SitesBLAST
Comparing Ga0059261_3926 FitnessBrowser__Korea:Ga0059261_3926 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)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), K714 (= K712), E717 (= E715), G747 (= G745), G750 (= G748), A751 (= A749), F764 (= F762), G766 (= G764), S767 (= S765), V770 (= V768), T795 (= T793), G796 (= G794), C828 (= C826), E924 (= E922), F926 (= F924)
- 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 (= K252), D290 (= D293), A291 (= A294), V322 (= V325), Q324 (= Q327), R351 (= R354), V353 (= V356), K354 (= K357), G355 (= G358), A356 (= A359), Y357 (= Y360), W358 (= W361), F376 (≠ Y379), T377 (= T380), R378 (= R381), K379 (= K382), T382 (= T385), A405 (= A408), T406 (= T409), H407 (= H410), N408 (= N411), Q431 (= Q434), C432 (= C435), L433 (= L436), Y457 (= Y460), S482 (= S485), F483 (= F486)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1217/1218 of 6x9dA
- active site: N692 (= N689), K715 (= K712), E795 (= E792), C829 (= C826), E925 (= E922), A1007 (= A1004)
- binding flavin-adenine dinucleotide: D291 (= D293), A292 (= A294), V323 (= V325), Q325 (= Q327), R352 (= R354), V354 (= V356), K355 (= K357), G356 (= G358), A357 (= A359), Y358 (= Y360), W359 (= W361), F377 (≠ Y379), T378 (= T380), R379 (= R381), K380 (= K382), T383 (= T385), A406 (= A408), T407 (= T409), H408 (= H410), N409 (= N411), Q432 (= Q434), C433 (= C435), E477 (= E479), S483 (= S485), F484 (= F486)
- binding 4-hydroxyproline: E659 (= E656), F693 (= F690), I697 (= I694), R828 (= R825), S830 (= S827), G987 (= G984), A988 (= A985), F995 (= F992)
- binding nicotinamide-adenine-dinucleotide: I688 (= I685), S689 (= S686), P690 (= P687), W691 (= W688), N692 (= N689), I697 (= I694), K715 (= K712), A717 (= A714), E718 (= E715), G748 (= G745), G751 (= G748), A752 (= A749), T766 (= T763), G767 (= G764), S768 (= S765), V771 (= V768), E795 (= E792), T796 (= T793), C829 (= C826), E925 (= E922), F927 (= F924), F995 (= F992)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1216/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D293), A291 (= A294), V322 (= V325), Q324 (= Q327), R351 (= R354), V353 (= V356), K354 (= K357), G355 (= G358), A356 (= A359), Y357 (= Y360), W358 (= W361), F376 (≠ Y379), T377 (= T380), R378 (= R381), K379 (= K382), T382 (= T385), A405 (= A408), T406 (= T409), H407 (= H410), N408 (= N411), C432 (= C435), L433 (= L436), E476 (= E479), S482 (= S485), F483 (= F486)
- binding nicotinamide-adenine-dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), I696 (= I694), K714 (= K712), E717 (= E715), G747 (= G745), G750 (= G748), T765 (= T763), G766 (= G764), S767 (= S765), V770 (= V768), I774 (= I772), E794 (= E792), T795 (= T793), C828 (= C826), E924 (= E922), F926 (= F924), F994 (= F992)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K252), Y457 (= Y460), Y469 (= Y472), R472 (= R475), R473 (= R476)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K252), D290 (= D293), Y457 (= Y460), Y469 (= Y472), R472 (= R475), R473 (= R476)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1216/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I685), S688 (= S686), P689 (= P687), W690 (= W688), N691 (= N689), I696 (= I694), K714 (= K712), A716 (= A714), E717 (= E715), G747 (= G745), G750 (= G748), A751 (= A749), T765 (= T763), G766 (= G764), S767 (= S765), V770 (= V768), E794 (= E792), T795 (= T793), C828 (= C826), E924 (= E922), F926 (= F924), F994 (= F992)
- 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 (= D293), A291 (= A294), V322 (= V325), Q324 (= Q327), V353 (= V356), K354 (= K357), G355 (= G358), A356 (= A359), W358 (= W361), F376 (≠ Y379), T377 (= T380), R378 (= R381), K379 (= K382), T382 (= T385), A405 (= A408), T406 (= T409), H407 (= H410), N408 (= N411), Q431 (= Q434), C432 (= C435), L433 (= L436), Y457 (= Y460), E476 (= E479)
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
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1215/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D293), A290 (= A294), V321 (= V325), Q323 (= Q327), R350 (= R354), V352 (= V356), K353 (= K357), G354 (= G358), A355 (= A359), Y356 (= Y360), W357 (= W361), F375 (≠ Y379), T376 (= T380), R377 (= R381), K378 (= K382), T381 (= T385), A404 (= A408), T405 (= T409), H406 (= H410), N407 (= N411), C431 (= C435), L432 (= L436), E475 (= E479), S481 (= S485), F482 (= F486)
- binding nicotinamide-adenine-dinucleotide: I686 (= I685), S687 (= S686), P688 (= P687), W689 (= W688), N690 (= N689), I695 (= I694), K713 (= K712), A715 (= A714), E716 (= E715), G746 (= G745), G749 (= G748), A750 (= A749), T764 (= T763), G765 (= G764), S766 (= S765), V769 (= V768), E793 (= E792), T794 (= T793), C827 (= C826), E923 (= E922), F925 (= F924), F993 (= F992)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y460), Y468 (= Y472), R471 (= R475), R472 (= R476)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1215/1216 of 6x99A
- active site: N690 (= N689), K713 (= K712), E793 (= E792), C827 (= C826), E923 (= E922), A1005 (= A1004)
- binding d-proline: W557 (= W560), T558 (≠ A561), E657 (= E656), F691 (= F690), R727 (≠ S726), R826 (= R825), S828 (= S827), G985 (= G984), A986 (= A985), F993 (= F992)
- binding flavin-adenine dinucleotide: D289 (= D293), A290 (= A294), V321 (= V325), R350 (= R354), V352 (= V356), K353 (= K357), G354 (= G358), A355 (= A359), Y356 (= Y360), W357 (= W361), F375 (≠ Y379), T376 (= T380), R377 (= R381), K378 (= K382), T381 (= T385), A404 (= A408), T405 (= T409), H406 (= H410), N407 (= N411), Q430 (= Q434), C431 (= C435), Y456 (= Y460), E475 (= E479), S481 (= S485), F482 (= F486)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1213/1214 of 6x9bA
- active site: N688 (= N689), K711 (= K712), E791 (= E792), C825 (= C826), E921 (= E922), A1003 (= A1004)
- binding flavin-adenine dinucleotide: D287 (= D293), A288 (= A294), V319 (= V325), R348 (= R354), V350 (= V356), K351 (= K357), G352 (= G358), A353 (= A359), Y354 (= Y360), W355 (= W361), F373 (≠ Y379), T374 (= T380), R375 (= R381), K376 (= K382), T379 (= T385), A402 (= A408), T403 (= T409), H404 (= H410), N405 (= N411), Q428 (= Q434), C429 (= C435), Y454 (= Y460), E473 (= E479), S479 (= S485), F480 (= F486)
- binding nicotinamide-adenine-dinucleotide: I684 (= I685), S685 (= S686), P686 (= P687), W687 (= W688), N688 (= N689), I693 (= I694), K711 (= K712), A713 (= A714), E714 (= E715), G744 (= G745), G747 (= G748), A748 (= A749), T762 (= T763), G763 (= G764), S764 (= S765), V767 (= V768), I771 (= I772), E791 (= E792), T792 (= T793), C825 (= C826), E921 (= E922), F923 (= F924)
- binding (4R)-4-hydroxy-D-proline: E655 (= E656), F689 (= F690), S826 (= S827), G983 (= G984), A984 (= A985), F991 (= F992)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
74% identity, 100% coverage: 3:1198/1199 of query aligns to 3:1213/1214 of 6x9aA
- active site: N688 (= N689), K711 (= K712), E791 (= E792), C825 (= C826), E921 (= E922), A1003 (= A1004)
- binding flavin-adenine dinucleotide: D287 (= D293), A288 (= A294), V319 (= V325), R348 (= R354), V350 (= V356), K351 (= K357), G352 (= G358), A353 (= A359), Y354 (= Y360), W355 (= W361), F373 (≠ Y379), T374 (= T380), R375 (= R381), K376 (= K382), T379 (= T385), A402 (= A408), T403 (= T409), H404 (= H410), N405 (= N411), C429 (= C435), E473 (= E479), S479 (= S485), F480 (= F486)
- binding (4S)-4-hydroxy-D-proline: W555 (= W560), T556 (≠ A561), E655 (= E656), F689 (= F690), R725 (≠ S726), S826 (= S827), G983 (= G984), A984 (= A985), F991 (= F992)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
74% identity, 99% coverage: 3:1195/1199 of query aligns to 2:1209/1209 of 6x9cA
- active site: N687 (= N689), K710 (= K712), E790 (= E792), C824 (= C826), E920 (= E922), A1002 (= A1004)
- binding dihydroflavine-adenine dinucleotide: D286 (= D293), A287 (= A294), V318 (= V325), Q320 (= Q327), R347 (= R354), V349 (= V356), K350 (= K357), G351 (= G358), A352 (= A359), Y353 (= Y360), W354 (= W361), F372 (≠ Y379), T373 (= T380), R374 (= R381), K375 (= K382), T378 (= T385), A401 (= A408), T402 (= T409), H403 (= H410), N404 (= N411), Q427 (= Q434), C428 (= C435), E472 (= E479), S478 (= S485), F479 (= F486)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I685), S684 (= S686), P685 (= P687), W686 (= W688), N687 (= N689), K710 (= K712), E713 (= E715), G743 (= G745), G746 (= G748), A747 (= A749), F760 (= F762), G762 (= G764), S763 (= S765), V766 (= V768), E920 (= E922), F922 (= F924)
- binding proline: R823 (= R825), C824 (= C826), S825 (= S827), G982 (= G984), A983 (= A985), F990 (= F992)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
74% identity, 100% coverage: 3:1197/1199 of query aligns to 3:1207/1207 of 5kf6A
- active site: N683 (= N689), K706 (= K712), E786 (= E792), C820 (= C826), E916 (= E922), A998 (= A1004)
- binding flavin-adenine dinucleotide: D282 (= D293), A283 (= A294), V314 (= V325), Q316 (= Q327), R343 (= R354), V345 (= V356), K346 (= K357), G347 (= G358), A348 (= A359), Y349 (= Y360), W350 (= W361), F368 (≠ Y379), T369 (= T380), R370 (= R381), K371 (= K382), T374 (= T385), A397 (= A408), T398 (= T409), H399 (= H410), N400 (= N411), Q423 (= Q434), C424 (= C435), L425 (= L436), E468 (= E479), S474 (= S485), F475 (= F486)
- binding nicotinamide-adenine-dinucleotide: I679 (= I685), S680 (= S686), P681 (= P687), W682 (= W688), N683 (= N689), I688 (= I694), K706 (= K712), A708 (= A714), E709 (= E715), G739 (= G745), G742 (= G748), A743 (= A749), F756 (= F762), T757 (= T763), G758 (= G764), S759 (= S765), V762 (= V768), I766 (= I772), E786 (= E792), T787 (= T793), C820 (= C826), E916 (= E922), F918 (= F924), F986 (= F992)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K252), D282 (= D293), Y449 (= Y460), R464 (= R475), R465 (= R476)
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)
73% identity, 100% coverage: 3:1197/1199 of query aligns to 3:1197/1197 of 6ufpA
- active site: N673 (= N689), K696 (= K712), E776 (= E792), C810 (= C826), E906 (= E922), A988 (= A1004)
- binding dihydroflavine-adenine dinucleotide: D285 (= D293), A286 (= A294), V317 (= V325), Q319 (= Q327), R346 (= R354), V348 (= V356), K349 (= K357), G350 (= G358), A351 (= A359), W353 (= W361), F371 (≠ Y379), T372 (= T380), R373 (= R381), K374 (= K382), T377 (= T385), A400 (= A408), T401 (= T409), H402 (= H410), N403 (= N411), Q426 (= Q434), C427 (= C435), L428 (= L436), S464 (= S485)
- binding nicotinamide-adenine-dinucleotide: I669 (= I685), P671 (= P687), W672 (= W688), N673 (= N689), I678 (= I694), K696 (= K712), E699 (= E715), G729 (= G745), G732 (= G748), F746 (= F762), T747 (= T763), G748 (= G764), S749 (= S765), V752 (= V768), E776 (= E792), T777 (= T793), C810 (= C826), E906 (= E922), F908 (= F924)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K252), D285 (= D293), Y439 (= Y460), Y451 (= Y472), R454 (= R475), R455 (= R476)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
50% identity, 81% coverage: 49:1019/1199 of query aligns to 33:975/983 of 3hazA
- active site: N652 (= N689), K675 (= K712), E752 (= E792), C786 (= C826), E878 (= E922), A960 (= A1004)
- binding flavin-adenine dinucleotide: D272 (= D293), A273 (= A294), Q306 (= Q327), R333 (= R354), V335 (= V356), K336 (= K357), G337 (= G358), A338 (= A359), Y339 (= Y360), W340 (= W361), F358 (≠ Y379), T359 (= T380), R360 (= R381), K361 (= K382), T364 (= T385), A387 (= A408), T388 (= T409), H389 (= H410), N390 (= N411), Y435 (= Y460), S460 (= S485), F461 (= F486)
- binding nicotinamide-adenine-dinucleotide: I648 (= I685), S649 (= S686), P650 (= P687), W651 (= W688), N652 (= N689), I657 (= I694), K675 (= K712), P676 (= P713), A677 (= A714), G708 (= G745), G711 (= G748), A712 (= A749), T726 (= T763), G727 (= G764), S728 (= S765), V731 (= V768), I735 (= I772), E752 (= E792), T753 (= T793), C786 (= C826), E878 (= E922), F880 (= F924), F948 (= F992)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
50% identity, 81% coverage: 49:1019/1199 of query aligns to 33:966/973 of 6bsnA
- active site: N643 (= N689), E743 (= E792), A777 (≠ C826), A951 (= A1004)
- binding dihydroflavine-adenine dinucleotide: D269 (= D293), A270 (= A294), Q303 (= Q327), R330 (= R354), V332 (= V356), K333 (= K357), G334 (= G358), A335 (= A359), Y336 (= Y360), W337 (= W361), F355 (≠ Y379), T356 (= T380), R357 (= R381), K358 (= K382), T361 (= T385), A384 (= A408), T385 (= T409), H386 (= H410), N387 (= N411), Y432 (= Y460), S457 (= S485), F458 (= F486)
- binding proline: M630 (≠ H676), W642 (= W688), F644 (= F690), G718 (= G764), R776 (= R825), S778 (= S827), F871 (= F924), I930 (= I983), G931 (= G984), A932 (= A985), F939 (= F992), A958 (≠ G1011), R959 (= R1012), A961 (≠ V1014)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
65% identity, 43% coverage: 15:524/1199 of query aligns to 1:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K252), Y433 (= Y460), R448 (= R475), R449 (= R476)
- binding flavin-adenine dinucleotide: D263 (= D293), A264 (= A294), V295 (= V325), Q297 (= Q327), R324 (= R354), V326 (= V356), K327 (= K357), G328 (= G358), A329 (= A359), Y330 (= Y360), W331 (= W361), Y349 (= Y379), T350 (= T380), R351 (= R381), K352 (= K382), T355 (= T385), A378 (= A408), T379 (= T409), H380 (= H410), N381 (= N411), C405 (= C435), L406 (= L436), E452 (= E479), S458 (= S485)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
64% identity, 43% coverage: 15:524/1199 of query aligns to 1:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D293), A260 (= A294), V291 (= V325), Q293 (= Q327), R320 (= R354), V322 (= V356), K323 (= K357), G324 (= G358), A325 (= A359), Y326 (= Y360), W327 (= W361), Y345 (= Y379), T346 (= T380), R347 (= R381), K348 (= K382), T351 (= T385), A374 (= A408), T375 (= T409), H376 (= H410), N377 (= N411), C401 (= C435), L402 (= L436), E448 (= E479), S454 (= S485)
- binding cyclopropanecarboxylic acid: K218 (= K252), Y429 (= Y460), Y441 (= Y472), R444 (= R475), R445 (= R476)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
64% identity, 43% coverage: 15:524/1199 of query aligns to 1:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D293), A260 (= A294), V291 (= V325), Q293 (= Q327), R320 (= R354), V322 (= V356), K323 (= K357), G324 (= G358), A325 (= A359), Y326 (= Y360), W327 (= W361), Y345 (= Y379), T346 (= T380), R347 (= R381), K348 (= K382), T351 (= T385), A374 (= A408), T375 (= T409), H376 (= H410), N377 (= N411), C401 (= C435), L402 (= L436), E448 (= E479), S454 (= S485)
- binding cyclobutanecarboxylic acid: K218 (= K252), L402 (= L436), Y429 (= Y460), Y441 (= Y472), R444 (= R475), R445 (= R476)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
64% identity, 43% coverage: 15:524/1199 of query aligns to 1:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D293), A260 (= A294), V291 (= V325), Q293 (= Q327), R320 (= R354), V322 (= V356), K323 (= K357), G324 (= G358), A325 (= A359), Y326 (= Y360), W327 (= W361), Y345 (= Y379), T346 (= T380), R347 (= R381), K348 (= K382), T351 (= T385), A374 (= A408), T375 (= T409), H376 (= H410), N377 (= N411), C401 (= C435), L402 (= L436), E448 (= E479), S454 (= S485)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K252), Y326 (= Y360), Y429 (= Y460), Y441 (= Y472), R444 (= R475), R445 (= R476)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
63% identity, 43% coverage: 14:524/1199 of query aligns to 1:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A294), V283 (= V325), Q285 (= Q327), R312 (= R354), V314 (= V356), K315 (= K357), G316 (= G358), A317 (= A359), Y318 (= Y360), W319 (= W361), Y337 (= Y379), T338 (= T380), R339 (= R381), K340 (= K382), T343 (= T385), A366 (= A408), T367 (= T409), H368 (= H410), N369 (= N411), C393 (= C435), L394 (= L436), E440 (= E479), S446 (= S485), F447 (= F486)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K252), Y421 (= Y460), R436 (= R475), R437 (= R476)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
60% identity, 43% coverage: 15:524/1199 of query aligns to 1:467/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D293), A230 (= A294), V261 (= V325), Q263 (= Q327), R290 (= R354), V292 (= V356), K293 (= K357), G294 (= G358), A295 (= A359), Y296 (= Y360), W297 (= W361), Y315 (= Y379), T316 (= T380), R317 (= R381), K318 (= K382), T321 (= T385), A344 (= A408), T345 (= T409), H346 (= H410), N347 (= N411), Q370 (= Q434), C371 (= C435), L372 (= L436), E418 (= E479), S424 (= S485)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
60% identity, 43% coverage: 15:524/1199 of query aligns to 1:466/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D293), A229 (= A294), V260 (= V325), Q262 (= Q327), V291 (= V356), K292 (= K357), G293 (= G358), A294 (= A359), Y295 (= Y360), W296 (= W361), Y314 (= Y379), T315 (= T380), R316 (= R381), K317 (= K382), T320 (= T385), A343 (= A408), T344 (= T409), H345 (= H410), N346 (= N411), C370 (= C435), L371 (= L436), E417 (= E479), S423 (= S485), F424 (= F486)
- binding proline: K187 (= K252), L371 (= L436), Y410 (= Y472), R413 (= R475), R414 (= R476)
Query Sequence
>Ga0059261_3926 FitnessBrowser__Korea:Ga0059261_3926
MTAPFADFAPPIRPQTPLRSAITAAYRRPEPECVPPLVEQASLPEGTREAARITASTLIT
ALRAKHKGTGVEGLVQEYALSSQEGVALMCLAEALLRIPDDATRDALIRDKIADGDWKSH
IGDGRSLFVNAATWGLVVTGKLTGSVNDAGLGAALTRLIARAGEPVIRRGVDMAMRMMGE
QFVTGETIAEALKRARTLEARGFQYSYDMLGEAATTMADADRYYRDYENAVRAIGEASAG
RGVVGGPGISIKLSALHPRYARAQAGRVMDELLPKVKALAVLARGYDIGFNIDAEEADRL
ELSLDLLESLALDPDLKGWDGLGFVVQAYGKRCPFVIDWIVDLAQRADRRIMVRLVKGAY
WDAEIKRAQVDGLPDFPVYTRKIYTDVAYIACARKLLANRDRIFPQFATHNAQTLATIYQ
MAGPDFSVGDYEFQCLHGMGEPLYDEVVGATKLNRPCRIYAPVGTHETLLAYLVRRLLEN
GANSSFVNRIADPEVSIAELVADPVDQVRSMDVVGAKHPLIALPTGLYGARRNSEGLDLS
NENVLAELAASLKVSAAAGWAAEPADRIGTSRPVYNPADGKDVVGTVVEVTPEAAQTAVA
TAQAAAADWAAVAPAERAACLDRAADIMQDRMQILMGLIIREAGKSAPNAIAEVREAIDF
LRYYAEQARAMLGAAHKPLGAVTCISPWNFPLAIFTGQVAAALVAGNTVLAKPAEETPLI
AAQGVSILHEAGIPAAALQLVPGDGRIGAALVAAPGTQAVMFTGSTEVARIIQKELAKRL
TDGGDPVPFIAETGGQNAMIVDSSALAEQVVGDVIASAFDSAGQRCSALRVLCLQDDVAD
RILVMLKGALHELSIGRTDSLSTDIGPVITAEAKANIEGHIARMLGMGRGVEQIELAGET
AQGTFVPPTIIELQSIADLEREVFGPVLHVVRYKRRDLDRVIDAINATGYGLTFGLHTRL
DETIAHVSQRVEAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVQTATVP
PGVASDTSDPALRDFALWLGEQGEAARAAGEASLLGAEVELPGPVGERNIYALHPRGSVL
LLPKTREGLIAQVSAALATGNRAVIGNTALRGELAGLPERVAARLSWADDWRKAGPYGGA
LIEGDAAARSAALAEIAALPGPIVLAQAGTPRLDWLVEEVSTSVNTTAAGGNASLMAVA
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