SitesBLAST
Comparing 7023590 Shewana3_0819 bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase (RefSeq) 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)
48% identity, 96% coverage: 30:1051/1064 of query aligns to 9:983/983 of 3hazA
- active site: N652 (= N715), K675 (= K738), E752 (= E816), C786 (= C850), E878 (= E946), A960 (= A1028)
- binding flavin-adenine dinucleotide: D272 (= D305), A273 (= A306), Q306 (= Q339), R333 (= R366), V335 (= V368), K336 (= K369), G337 (= G370), A338 (= A371), Y339 (= Y372), W340 (= W373), F358 (≠ Y391), T359 (= T392), R360 (= R393), K361 (= K394), T364 (= T397), A387 (= A422), T388 (≠ S423), H389 (= H424), N390 (= N425), Y435 (= Y469), S460 (= S494), F461 (= F495)
- binding nicotinamide-adenine-dinucleotide: I648 (= I711), S649 (= S712), P650 (= P713), W651 (= W714), N652 (= N715), I657 (= I720), K675 (= K738), P676 (= P739), A677 (= A740), G708 (= G771), G711 (= G775), A712 (≠ N776), T726 (= T790), G727 (= G791), S728 (= S792), V731 (≠ T795), I735 (= I799), E752 (= E816), T753 (= T817), C786 (= C850), E878 (= E946), F880 (= F948), F948 (= F1016)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 96% coverage: 30:1049/1064 of query aligns to 9:972/973 of 6bsnA
- active site: N643 (= N715), E743 (= E816), A777 (≠ C850), A951 (= A1028)
- binding dihydroflavine-adenine dinucleotide: D269 (= D305), A270 (= A306), Q303 (= Q339), R330 (= R366), V332 (= V368), K333 (= K369), G334 (= G370), A335 (= A371), Y336 (= Y372), W337 (= W373), F355 (≠ Y391), T356 (= T392), R357 (= R393), K358 (= K394), T361 (= T397), A384 (= A422), T385 (≠ S423), H386 (= H424), N387 (= N425), Y432 (= Y469), S457 (= S494), F458 (= F495)
- binding proline: M630 (≠ L702), W642 (= W714), F644 (= F716), G718 (= G791), R776 (= R849), S778 (= S851), F871 (= F948), I930 (= I1007), G931 (= G1008), A932 (= A1009), F939 (= F1016), A958 (≠ T1035), R959 (= R1036), A961 (≠ V1038)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1016/1216 of 6x99A
- active site: N690 (= N715), K713 (= K738), E793 (= E816), C827 (= C850), E923 (= E946), A1005 (= A1028)
- binding d-proline: W557 (= W568), T558 (≠ Q569), E657 (= E668), F691 (= F716), R727 (≠ Q752), R826 (= R849), S828 (= S851), G985 (= G1008), A986 (= A1009), F993 (= F1016)
- binding flavin-adenine dinucleotide: D289 (= D305), A290 (= A306), V321 (= V337), R350 (= R366), V352 (= V368), K353 (= K369), G354 (= G370), A355 (= A371), Y356 (= Y372), W357 (= W373), F375 (≠ Y391), T376 (= T392), R377 (= R393), K378 (= K394), T381 (= T397), A404 (= A422), T405 (≠ S423), H406 (= H424), N407 (= N425), Q430 (= Q444), C431 (≠ R445), Y456 (= Y469), E475 (= E488), S481 (= S494), F482 (= F495)
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, 95% coverage: 25:1039/1064 of query aligns to 18:1018/1218 of 6x9dA
- active site: N692 (= N715), K715 (= K738), E795 (= E816), C829 (= C850), E925 (= E946), A1007 (= A1028)
- binding flavin-adenine dinucleotide: D291 (= D305), A292 (= A306), V323 (= V337), Q325 (= Q339), R352 (= R366), V354 (= V368), K355 (= K369), G356 (= G370), A357 (= A371), Y358 (= Y372), W359 (= W373), F377 (≠ Y391), T378 (= T392), R379 (= R393), K380 (= K394), T383 (= T397), A406 (= A422), T407 (≠ S423), H408 (= H424), N409 (= N425), Q432 (= Q444), C433 (≠ R445), E477 (= E488), S483 (= S494), F484 (= F495)
- binding 4-hydroxyproline: E659 (= E668), F693 (= F716), I697 (= I720), R828 (= R849), S830 (= S851), G987 (= G1008), A988 (= A1009), F995 (= F1016)
- binding nicotinamide-adenine-dinucleotide: I688 (= I711), S689 (= S712), P690 (= P713), W691 (= W714), N692 (= N715), I697 (= I720), K715 (= K738), A717 (= A740), E718 (= E741), G748 (= G771), G751 (= G775), A752 (≠ N776), T766 (= T790), G767 (= G791), S768 (= S792), V771 (≠ T795), E795 (= E816), T796 (= T817), C829 (= C850), E925 (= E946), F927 (= F948), F995 (= F1016)
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, 95% coverage: 25:1039/1064 of query aligns to 18:1014/1214 of 6x9aA
- active site: N688 (= N715), K711 (= K738), E791 (= E816), C825 (= C850), E921 (= E946), A1003 (= A1028)
- binding flavin-adenine dinucleotide: D287 (= D305), A288 (= A306), V319 (= V337), R348 (= R366), V350 (= V368), K351 (= K369), G352 (= G370), A353 (= A371), Y354 (= Y372), W355 (= W373), F373 (≠ Y391), T374 (= T392), R375 (= R393), K376 (= K394), T379 (= T397), A402 (= A422), T403 (≠ S423), H404 (= H424), N405 (= N425), C429 (≠ R445), E473 (= E488), S479 (= S494), F480 (= F495)
- binding (4S)-4-hydroxy-D-proline: W555 (= W568), T556 (≠ Q569), E655 (= E668), F689 (= F716), R725 (≠ Q752), S826 (= S851), G983 (= G1008), A984 (= A1009), F991 (= F1016)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1017/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D305), A291 (= A306), V322 (= V337), Q324 (= Q339), R351 (= R366), V353 (= V368), K354 (= K369), G355 (= G370), A356 (= A371), Y357 (= Y372), W358 (= W373), F376 (≠ Y391), T377 (= T392), R378 (= R393), K379 (= K394), T382 (= T397), A405 (= A422), T406 (≠ S423), H407 (= H424), N408 (= N425), C432 (≠ R445), L433 (= L446), E476 (= E488), S482 (= S494), F483 (= F495)
- binding nicotinamide-adenine-dinucleotide: I687 (= I711), S688 (= S712), P689 (= P713), W690 (= W714), N691 (= N715), I696 (= I720), K714 (= K738), E717 (= E741), G747 (= G771), G750 (= G775), T765 (= T790), G766 (= G791), S767 (= S792), V770 (≠ T795), I774 (= I799), E794 (= E816), T795 (= T817), C828 (= C850), E924 (= E946), F926 (= F948), F994 (= F1016)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K264), Y457 (= Y469), Y469 (= Y481), R472 (= R484), R473 (= R485)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K264), D290 (= D305), Y457 (= Y469), Y469 (= Y481), R472 (= R484), R473 (= R485)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1017/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I711), S688 (= S712), P689 (= P713), W690 (= W714), N691 (= N715), I696 (= I720), K714 (= K738), A716 (= A740), E717 (= E741), G747 (= G771), G750 (= G775), A751 (≠ N776), T765 (= T790), G766 (= G791), S767 (= S792), V770 (≠ T795), E794 (= E816), T795 (= T817), C828 (= C850), E924 (= E946), F926 (= F948), F994 (= F1016)
- 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 (= D305), A291 (= A306), V322 (= V337), Q324 (= Q339), V353 (= V368), K354 (= K369), G355 (= G370), A356 (= A371), W358 (= W373), F376 (≠ Y391), T377 (= T392), R378 (= R393), K379 (= K394), T382 (= T397), A405 (= A422), T406 (≠ S423), H407 (= H424), N408 (= N425), Q431 (= Q444), C432 (≠ R445), L433 (= L446), Y457 (= Y469), E476 (= E488)
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)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1017/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I711), S688 (= S712), P689 (= P713), W690 (= W714), N691 (= N715), K714 (= K738), E717 (= E741), G747 (= G771), G750 (= G775), A751 (≠ N776), F764 (= F789), G766 (= G791), S767 (= S792), V770 (≠ T795), T795 (= T817), G796 (= G818), C828 (= C850), E924 (= E946), F926 (= F948)
- 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 (= K264), D290 (= D305), A291 (= A306), V322 (= V337), Q324 (= Q339), R351 (= R366), V353 (= V368), K354 (= K369), G355 (= G370), A356 (= A371), Y357 (= Y372), W358 (= W373), F376 (≠ Y391), T377 (= T392), R378 (= R393), K379 (= K394), T382 (= T397), A405 (= A422), T406 (≠ S423), H407 (= H424), N408 (= N425), Q431 (= Q444), C432 (≠ R445), L433 (= L446), Y457 (= Y469), S482 (= S494), F483 (= F495)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 17:1013/1209 of 6x9cA
- active site: N687 (= N715), K710 (= K738), E790 (= E816), C824 (= C850), E920 (= E946), A1002 (= A1028)
- binding dihydroflavine-adenine dinucleotide: D286 (= D305), A287 (= A306), V318 (= V337), Q320 (= Q339), R347 (= R366), V349 (= V368), K350 (= K369), G351 (= G370), A352 (= A371), Y353 (= Y372), W354 (= W373), F372 (≠ Y391), T373 (= T392), R374 (= R393), K375 (= K394), T378 (= T397), A401 (= A422), T402 (≠ S423), H403 (= H424), N404 (= N425), Q427 (= Q444), C428 (≠ R445), E472 (= E488), S478 (= S494), F479 (= F495)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I711), S684 (= S712), P685 (= P713), W686 (= W714), N687 (= N715), K710 (= K738), E713 (= E741), G743 (= G771), G746 (= G775), A747 (≠ N776), F760 (= F789), G762 (= G791), S763 (= S792), V766 (≠ T795), E920 (= E946), F922 (= F948)
- binding proline: R823 (= R849), C824 (= C850), S825 (= S851), G982 (= G1008), A983 (= A1009), F990 (= F1016)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1014/1214 of 6x9bA
- active site: N688 (= N715), K711 (= K738), E791 (= E816), C825 (= C850), E921 (= E946), A1003 (= A1028)
- binding flavin-adenine dinucleotide: D287 (= D305), A288 (= A306), V319 (= V337), R348 (= R366), V350 (= V368), K351 (= K369), G352 (= G370), A353 (= A371), Y354 (= Y372), W355 (= W373), F373 (≠ Y391), T374 (= T392), R375 (= R393), K376 (= K394), T379 (= T397), A402 (= A422), T403 (≠ S423), H404 (= H424), N405 (= N425), Q428 (= Q444), C429 (≠ R445), Y454 (= Y469), E473 (= E488), S479 (= S494), F480 (= F495)
- binding nicotinamide-adenine-dinucleotide: I684 (= I711), S685 (= S712), P686 (= P713), W687 (= W714), N688 (= N715), I693 (= I720), K711 (= K738), A713 (= A740), E714 (= E741), G744 (= G771), G747 (= G775), A748 (≠ N776), T762 (= T790), G763 (= G791), S764 (= S792), V767 (≠ T795), I771 (= I799), E791 (= E816), T792 (= T817), C825 (= C850), E921 (= E946), F923 (= F948)
- binding (4R)-4-hydroxy-D-proline: E655 (= E668), F689 (= F716), S826 (= S851), G983 (= G1008), A984 (= A1009), F991 (= F1016)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1016/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D305), A290 (= A306), V321 (= V337), Q323 (= Q339), R350 (= R366), V352 (= V368), K353 (= K369), G354 (= G370), A355 (= A371), Y356 (= Y372), W357 (= W373), F375 (≠ Y391), T376 (= T392), R377 (= R393), K378 (= K394), T381 (= T397), A404 (= A422), T405 (≠ S423), H406 (= H424), N407 (= N425), C431 (≠ R445), L432 (= L446), E475 (= E488), S481 (= S494), F482 (= F495)
- binding nicotinamide-adenine-dinucleotide: I686 (= I711), S687 (= S712), P688 (= P713), W689 (= W714), N690 (= N715), I695 (= I720), K713 (= K738), A715 (= A740), E716 (= E741), G746 (= G771), G749 (= G775), A750 (≠ N776), T764 (= T790), G765 (= G791), S766 (= S792), V769 (≠ T795), E793 (= E816), T794 (= T817), C827 (= C850), E923 (= E946), F925 (= F948), F993 (= F1016)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y469), Y468 (= Y481), R471 (= R484), R472 (= R485)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:1009/1207 of 5kf6A
- active site: N683 (= N715), K706 (= K738), E786 (= E816), C820 (= C850), E916 (= E946), A998 (= A1028)
- binding flavin-adenine dinucleotide: D282 (= D305), A283 (= A306), V314 (= V337), Q316 (= Q339), R343 (= R366), V345 (= V368), K346 (= K369), G347 (= G370), A348 (= A371), Y349 (= Y372), W350 (= W373), F368 (≠ Y391), T369 (= T392), R370 (= R393), K371 (= K394), T374 (= T397), A397 (= A422), T398 (≠ S423), H399 (= H424), N400 (= N425), Q423 (= Q444), C424 (≠ R445), L425 (= L446), E468 (= E488), S474 (= S494), F475 (= F495)
- binding nicotinamide-adenine-dinucleotide: I679 (= I711), S680 (= S712), P681 (= P713), W682 (= W714), N683 (= N715), I688 (= I720), K706 (= K738), A708 (= A740), E709 (= E741), G739 (= G771), G742 (= G775), A743 (≠ N776), F756 (= F789), T757 (= T790), G758 (= G791), S759 (= S792), V762 (≠ T795), I766 (= I799), E786 (= E816), T787 (= T817), C820 (= C850), E916 (= E946), F918 (= F948), F986 (= F1016)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K264), D282 (= D305), Y449 (= Y469), R464 (= R484), R465 (= R485)
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)
48% identity, 95% coverage: 25:1039/1064 of query aligns to 18:999/1197 of 6ufpA
- active site: N673 (= N715), K696 (= K738), E776 (= E816), C810 (= C850), E906 (= E946), A988 (= A1028)
- binding dihydroflavine-adenine dinucleotide: D285 (= D305), A286 (= A306), V317 (= V337), Q319 (= Q339), R346 (= R366), V348 (= V368), K349 (= K369), G350 (= G370), A351 (= A371), W353 (= W373), F371 (≠ Y391), T372 (= T392), R373 (= R393), K374 (= K394), T377 (= T397), A400 (= A422), T401 (≠ S423), H402 (= H424), N403 (= N425), Q426 (= Q444), C427 (≠ R445), L428 (= L446), S464 (= S494)
- binding nicotinamide-adenine-dinucleotide: I669 (= I711), P671 (= P713), W672 (= W714), N673 (= N715), I678 (= I720), K696 (= K738), E699 (= E741), G729 (= G771), G732 (= G775), F746 (= F789), T747 (= T790), G748 (= G791), S749 (= S792), V752 (≠ T795), E776 (= E816), T777 (= T817), C810 (= C850), E906 (= E946), F908 (= F948)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K264), D285 (= D305), Y439 (= Y469), Y451 (= Y481), R454 (= R484), R455 (= R485)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
34% identity, 86% coverage: 132:1046/1064 of query aligns to 23:949/959 of 5ur2B
- active site: N618 (= N715), K641 (= K738), E722 (= E816), C756 (= C850), E851 (= E946), T931 (≠ A1028)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K264), D215 (= D305), M216 (≠ A306), Q249 (= Q339), V278 (= V368), K279 (= K369), G280 (= G370), A281 (= A371), W283 (= W373), Y300 (= Y391), T301 (= T392), N302 (≠ R393), K303 (= K394), S306 (≠ T397), A329 (= A422), S330 (= S423), H331 (= H424), N332 (= N425), Q356 (= Q444), M357 (≠ R445), L358 (= L446), Y379 (= Y469), E398 (= E488), E403 (≠ T493), W405 (≠ F495)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
46% identity, 48% coverage: 28:533/1064 of query aligns to 7:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K264), Y433 (= Y469), R448 (= R484), R449 (= R485)
- binding flavin-adenine dinucleotide: D263 (= D305), A264 (= A306), V295 (= V337), Q297 (= Q339), R324 (= R366), V326 (= V368), K327 (= K369), G328 (= G370), A329 (= A371), Y330 (= Y372), W331 (= W373), Y349 (= Y391), T350 (= T392), R351 (= R393), K352 (= K394), T355 (= T397), A378 (= A422), T379 (≠ S423), H380 (= H424), N381 (= N425), C405 (≠ R445), L406 (= L446), E452 (= E488), S458 (= S494)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
46% identity, 48% coverage: 28:533/1064 of query aligns to 7:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D305), A260 (= A306), V291 (= V337), Q293 (= Q339), R320 (= R366), V322 (= V368), K323 (= K369), G324 (= G370), A325 (= A371), Y326 (= Y372), W327 (= W373), Y345 (= Y391), T346 (= T392), R347 (= R393), K348 (= K394), T351 (= T397), A374 (= A422), T375 (≠ S423), H376 (= H424), N377 (= N425), C401 (≠ R445), L402 (= L446), E448 (= E488), S454 (= S494)
- binding cyclopropanecarboxylic acid: K218 (= K264), Y429 (= Y469), Y441 (= Y481), R444 (= R484), R445 (= R485)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
46% identity, 48% coverage: 28:533/1064 of query aligns to 7:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D305), A260 (= A306), V291 (= V337), Q293 (= Q339), R320 (= R366), V322 (= V368), K323 (= K369), G324 (= G370), A325 (= A371), Y326 (= Y372), W327 (= W373), Y345 (= Y391), T346 (= T392), R347 (= R393), K348 (= K394), T351 (= T397), A374 (= A422), T375 (≠ S423), H376 (= H424), N377 (= N425), C401 (≠ R445), L402 (= L446), E448 (= E488), S454 (= S494)
- binding cyclobutanecarboxylic acid: K218 (= K264), L402 (= L446), Y429 (= Y469), Y441 (= Y481), R444 (= R484), R445 (= R485)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
46% identity, 48% coverage: 28:533/1064 of query aligns to 7:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D305), A260 (= A306), V291 (= V337), Q293 (= Q339), R320 (= R366), V322 (= V368), K323 (= K369), G324 (= G370), A325 (= A371), Y326 (= Y372), W327 (= W373), Y345 (= Y391), T346 (= T392), R347 (= R393), K348 (= K394), T351 (= T397), A374 (= A422), T375 (≠ S423), H376 (= H424), N377 (= N425), C401 (≠ R445), L402 (= L446), E448 (= E488), S454 (= S494)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K264), Y326 (= Y372), Y429 (= Y469), Y441 (= Y481), R444 (= R484), R445 (= R485)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
34% identity, 82% coverage: 178:1051/1064 of query aligns to 85:968/979 of 4nmdA
- active site: N631 (= N715), K654 (= K738), E735 (= E816), C769 (= C850), E865 (= E946), A945 (= A1028)
- binding dihydroflavine-adenine dinucleotide: D226 (= D305), M227 (≠ A306), V256 (= V337), Q258 (= Q339), R285 (= R366), V287 (= V368), K288 (= K369), G289 (= G370), A290 (= A371), W292 (= W373), W309 (≠ Y391), T310 (= T392), I311 (≠ R393), K312 (= K394), S315 (≠ T397), A338 (= A422), S339 (= S423), H340 (= H424), N341 (= N425), Q365 (= Q444), V366 (≠ R445), L367 (= L446), Y388 (= Y469), F414 (= F495)
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
33% identity, 82% coverage: 178:1051/1064 of query aligns to 84:968/979 of 4nmfB
- active site: N631 (= N715), K654 (= K738), E735 (= E816), C769 (= C850), E865 (= E946), A945 (= A1028)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K264), Y290 (= Y372), Y387 (= Y469), Y399 (= Y481), R402 (= R484), R403 (= R485)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K264), L366 (= L446), Y399 (= Y481), R402 (= R484)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K264), D225 (= D305), M226 (≠ A306), V255 (= V337), Q257 (= Q339), R284 (= R366), V286 (= V368), K287 (= K369), G288 (= G370), A289 (= A371), W291 (= W373), W308 (≠ Y391), T309 (= T392), I310 (≠ R393), K311 (= K394), S314 (≠ T397), A337 (= A422), S338 (= S423), H339 (= H424), N340 (= N425), Q364 (= Q444), L366 (= L446), Y387 (= Y469), E406 (= E488), E411 (≠ T493), S412 (= S494), F413 (= F495)
Query Sequence
>7023590 Shewana3_0819 bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase (RefSeq)
MEAITMFKASEVLAGRYDSANLDELFKAVTDNYIVDEEQYLSELIKLVPSSDEAIERVTR
RAHELVNKVRQFDKKGLMVGIDAFLQQYSLETQEGIILMCLAEALLRIPDAATADALIED
KLSGAKWDEHLSKSDSVLVNASTWGLMLTGKIVKLDKKIDGTPSNLLSRLVNRLGEPVIR
QAMMAAMKIMGKQFVLGRTMKEALKNSEDKRKLGYTHSYDMLGEAALTRKDAEKYFNDYA
NAITELGAQSYNENESPRPTISIKLSALHPRYEVANEDRVLTELYDTVIRLIKLARGLNI
GISIDAEEVDRLELSLKLFQKLFNADATKGWGLLGIVVQAYSKRALPVLVWLTRLAKEQG
DEIPVRLVKGAYWDSELKWAQQAGEAAYPLYTRKAGTDVSYLACARYLLSDATRGAIYPQ
FASHNAQTVAAISDMAGDRNHEFQRLHGMGQELYDTILSEAGAKAVRIYAPIGAHKDLLP
YLVRRLLENGANTSFVHKLVDPKTPIESLVVHPLKTLTGYKTLANNKIVLPTDIFGSDRK
NSKGLNMNIISEAEPFFAALDKFKSTQWQAGPLVNGQTLTGEHKTVVSPFDTTQTVGQVA
FADKAAIEQAVASADAAFATWTRTPVEVRASALQKLADLLEENREELIALCTREAGKSIQ
DGIDEVREAVDFCRYYAVQAKKLMSKPELLPGPTGELNELFLQGRGVFVCISPWNFPLAI
FLGQVSAALAAGNTVVAKPAEQTSIIGYRAVQLAHQAGIPTDVLQYLPGTGATVGNALTA
DERIGGVCFTGSTGTAKLINRTLANREGAIIPLIAETGGQNAMVVDSTSQPEQVVNDVVS
SSFTSAGQRCSALRVLFLQEDIADRVIDVLQGAMDELVIGNPSSVKTDVGPVIDATAKAN
LDAHIDHIKQVGKLIKQMSLPAGTENGHFVSPTAVEIDSIKVLEKEHFGPILHVIRYKAS
ELAHVIDEINSTGFGLTLGIHSRNEGHALEVADKVNVGNVYINRNQIGAVVGVQPFGGQG
LSGTGPKAGGPHYLTRFVTEKTRTNNITAIGGNATLLSLGDSDA
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