SitesBLAST
Comparing GFF3021 FitnessBrowser__psRCH2:GFF3021 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)
51% identity, 97% coverage: 22:1042/1053 of query aligns to 6:983/983 of 3hazA
- active site: N652 (= N707), K675 (= K730), E752 (= E808), C786 (= C842), E878 (= E937), A960 (= A1019)
- binding flavin-adenine dinucleotide: D272 (= D296), A273 (= A297), Q306 (= Q330), R333 (= R357), V335 (= V359), K336 (= K360), G337 (= G361), A338 (= A362), Y339 (= Y363), W340 (= W364), F358 (≠ Y382), T359 (= T383), R360 (= R384), K361 (= K385), T364 (= T388), A387 (= A413), T388 (≠ S414), H389 (= H415), N390 (= N416), Y435 (= Y463), S460 (= S488), F461 (= F489)
- binding nicotinamide-adenine-dinucleotide: I648 (≠ V703), S649 (= S704), P650 (= P705), W651 (= W706), N652 (= N707), I657 (= I712), K675 (= K730), P676 (= P731), A677 (= A732), G708 (= G763), G711 (= G767), A712 (≠ G768), T726 (= T782), G727 (= G783), S728 (= S784), V731 (≠ T787), I735 (= I791), E752 (= E808), T753 (= T809), C786 (= C842), E878 (= E937), F880 (= F939), F948 (= F1007)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
51% identity, 97% coverage: 22:1040/1053 of query aligns to 6:972/973 of 6bsnA
- active site: N643 (= N707), E743 (= E808), A777 (≠ C842), A951 (= A1019)
- binding dihydroflavine-adenine dinucleotide: D269 (= D296), A270 (= A297), Q303 (= Q330), R330 (= R357), V332 (= V359), K333 (= K360), G334 (= G361), A335 (= A362), Y336 (= Y363), W337 (= W364), F355 (≠ Y382), T356 (= T383), R357 (= R384), K358 (= K385), T361 (= T388), A384 (= A413), T385 (≠ S414), H386 (= H415), N387 (= N416), Y432 (= Y463), S457 (= S488), F458 (= F489)
- binding proline: M630 (≠ H694), W642 (= W706), F644 (= F708), G718 (= G783), R776 (= R841), S778 (= S843), F871 (= F939), I930 (= I998), G931 (= G999), A932 (= A1000), F939 (= F1007), A958 (≠ L1026), R959 (= R1027), A961 (= A1029)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1036/1216 of 6x99A
- active site: N690 (= N707), K713 (= K730), E793 (= E808), C827 (= C842), E923 (= E937), A1005 (= A1019)
- binding d-proline: W557 (= W561), T558 (≠ Q562), E657 (= E661), F691 (= F708), R727 (≠ E744), R826 (= R841), S828 (= S843), G985 (= G999), A986 (= A1000), F993 (= F1007)
- binding flavin-adenine dinucleotide: D289 (= D296), A290 (= A297), V321 (= V328), R350 (= R357), V352 (= V359), K353 (= K360), G354 (= G361), A355 (= A362), Y356 (= Y363), W357 (= W364), F375 (≠ Y382), T376 (= T383), R377 (= R384), K378 (= K385), T381 (= T388), A404 (= A413), T405 (≠ S414), H406 (= H415), N407 (= N416), Q430 (= Q439), C431 (≠ R440), Y456 (= Y463), E475 (= E482), S481 (= S488), F482 (= F489)
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, 98% coverage: 23:1050/1053 of query aligns to 21:1038/1218 of 6x9dA
- active site: N692 (= N707), K715 (= K730), E795 (= E808), C829 (= C842), E925 (= E937), A1007 (= A1019)
- binding flavin-adenine dinucleotide: D291 (= D296), A292 (= A297), V323 (= V328), Q325 (= Q330), R352 (= R357), V354 (= V359), K355 (= K360), G356 (= G361), A357 (= A362), Y358 (= Y363), W359 (= W364), F377 (≠ Y382), T378 (= T383), R379 (= R384), K380 (= K385), T383 (= T388), A406 (= A413), T407 (≠ S414), H408 (= H415), N409 (= N416), Q432 (= Q439), C433 (≠ R440), E477 (= E482), S483 (= S488), F484 (= F489)
- binding 4-hydroxyproline: E659 (= E661), F693 (= F708), I697 (= I712), R828 (= R841), S830 (= S843), G987 (= G999), A988 (= A1000), F995 (= F1007)
- binding nicotinamide-adenine-dinucleotide: I688 (≠ V703), S689 (= S704), P690 (= P705), W691 (= W706), N692 (= N707), I697 (= I712), K715 (= K730), A717 (= A732), E718 (= E733), G748 (= G763), G751 (= G767), A752 (≠ G768), T766 (= T782), G767 (= G783), S768 (= S784), V771 (≠ T787), E795 (= E808), T796 (= T809), C829 (= C842), E925 (= E937), F927 (= F939), F995 (= F1007)
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, 98% coverage: 23:1050/1053 of query aligns to 21:1034/1214 of 6x9aA
- active site: N688 (= N707), K711 (= K730), E791 (= E808), C825 (= C842), E921 (= E937), A1003 (= A1019)
- binding flavin-adenine dinucleotide: D287 (= D296), A288 (= A297), V319 (= V328), R348 (= R357), V350 (= V359), K351 (= K360), G352 (= G361), A353 (= A362), Y354 (= Y363), W355 (= W364), F373 (≠ Y382), T374 (= T383), R375 (= R384), K376 (= K385), T379 (= T388), A402 (= A413), T403 (≠ S414), H404 (= H415), N405 (= N416), C429 (≠ R440), E473 (= E482), S479 (= S488), F480 (= F489)
- binding (4S)-4-hydroxy-D-proline: W555 (= W561), T556 (≠ Q562), E655 (= E661), F689 (= F708), R725 (≠ E744), S826 (= S843), G983 (= G999), A984 (= A1000), F991 (= F1007)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1037/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (≠ V703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), K714 (= K730), E717 (= E733), G747 (= G763), G750 (= G767), A751 (≠ G768), F764 (= F781), G766 (= G783), S767 (= S784), V770 (≠ T787), T795 (= T809), G796 (= G810), C828 (= C842), E924 (= E937), F926 (= F939)
- 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 (= K255), D290 (= D296), A291 (= A297), V322 (= V328), Q324 (= Q330), R351 (= R357), V353 (= V359), K354 (= K360), G355 (= G361), A356 (= A362), Y357 (= Y363), W358 (= W364), F376 (≠ Y382), T377 (= T383), R378 (= R384), K379 (= K385), T382 (= T388), A405 (= A413), T406 (≠ S414), H407 (= H415), N408 (= N416), Q431 (= Q439), C432 (≠ R440), L433 (= L441), Y457 (= Y463), S482 (= S488), F483 (= F489)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 20:1033/1209 of 6x9cA
- active site: N687 (= N707), K710 (= K730), E790 (= E808), C824 (= C842), E920 (= E937), A1002 (= A1019)
- binding dihydroflavine-adenine dinucleotide: D286 (= D296), A287 (= A297), V318 (= V328), Q320 (= Q330), R347 (= R357), V349 (= V359), K350 (= K360), G351 (= G361), A352 (= A362), Y353 (= Y363), W354 (= W364), F372 (≠ Y382), T373 (= T383), R374 (= R384), K375 (= K385), T378 (= T388), A401 (= A413), T402 (≠ S414), H403 (= H415), N404 (= N416), Q427 (= Q439), C428 (≠ R440), E472 (= E482), S478 (= S488), F479 (= F489)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (≠ V703), S684 (= S704), P685 (= P705), W686 (= W706), N687 (= N707), K710 (= K730), E713 (= E733), G743 (= G763), G746 (= G767), A747 (≠ G768), F760 (= F781), G762 (= G783), S763 (= S784), V766 (≠ T787), E920 (= E937), F922 (= F939)
- binding proline: R823 (= R841), C824 (= C842), S825 (= S843), G982 (= G999), A983 (= A1000), F990 (= F1007)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1037/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D296), A291 (= A297), V322 (= V328), Q324 (= Q330), R351 (= R357), V353 (= V359), K354 (= K360), G355 (= G361), A356 (= A362), Y357 (= Y363), W358 (= W364), F376 (≠ Y382), T377 (= T383), R378 (= R384), K379 (= K385), T382 (= T388), A405 (= A413), T406 (≠ S414), H407 (= H415), N408 (= N416), C432 (≠ R440), L433 (= L441), E476 (= E482), S482 (= S488), F483 (= F489)
- binding nicotinamide-adenine-dinucleotide: I687 (≠ V703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), I696 (= I712), K714 (= K730), E717 (= E733), G747 (= G763), G750 (= G767), T765 (= T782), G766 (= G783), S767 (= S784), V770 (≠ T787), I774 (= I791), E794 (= E808), T795 (= T809), C828 (= C842), E924 (= E937), F926 (= F939), F994 (= F1007)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K255), Y457 (= Y463), Y469 (= Y475), R472 (= R478), R473 (= R479)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K255), D290 (= D296), Y457 (= Y463), Y469 (= Y475), R472 (= R478), R473 (= R479)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1037/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (≠ V703), S688 (= S704), P689 (= P705), W690 (= W706), N691 (= N707), I696 (= I712), K714 (= K730), A716 (= A732), E717 (= E733), G747 (= G763), G750 (= G767), A751 (≠ G768), T765 (= T782), G766 (= G783), S767 (= S784), V770 (≠ T787), E794 (= E808), T795 (= T809), C828 (= C842), E924 (= E937), F926 (= F939), F994 (= F1007)
- 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 (= D296), A291 (= A297), V322 (= V328), Q324 (= Q330), V353 (= V359), K354 (= K360), G355 (= G361), A356 (= A362), W358 (= W364), F376 (≠ Y382), T377 (= T383), R378 (= R384), K379 (= K385), T382 (= T388), A405 (= A413), T406 (≠ S414), H407 (= H415), N408 (= N416), Q431 (= Q439), C432 (≠ R440), L433 (= L441), Y457 (= Y463), E476 (= E482)
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
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, 98% coverage: 23:1050/1053 of query aligns to 21:1034/1214 of 6x9bA
- active site: N688 (= N707), K711 (= K730), E791 (= E808), C825 (= C842), E921 (= E937), A1003 (= A1019)
- binding flavin-adenine dinucleotide: D287 (= D296), A288 (= A297), V319 (= V328), R348 (= R357), V350 (= V359), K351 (= K360), G352 (= G361), A353 (= A362), Y354 (= Y363), W355 (= W364), F373 (≠ Y382), T374 (= T383), R375 (= R384), K376 (= K385), T379 (= T388), A402 (= A413), T403 (≠ S414), H404 (= H415), N405 (= N416), Q428 (= Q439), C429 (≠ R440), Y454 (= Y463), E473 (= E482), S479 (= S488), F480 (= F489)
- binding nicotinamide-adenine-dinucleotide: I684 (≠ V703), S685 (= S704), P686 (= P705), W687 (= W706), N688 (= N707), I693 (= I712), K711 (= K730), A713 (= A732), E714 (= E733), G744 (= G763), G747 (= G767), A748 (≠ G768), T762 (= T782), G763 (= G783), S764 (= S784), V767 (≠ T787), I771 (= I791), E791 (= E808), T792 (= T809), C825 (= C842), E921 (= E937), F923 (= F939)
- binding (4R)-4-hydroxy-D-proline: E655 (= E661), F689 (= F708), S826 (= S843), G983 (= G999), A984 (= A1000), F991 (= F1007)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1036/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D296), A290 (= A297), V321 (= V328), Q323 (= Q330), R350 (= R357), V352 (= V359), K353 (= K360), G354 (= G361), A355 (= A362), Y356 (= Y363), W357 (= W364), F375 (≠ Y382), T376 (= T383), R377 (= R384), K378 (= K385), T381 (= T388), A404 (= A413), T405 (≠ S414), H406 (= H415), N407 (= N416), C431 (≠ R440), L432 (= L441), E475 (= E482), S481 (= S488), F482 (= F489)
- binding nicotinamide-adenine-dinucleotide: I686 (≠ V703), S687 (= S704), P688 (= P705), W689 (= W706), N690 (= N707), I695 (= I712), K713 (= K730), A715 (= A732), E716 (= E733), G746 (= G763), G749 (= G767), A750 (≠ G768), T764 (= T782), G765 (= G783), S766 (= S784), V769 (≠ T787), E793 (= E808), T794 (= T809), C827 (= C842), E923 (= E937), F925 (= F939), F993 (= F1007)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y463), Y468 (= Y475), R471 (= R478), R472 (= R479)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
48% identity, 98% coverage: 23:1050/1053 of query aligns to 21:1029/1207 of 5kf6A
- active site: N683 (= N707), K706 (= K730), E786 (= E808), C820 (= C842), E916 (= E937), A998 (= A1019)
- binding flavin-adenine dinucleotide: D282 (= D296), A283 (= A297), V314 (= V328), Q316 (= Q330), R343 (= R357), V345 (= V359), K346 (= K360), G347 (= G361), A348 (= A362), Y349 (= Y363), W350 (= W364), F368 (≠ Y382), T369 (= T383), R370 (= R384), K371 (= K385), T374 (= T388), A397 (= A413), T398 (≠ S414), H399 (= H415), N400 (= N416), Q423 (= Q439), C424 (≠ R440), L425 (= L441), E468 (= E482), S474 (= S488), F475 (= F489)
- binding nicotinamide-adenine-dinucleotide: I679 (≠ V703), S680 (= S704), P681 (= P705), W682 (= W706), N683 (= N707), I688 (= I712), K706 (= K730), A708 (= A732), E709 (= E733), G739 (= G763), G742 (= G767), A743 (≠ G768), F756 (= F781), T757 (= T782), G758 (= G783), S759 (= S784), V762 (≠ T787), I766 (= I791), E786 (= E808), T787 (= T809), C820 (= C842), E916 (= E937), F918 (= F939), F986 (= F1007)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K255), D282 (= D296), Y449 (= Y463), R464 (= R478), R465 (= R479)
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, 98% coverage: 23:1050/1053 of query aligns to 21:1019/1197 of 6ufpA
- active site: N673 (= N707), K696 (= K730), E776 (= E808), C810 (= C842), E906 (= E937), A988 (= A1019)
- binding dihydroflavine-adenine dinucleotide: D285 (= D296), A286 (= A297), V317 (= V328), Q319 (= Q330), R346 (= R357), V348 (= V359), K349 (= K360), G350 (= G361), A351 (= A362), W353 (= W364), F371 (≠ Y382), T372 (= T383), R373 (= R384), K374 (= K385), T377 (= T388), A400 (= A413), T401 (≠ S414), H402 (= H415), N403 (= N416), Q426 (= Q439), C427 (≠ R440), L428 (= L441), S464 (= S488)
- binding nicotinamide-adenine-dinucleotide: I669 (≠ V703), P671 (= P705), W672 (= W706), N673 (= N707), I678 (= I712), K696 (= K730), E699 (= E733), G729 (= G763), G732 (= G767), F746 (= F781), T747 (= T782), G748 (= G783), S749 (= S784), V752 (≠ T787), E776 (= E808), T777 (= T809), C810 (= C842), E906 (= E937), F908 (= F939)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K255), D285 (= D296), Y439 (= Y463), Y451 (= Y475), R454 (= R478), R455 (= R479)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
34% identity, 84% coverage: 159:1038/1053 of query aligns to 69:950/959 of 5ur2B
- active site: N618 (= N707), K641 (= K730), E722 (= E808), C756 (= C842), E851 (= E937), T931 (≠ A1019)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K255), D215 (= D296), M216 (≠ A297), Q249 (= Q330), V278 (= V359), K279 (= K360), G280 (= G361), A281 (= A362), W283 (= W364), Y300 (= Y382), T301 (= T383), N302 (≠ R384), K303 (= K385), S306 (≠ T388), A329 (= A413), S330 (= S414), H331 (= H415), N332 (= N416), Q356 (= Q439), M357 (≠ R440), L358 (= L441), Y379 (= Y463), E398 (= E482), E403 (≠ S487), W405 (≠ F489)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
48% identity, 48% coverage: 23:525/1053 of query aligns to 7:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K255), Y433 (= Y463), R448 (= R478), R449 (= R479)
- binding flavin-adenine dinucleotide: D263 (= D296), A264 (= A297), V295 (= V328), Q297 (= Q330), R324 (= R357), V326 (= V359), K327 (= K360), G328 (= G361), A329 (= A362), Y330 (= Y363), W331 (= W364), Y349 (= Y382), T350 (= T383), R351 (= R384), K352 (= K385), T355 (= T388), A378 (= A413), T379 (≠ S414), H380 (= H415), N381 (= N416), C405 (≠ R440), L406 (= L441), E452 (= E482), S458 (= S488)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
48% identity, 48% coverage: 23:525/1053 of query aligns to 7:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D296), A260 (= A297), V291 (= V328), Q293 (= Q330), R320 (= R357), V322 (= V359), K323 (= K360), G324 (= G361), A325 (= A362), Y326 (= Y363), W327 (= W364), Y345 (= Y382), T346 (= T383), R347 (= R384), K348 (= K385), T351 (= T388), A374 (= A413), T375 (≠ S414), H376 (= H415), N377 (= N416), C401 (≠ R440), L402 (= L441), E448 (= E482), S454 (= S488)
- binding cyclopropanecarboxylic acid: K218 (= K255), Y429 (= Y463), Y441 (= Y475), R444 (= R478), R445 (= R479)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
48% identity, 48% coverage: 23:525/1053 of query aligns to 7:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D296), A260 (= A297), V291 (= V328), Q293 (= Q330), R320 (= R357), V322 (= V359), K323 (= K360), G324 (= G361), A325 (= A362), Y326 (= Y363), W327 (= W364), Y345 (= Y382), T346 (= T383), R347 (= R384), K348 (= K385), T351 (= T388), A374 (= A413), T375 (≠ S414), H376 (= H415), N377 (= N416), C401 (≠ R440), L402 (= L441), E448 (= E482), S454 (= S488)
- binding cyclobutanecarboxylic acid: K218 (= K255), L402 (= L441), Y429 (= Y463), Y441 (= Y475), R444 (= R478), R445 (= R479)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
48% identity, 48% coverage: 23:525/1053 of query aligns to 7:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D296), A260 (= A297), V291 (= V328), Q293 (= Q330), R320 (= R357), V322 (= V359), K323 (= K360), G324 (= G361), A325 (= A362), Y326 (= Y363), W327 (= W364), Y345 (= Y382), T346 (= T383), R347 (= R384), K348 (= K385), T351 (= T388), A374 (= A413), T375 (≠ S414), H376 (= H415), N377 (= N416), C401 (≠ R440), L402 (= L441), E448 (= E482), S454 (= S488)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K255), Y326 (= Y363), Y429 (= Y463), Y441 (= Y475), R444 (= R478), R445 (= R479)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
47% identity, 48% coverage: 23:525/1053 of query aligns to 8:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A297), V283 (= V328), Q285 (= Q330), R312 (= R357), V314 (= V359), K315 (= K360), G316 (= G361), A317 (= A362), Y318 (= Y363), W319 (= W364), Y337 (= Y382), T338 (= T383), R339 (= R384), K340 (= K385), T343 (= T388), A366 (= A413), T367 (≠ S414), H368 (= H415), N369 (= N416), C393 (≠ R440), L394 (= L441), E440 (= E482), S446 (= S488), F447 (= F489)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K255), Y421 (= Y463), R436 (= R478), R437 (= R479)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
34% identity, 82% coverage: 182:1042/1053 of query aligns to 97:966/977 of 4nmaA
- active site: N629 (= N707), K652 (= K730), E733 (= E808), C767 (= C842), E863 (≠ H938), A943 (= A1019)
- binding flavin-adenine dinucleotide: D226 (= D296), M227 (≠ A297), Q258 (= Q330), R285 (= R357), V287 (= V359), K288 (= K360), G289 (= G361), A290 (= A362), Y291 (= Y363), W292 (= W364), W309 (≠ Y382), T310 (= T383), I311 (≠ R384), K312 (= K385), S315 (≠ T388), A338 (= A413), S339 (= S414), H340 (= H415), N341 (= N416), Q365 (= Q439), L367 (= L441), E407 (= E482), S413 (= S488), F414 (= F489)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K255), Y388 (= Y463), Y400 (= Y475), R403 (= R478), R404 (= R479)
Query Sequence
>GFF3021 FitnessBrowser__psRCH2:GFF3021
MFKAGHVLDGAFANQKAAEFFPAISANYSVDEAQYLTELLQLADPGEAGIAAIRERARSL
IEAVRGRDNAVDTLDALLRQYSLDTQEGLMLMCLAEALLRVPDAATADALIRDKLNAAEW
ERHLGQSDNVLVNFAAWGLVMTGKVVDPETADGRPKNVIGRLLKRSGEPVIRGAMNQAMK
LMGKQFVLGRTISEALKNGRPEREKGYTYSFDMLGEAALTAEDAAKYMADYRQAVETVGA
EPQVGKGPRPSVSIKLSALHPRYELAQRERVLTELFGSVRELAILARRLNVGITIDAEEA
DRLELSLELYEKLLRDPAIAGWGEFGLVIQAYSKRCLPVLVWLTLLGRELGERIPLRLVK
GAYWDSEIKQCQVQGLDGYPVYTRKEGTDTSYLACARYLLSEHTRGVIYPQFASHNAHTV
SCILAMAEETAQPREFEFQRLHGMGDALYDTVIEKYARNVRIYAPVGAHKDLLPYLVRRL
LENGANSSFVHQLVDPRVPVESLIDHPVTQLRRFAAPGNPRIPLPPALFGNRKNSQGINM
NIQNQWTELASAYQPFLERQWQAAPVISGRTLAGTPSEVRCPYELNKVVGQAQFASADQA
RQAIDRLAAYWPIWNATPVEARAAVLERLGDLLEQHRAELMALCTVEAGKSLQDGIDEVR
EAVDFCRYYAQQARLKLGREELKGPTGERNELFHEGRGVFVCVSPWNFPLAIYLGQITAA
LVAGNTVLAKPAEQTSLIAARALELMFEAGLPQEAIAFLPGDGATLGGVFCRDPRVVGVC
FTGSTDTARIINRQLAEKEGPIATLIAETGGQNAMIVDSTALPEQVIKDAVGSAFTSAGQ
RCSALRVLYVQRDIADRVIDLLKGAMAELRVGPTHLRENDIGPVIDQEAREGLLAHIQQL
KSEGRLIAEATVPAGLNGHFVAPVAFEIDGIHQLKKEHFGPVLHVVRYDAADLEKVVAAI
NGTGYGLTLGVHSRNEETAERIEQLARVGNLYVNRNQIGAVVGVQPFGGCRLSGTGPKAG
GPSYLLRFANERTTSTNTTAVGGNASLLSLGDD
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