= S783), V770 (= V786), I774 (= I790), E794 (= E810), T795 (= T811), C828 (= C844), E924 (= E940), F926 (= F942), F994 (= F1010)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K265), Y457 (= Y473), Y469 (= Y485), R472 (= R488), R473 (= R489)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K265), D290 (= D306), Y457 (= Y473), Y469 (= Y485), R472 (= R488), R473 (= R489)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), I696 (= I712), K714 (= K730), A716 (= A732), E717 (= E733), G747 (= G763), G750 (= G766), A751 (= A767), T765 (= T781), G766 (= G782), S767 (= S783), V770 (= V786), E794 (= E810), T795 (= T811), C828 (= C844), E924 (= E940), F926 (= F942), F994 (= F1010)
- 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 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), W358 (= W374), F376 (= F392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), Q431 (= Q447), C432 (= C448), L433 (= L449), Y457 (= Y473), E476 (= E492), G1217 (= G1233)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D306), A290 (= A307), V321 (= V338), Q323 (= Q340), R350 (= R367), V352 (= V369), K353 (= K370), G354 (= G371), A355 (= A372), Y356 (= Y373), W357 (= W374), F375 (= F392), T376 (= T393), R377 (= R394), K378 (= K395), T381 (= T398), A404 (= A421), T405 (= T422), H406 (= H423), N407 (= N424), C431 (= C448), L432 (= L449), E475 (= E492), S481 (= S498), F482 (= F499)
- binding nicotinamide-adenine-dinucleotide: I686 (= I703), S687 (= S704), P688 (= P705), W689 (= W706), N690 (= N707), I695 (= I712), K713 (= K730), A715 (= A732), E716 (= E733), G746 (= G763), G749 (= G766), A750 (= A767), T764 (= T781), G765 (= G782), S766 (= S783), V769 (= V786), E793 (= E810), T794 (= T811), C827 (= C844), E923 (= E940), F925 (= F942), F993 (= F1010)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y473), Y468 (= Y485), R471 (= R488), R472 (= R489)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
100% identity, 99% coverage: 14:1232/1233 of query aligns to 1:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), K714 (= K730), E717 (= E733), G747 (= G763), G750 (= G766), A751 (= A767), F764 (= F780), G766 (= G782), S767 (= S783), V770 (= V786), T795 (= T811), G796 (= G812), C828 (= C844), E924 (= E940), F926 (= F942)
- 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 (= K265), D290 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), R351 (= R367), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), Y357 (= Y373), W358 (= W374), F376 (= F392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), Q431 (= Q447), C432 (= C448), L433 (= L449), Y457 (= Y473), S482 (= S498), F483 (= F499)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1216/1216 of 6x99A
- active site: N690 (= N707), K713 (= K730), E793 (= E810), C827 (= C844), E923 (= E940), A1005 (= A1022)
- binding d-proline: W557 (= W574), T558 (= T575), E657 (= E674), F691 (= F708), R727 (= R744), R826 (= R843), S828 (= S845), G985 (= G1002), A986 (= A1003), F993 (= F1010)
- binding flavin-adenine dinucleotide: D289 (= D306), A290 (= A307), V321 (= V338), R350 (= R367), V352 (= V369), K353 (= K370), G354 (= G371), A355 (= A372), Y356 (= Y373), W357 (= W374), F375 (= F392), T376 (= T393), R377 (= R394), K378 (= K395), T381 (= T398), A404 (= A421), T405 (= T422), H406 (= H423), N407 (= N424), Q430 (= Q447), C431 (= C448), Y456 (= Y473), E475 (= E492), S481 (= S498), F482 (= F499)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1214/1214 of 6x9bA
- active site: N688 (= N707), K711 (= K730), E791 (= E810), C825 (= C844), E921 (= E940), A1003 (= A1022)
- binding flavin-adenine dinucleotide: D287 (= D306), A288 (= A307), V319 (= V338), R348 (= R367), V350 (= V369), K351 (= K370), G352 (= G371), A353 (= A372), Y354 (= Y373), W355 (= W374), F373 (= F392), T374 (= T393), R375 (= R394), K376 (= K395), T379 (= T398), A402 (= A421), T403 (= T422), H404 (= H423), N405 (= N424), Q428 (= Q447), C429 (= C448), Y454 (= Y473), E473 (= E492), S479 (= S498), F480 (= F499)
- binding nicotinamide-adenine-dinucleotide: I684 (= I703), S685 (= S704), P686 (= P705), W687 (= W706), N688 (= N707), I693 (= I712), K711 (= K730), A713 (= A732), E714 (= E733), G744 (= G763), G747 (= G766), A748 (= A767), T762 (= T781), G763 (= G782), S764 (= S783), V767 (= V786), I771 (= I790), E791 (= E810), T792 (= T811), C825 (= C844), E921 (= E940), F923 (= F942)
- binding (4R)-4-hydroxy-D-proline: E655 (= E674), F689 (= F708), S826 (= S845), G983 (= G1002), A984 (= A1003), F991 (= F1010)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
100% identity, 99% coverage: 14:1233/1233 of query aligns to 1:1214/1214 of 6x9aA
- active site: N688 (= N707), K711 (= K730), E791 (= E810), C825 (= C844), E921 (= E940), A1003 (= A1022)
- binding flavin-adenine dinucleotide: D287 (= D306), A288 (= A307), V319 (= V338), R348 (= R367), V350 (= V369), K351 (= K370), G352 (= G371), A353 (= A372), Y354 (= Y373), W355 (= W374), F373 (= F392), T374 (= T393), R375 (= R394), K376 (= K395), T379 (= T398), A402 (= A421), T403 (= T422), H404 (= H423), N405 (= N424), C429 (= C448), E473 (= E492), S479 (= S498), F480 (= F499)
- binding (4S)-4-hydroxy-D-proline: W555 (= W574), T556 (= T575), E655 (= E674), F689 (= F708), R725 (= R744), S826 (= S845), G983 (= G1002), A984 (= A1003), F991 (= F1010)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
100% identity, 99% coverage: 15:1229/1233 of query aligns to 1:1209/1209 of 6x9cA
- active site: N687 (= N707), K710 (= K730), E790 (= E810), C824 (= C844), E920 (= E940), A1002 (= A1022)
- binding dihydroflavine-adenine dinucleotide: D286 (= D306), A287 (= A307), V318 (= V338), Q320 (= Q340), R347 (= R367), V349 (= V369), K350 (= K370), G351 (= G371), A352 (= A372), Y353 (= Y373), W354 (= W374), F372 (= F392), T373 (= T393), R374 (= R394), K375 (= K395), T378 (= T398), A401 (= A421), T402 (= T422), H403 (= H423), N404 (= N424), Q427 (= Q447), C428 (= C448), E472 (= E492), S478 (= S498), F479 (= F499)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I703), S684 (= S704), P685 (= P705), W686 (= W706), N687 (= N707), K710 (= K730), E713 (= E733), G743 (= G763), G746 (= G766), A747 (= A767), F760 (= F780), G762 (= G782), S763 (= S783), V766 (= V786), E920 (= E940), F922 (= F942)
- binding proline: R823 (= R843), C824 (= C844), S825 (= S845), G982 (= G1002), A983 (= A1003), F990 (= F1010)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
99% identity, 99% coverage: 14:1231/1233 of query aligns to 1:1207/1207 of 5kf6A
- active site: N683 (= N707), K706 (= K730), E786 (= E810), C820 (= C844), E916 (= E940), A998 (= A1022)
- binding flavin-adenine dinucleotide: D282 (= D306), A283 (= A307), V314 (= V338), Q316 (= Q340), R343 (= R367), V345 (= V369), K346 (= K370), G347 (= G371), A348 (= A372), Y349 (= Y373), W350 (= W374), F368 (= F392), T369 (= T393), R370 (= R394), K371 (= K395), T374 (= T398), A397 (= A421), T398 (= T422), H399 (= H423), N400 (= N424), Q423 (= Q447), C424 (= C448), L425 (= L449), E468 (= E492), S474 (= S498), F475 (= F499)
- binding nicotinamide-adenine-dinucleotide: I679 (= I703), S680 (= S704), P681 (= P705), W682 (= W706), N683 (= N707), I688 (= I712), K706 (= K730), A708 (= A732), E709 (= E733), G739 (= G763), G742 (= G766), A743 (= A767), F756 (= F780), T757 (= T781), G758 (= G782), S759 (= S783), V762 (= V786), I766 (= I790), E786 (= E810), T787 (= T811), C820 (= C844), E916 (= E940), F918 (= F942), F986 (= F1010)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K265), D282 (= D306), Y449 (= Y473), R464 (= R488), R465 (= R489)
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)
98% identity, 99% coverage: 14:1231/1233 of query aligns to 1:1197/1197 of 6ufpA
- active site: N673 (= N707), K696 (= K730), E776 (= E810), C810 (= C844), E906 (= E940), A988 (= A1022)
- binding dihydroflavine-adenine dinucleotide: D285 (= D306), A286 (= A307), V317 (= V338), Q319 (= Q340), R346 (= R367), V348 (= V369), K349 (= K370), G350 (= G371), A351 (= A372), W353 (= W374), F371 (= F392), T372 (= T393), R373 (= R394), K374 (= K395), T377 (= T398), A400 (= A421), T401 (= T422), H402 (= H423), N403 (= N424), Q426 (= Q447), C427 (= C448), L428 (= L449), S464 (= S498)
- binding nicotinamide-adenine-dinucleotide: I669 (= I703), P671 (= P705), W672 (= W706), N673 (= N707), I678 (= I712), K696 (= K730), E699 (= E733), G729 (= G763), G732 (= G766), F746 (= F780), T747 (= T781), G748 (= G782), S749 (= S783), V752 (= V786), E776 (= E810), T777 (= T811), C810 (= C844), E906 (= E940), F908 (= F942)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K265), D285 (= D306), Y439 (= Y473), Y451 (= Y485), R454 (= R488), R455 (= R489)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 81% coverage: 35:1037/1233 of query aligns to 8:966/973 of 6bsnA
- active site: N643 (= N707), E743 (= E810), A777 (≠ C844), A951 (= A1022)
- binding dihydroflavine-adenine dinucleotide: D269 (= D306), A270 (= A307), Q303 (= Q340), R330 (= R367), V332 (= V369), K333 (= K370), G334 (= G371), A335 (= A372), Y336 (= Y373), W337 (= W374), F355 (= F392), T356 (= T393), R357 (= R394), K358 (= K395), T361 (= T398), A384 (= A421), T385 (= T422), H386 (= H423), N387 (= N424), Y432 (= Y473), S457 (= S498), F458 (= F499)
- binding proline: M630 (vs. gap), W642 (= W706), F644 (= F708), G718 (= G782), R776 (= R843), S778 (= S845), F871 (= F942), I930 (= I1001), G931 (= G1002), A932 (= A1003), F939 (= F1010), A958 (≠ G1029), R959 (= R1030), A961 (≠ V1032)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
49% identity, 81% coverage: 35:1037/1233 of query aligns to 8:975/983 of 3hazA
- active site: N652 (= N707), K675 (= K730), E752 (= E810), C786 (= C844), E878 (= E940), A960 (= A1022)
- binding flavin-adenine dinucleotide: D272 (= D306), A273 (= A307), Q306 (= Q340), R333 (= R367), V335 (= V369), K336 (= K370), G337 (= G371), A338 (= A372), Y339 (= Y373), W340 (= W374), F358 (= F392), T359 (= T393), R360 (= R394), K361 (= K395), T364 (= T398), A387 (= A421), T388 (= T422), H389 (= H423), N390 (= N424), Y435 (= Y473), S460 (= S498), F461 (= F499)
- binding nicotinamide-adenine-dinucleotide: I648 (= I703), S649 (= S704), P650 (= P705), W651 (= W706), N652 (= N707), I657 (= I712), K675 (= K730), P676 (= P731), A677 (= A732), G708 (= G763), G711 (= G766), A712 (= A767), T726 (= T781), G727 (= G782), S728 (= S783), V731 (= V786), I735 (= I790), E752 (= E810), T753 (= T811), C786 (= C844), E878 (= E940), F880 (= F942), F948 (= F1010)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
66% identity, 41% coverage: 28:537/1233 of query aligns to 1:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K265), Y433 (= Y473), R448 (= R488), R449 (= R489)
- binding flavin-adenine dinucleotide: D263 (= D306), A264 (= A307), V295 (= V338), Q297 (= Q340), R324 (= R367), V326 (= V369), K327 (= K370), G328 (= G371), A329 (= A372), Y330 (= Y373), W331 (= W374), Y349 (≠ F392), T350 (= T393), R351 (= R394), K352 (= K395), T355 (= T398), A378 (= A421), T379 (= T422), H380 (= H423), N381 (= N424), C405 (= C448), L406 (= L449), E452 (= E492), S458 (= S498)
8dkoB Minimal puta proline dehydrogenase domain (design #1) complexed with s-(-)-tetrahydro-2-furoic acid (see paper)
100% identity, 27% coverage: 190:526/1233 of query aligns to 57:393/393 of 8dkoB
- binding flavin-adenine dinucleotide: D173 (= D306), A174 (= A307), V205 (= V338), Q207 (= Q340), R234 (= R367), V236 (= V369), K237 (= K370), G238 (= G371), A239 (= A372), Y240 (= Y373), W241 (= W374), F259 (= F392), T260 (= T393), R261 (= R394), K262 (= K395), T265 (= T398), A288 (= A421), T289 (= T422), H290 (= H423), N291 (= N424), C315 (= C448), L316 (= L449), E359 (= E492), S365 (= S498), F366 (= F499)
- binding tetrahydrofuran-2-carboxylic acid: K132 (= K265), D173 (= D306), Y340 (= Y473), R355 (= R488), R356 (= R489)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
65% identity, 41% coverage: 28:537/1233 of query aligns to 1:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (≠ F392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E492), S454 (= S498)
- binding cyclopropanecarboxylic acid: K218 (= K265), Y429 (= Y473), Y441 (= Y485), R444 (= R488), R445 (= R489)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
65% identity, 41% coverage: 28:537/1233 of query aligns to 1:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (≠ F392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E492), S454 (= S498)
- binding cyclobutanecarboxylic acid: K218 (= K265), L402 (= L449), Y429 (= Y473), Y441 (= Y485), R444 (= R488), R445 (= R489)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
65% identity, 41% coverage: 28:537/1233 of query aligns to 1:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (≠ F392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E492), S454 (= S498)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K265), Y326 (= Y373), Y429 (= Y473), Y441 (= Y485), R444 (= R488), R445 (= R489)
8dkqA Minimal puta proline dehydrogenase domain (design #2) complexed with 2-(furan-2-yl)acetic acid (see paper)
90% identity, 29% coverage: 162:521/1233 of query aligns to 6:381/381 of 8dkqA
- binding flavin-adenine dinucleotide: D166 (= D306), A167 (= A307), V198 (= V338), Q200 (= Q340), R227 (= R367), V229 (= V369), K230 (= K370), G231 (= G371), A232 (= A372), Y233 (= Y373), W234 (= W374), F252 (= F392), T253 (= T393), R254 (= R394), K255 (= K395), T258 (= T398), A281 (= A421), T282 (= T422), H283 (= H423), N284 (= N424), C308 (= C448), L309 (= L449), E352 (= E492), S358 (= S498), F359 (= F499)
- binding (furan-2-yl)acetic acid: K125 (= K265), D166 (= D306), A232 (= A372), L309 (= L449), Y333 (= Y473), R348 (= R488), R349 (= R489)
8dkqB Minimal puta proline dehydrogenase domain (design #2) complexed with 2-(furan-2-yl)acetic acid (see paper)
100% identity, 27% coverage: 192:521/1233 of query aligns to 59:388/388 of 8dkqB
- binding flavin-adenine dinucleotide: D173 (= D306), A174 (= A307), V205 (= V338), Q207 (= Q340), R234 (= R367), V236 (= V369), K237 (= K370), G238 (= G371), A239 (= A372), Y240 (= Y373), W241 (= W374), F259 (= F392), T260 (= T393), R261 (= R394), K262 (= K395), T265 (= T398), A288 (= A421), T289 (= T422), H290 (= H423), N291 (= N424), Q314 (= Q447), C315 (= C448), L316 (= L449), E359 (= E492), S365 (= S498), F366 (= F499)
- binding (furan-2-yl)acetic acid: K132 (= K265), D173 (= D306), A239 (= A372), L316 (= L449), Y340 (= Y473), R355 (= R488), R356 (= R489)
Query Sequence
>SMc02181 SMc02181 bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase
MSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEI
RDAAASTARKLIEALRGKHSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDAL
IRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTSTVNDRSLAAALTRLISRCGEPVI
RRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDY
ESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYD
IGLNIDAEEADRLELSLDLLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRS
GRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDVSYIACAAKLLAATDVVFPQF
ATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHE
TLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAEL
FGDARTNSAGLDLSNEETLASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRD
VVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAACLDRAAELMQARMPTLLGLIIRE
AGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIAAA
LVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMF
TGSTEVARLIQAQLADRLSPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSA
GQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDRLSVDVGPVITSEAKDNIEKHIE
RMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDRLV
DDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGP
KAGGPLYLGRLVTTAPVPPQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGL
DLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAAALATGNSVAIDAASGLQASLKN
LPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEIAR
NPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
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