SitesBLAST
Comparing Ac3H11_2850 FitnessBrowser__acidovorax_3H11:Ac3H11_2850 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)
60% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1218/1218 of 6x9dA
- active site: N692 (= N722), K715 (= K745), E795 (= E826), C829 (= C860), E925 (= E958), A1007 (= A1040)
- binding flavin-adenine dinucleotide: D291 (= D304), A292 (= A305), V323 (= V336), Q325 (= Q338), R352 (= R365), V354 (= V367), K355 (= K368), G356 (= G369), A357 (= A370), Y358 (= Y371), W359 (= W372), F377 (≠ Y390), T378 (= T391), R379 (= R392), K380 (= K393), T383 (= T396), A406 (= A419), T407 (= T420), H408 (= H421), N409 (= N422), Q432 (= Q445), C433 (= C446), E477 (= E502), S483 (= S508), F484 (= F509)
- binding 4-hydroxyproline: E659 (= E688), F693 (= F723), I697 (= I727), R828 (= R859), S830 (= S861), G987 (= G1020), A988 (= A1021), F995 (= F1028)
- binding nicotinamide-adenine-dinucleotide: I688 (= I718), S689 (= S719), P690 (= P720), W691 (= W721), N692 (= N722), I697 (= I727), K715 (= K745), A717 (= A747), E718 (= E748), G748 (= G778), G751 (= G782), A752 (= A783), T766 (= T797), G767 (= G798), S768 (= S799), V771 (= V802), E795 (= E826), T796 (= T827), C829 (= C860), E925 (= E958), F927 (= F960), F995 (= F1028)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1216/1216 of 6x99A
- active site: N690 (= N722), K713 (= K745), E793 (= E826), C827 (= C860), E923 (= E958), A1005 (= A1040)
- binding d-proline: W557 (= W588), T558 (= T589), E657 (= E688), F691 (= F723), R727 (= R759), R826 (= R859), S828 (= S861), G985 (= G1020), A986 (= A1021), F993 (= F1028)
- binding flavin-adenine dinucleotide: D289 (= D304), A290 (= A305), V321 (= V336), R350 (= R365), V352 (= V367), K353 (= K368), G354 (= G369), A355 (= A370), Y356 (= Y371), W357 (= W372), F375 (≠ Y390), T376 (= T391), R377 (= R392), K378 (= K393), T381 (= T396), A404 (= A419), T405 (= T420), H406 (= H421), N407 (= N422), Q430 (= Q445), C431 (= C446), Y456 (= Y483), E475 (= E502), S481 (= S508), F482 (= F509)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
60% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D304), A291 (= A305), V322 (= V336), Q324 (= Q338), R351 (= R365), V353 (= V367), K354 (= K368), G355 (= G369), A356 (= A370), Y357 (= Y371), W358 (= W372), F376 (≠ Y390), T377 (= T391), R378 (= R392), K379 (= K393), T382 (= T396), A405 (= A419), T406 (= T420), H407 (= H421), N408 (= N422), C432 (= C446), L433 (= L447), E476 (= E502), S482 (= S508), F483 (= F509)
- binding nicotinamide-adenine-dinucleotide: I687 (= I718), S688 (= S719), P689 (= P720), W690 (= W721), N691 (= N722), I696 (= I727), K714 (= K745), E717 (= E748), G747 (= G778), G750 (= G782), T765 (= T797), G766 (= G798), S767 (= S799), V770 (= V802), I774 (≠ L806), E794 (= E826), T795 (= T827), C828 (= C860), E924 (= E958), F926 (= F960), F994 (= F1028)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K263), Y457 (= Y483), Y469 (= Y495), R472 (= R498), R473 (= R499)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K263), D290 (= D304), Y457 (= Y483), Y469 (= Y495), R472 (= R498), R473 (= R499)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
60% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I718), S688 (= S719), P689 (= P720), W690 (= W721), N691 (= N722), I696 (= I727), K714 (= K745), A716 (= A747), E717 (= E748), G747 (= G778), G750 (= G782), A751 (= A783), T765 (= T797), G766 (= G798), S767 (= S799), V770 (= V802), E794 (= E826), T795 (= T827), C828 (= C860), E924 (= E958), F926 (= F960), F994 (= F1028)
- 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 (= D304), A291 (= A305), V322 (= V336), Q324 (= Q338), V353 (= V367), K354 (= K368), G355 (= G369), A356 (= A370), W358 (= W372), F376 (≠ Y390), T377 (= T391), R378 (= R392), K379 (= K393), T382 (= T396), A405 (= A419), T406 (= T420), H407 (= H421), N408 (= N422), Q431 (= Q445), C432 (= C446), L433 (= L447), Y457 (= Y483), E476 (= E502), G1217 (= G1261)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
59% identity, 100% coverage: 6:1260/1261 of query aligns to 3:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I718), S688 (= S719), P689 (= P720), W690 (= W721), N691 (= N722), K714 (= K745), E717 (= E748), G747 (= G778), G750 (= G782), A751 (= A783), F764 (= F796), G766 (= G798), S767 (= S799), V770 (= V802), T795 (= T827), G796 (= G828), C828 (= C860), E924 (= E958), F926 (= F960)
- 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 (= K263), D290 (= D304), A291 (= A305), V322 (= V336), Q324 (= Q338), R351 (= R365), V353 (= V367), K354 (= K368), G355 (= G369), A356 (= A370), Y357 (= Y371), W358 (= W372), F376 (≠ Y390), T377 (= T391), R378 (= R392), K379 (= K393), T382 (= T396), A405 (= A419), T406 (= T420), H407 (= H421), N408 (= N422), Q431 (= Q445), C432 (= C446), L433 (= L447), Y457 (= Y483), S482 (= S508), F483 (= F509)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
59% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D304), A290 (= A305), V321 (= V336), Q323 (= Q338), R350 (= R365), V352 (= V367), K353 (= K368), G354 (= G369), A355 (= A370), Y356 (= Y371), W357 (= W372), F375 (≠ Y390), T376 (= T391), R377 (= R392), K378 (= K393), T381 (= T396), A404 (= A419), T405 (= T420), H406 (= H421), N407 (= N422), C431 (= C446), L432 (= L447), E475 (= E502), S481 (= S508), F482 (= F509)
- binding nicotinamide-adenine-dinucleotide: I686 (= I718), S687 (= S719), P688 (= P720), W689 (= W721), N690 (= N722), I695 (= I727), K713 (= K745), A715 (= A747), E716 (= E748), G746 (= G778), G749 (= G782), A750 (= A783), T764 (= T797), G765 (= G798), S766 (= S799), V769 (= V802), E793 (= E826), T794 (= T827), C827 (= C860), E923 (= E958), F925 (= F960), F993 (= F1028)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y483), Y468 (= Y495), R471 (= R498), R472 (= R499)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1214/1214 of 6x9bA
- active site: N688 (= N722), K711 (= K745), E791 (= E826), C825 (= C860), E921 (= E958), A1003 (= A1040)
- binding flavin-adenine dinucleotide: D287 (= D304), A288 (= A305), V319 (= V336), R348 (= R365), V350 (= V367), K351 (= K368), G352 (= G369), A353 (= A370), Y354 (= Y371), W355 (= W372), F373 (≠ Y390), T374 (= T391), R375 (= R392), K376 (= K393), T379 (= T396), A402 (= A419), T403 (= T420), H404 (= H421), N405 (= N422), Q428 (= Q445), C429 (= C446), Y454 (= Y483), E473 (= E502), S479 (= S508), F480 (= F509)
- binding nicotinamide-adenine-dinucleotide: I684 (= I718), S685 (= S719), P686 (= P720), W687 (= W721), N688 (= N722), I693 (= I727), K711 (= K745), A713 (= A747), E714 (= E748), G744 (= G778), G747 (= G782), A748 (= A783), T762 (= T797), G763 (= G798), S764 (= S799), V767 (= V802), I771 (≠ L806), E791 (= E826), T792 (= T827), C825 (= C860), E921 (= E958), F923 (= F960)
- binding (4R)-4-hydroxy-D-proline: E655 (= E688), F689 (= F723), S826 (= S861), G983 (= G1020), A984 (= A1021), F991 (= F1028)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
59% identity, 100% coverage: 6:1261/1261 of query aligns to 3:1214/1214 of 6x9aA
- active site: N688 (= N722), K711 (= K745), E791 (= E826), C825 (= C860), E921 (= E958), A1003 (= A1040)
- binding flavin-adenine dinucleotide: D287 (= D304), A288 (= A305), V319 (= V336), R348 (= R365), V350 (= V367), K351 (= K368), G352 (= G369), A353 (= A370), Y354 (= Y371), W355 (= W372), F373 (≠ Y390), T374 (= T391), R375 (= R392), K376 (= K393), T379 (= T396), A402 (= A419), T403 (= T420), H404 (= H421), N405 (= N422), C429 (= C446), E473 (= E502), S479 (= S508), F480 (= F509)
- binding (4S)-4-hydroxy-D-proline: W555 (= W588), T556 (= T589), E655 (= E688), F689 (= F723), R725 (= R759), S826 (= S861), G983 (= G1020), A984 (= A1021), F991 (= F1028)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 99% coverage: 6:1257/1261 of query aligns to 2:1209/1209 of 6x9cA
- active site: N687 (= N722), K710 (= K745), E790 (= E826), C824 (= C860), E920 (= E958), A1002 (= A1040)
- binding dihydroflavine-adenine dinucleotide: D286 (= D304), A287 (= A305), V318 (= V336), Q320 (= Q338), R347 (= R365), V349 (= V367), K350 (= K368), G351 (= G369), A352 (= A370), Y353 (= Y371), W354 (= W372), F372 (≠ Y390), T373 (= T391), R374 (= R392), K375 (= K393), T378 (= T396), A401 (= A419), T402 (= T420), H403 (= H421), N404 (= N422), Q427 (= Q445), C428 (= C446), E472 (= E502), S478 (= S508), F479 (= F509)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I718), S684 (= S719), P685 (= P720), W686 (= W721), N687 (= N722), K710 (= K745), E713 (= E748), G743 (= G778), G746 (= G782), A747 (= A783), F760 (= F796), G762 (= G798), S763 (= S799), V766 (= V802), E920 (= E958), F922 (= F960)
- binding proline: R823 (= R859), C824 (= C860), S825 (= S861), G982 (= G1020), A983 (= A1021), F990 (= F1028)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
59% identity, 99% coverage: 6:1258/1261 of query aligns to 3:1206/1207 of 5kf6A
- active site: N683 (= N722), K706 (= K745), E786 (= E826), C820 (= C860), E916 (= E958), A998 (= A1040)
- binding flavin-adenine dinucleotide: D282 (= D304), A283 (= A305), V314 (= V336), Q316 (= Q338), R343 (= R365), V345 (= V367), K346 (= K368), G347 (= G369), A348 (= A370), Y349 (= Y371), W350 (= W372), F368 (≠ Y390), T369 (= T391), R370 (= R392), K371 (= K393), T374 (= T396), A397 (= A419), T398 (= T420), H399 (= H421), N400 (= N422), Q423 (= Q445), C424 (= C446), L425 (= L447), E468 (= E502), S474 (= S508), F475 (= F509)
- binding nicotinamide-adenine-dinucleotide: I679 (= I718), S680 (= S719), P681 (= P720), W682 (= W721), N683 (= N722), I688 (= I727), K706 (= K745), A708 (= A747), E709 (= E748), G739 (= G778), G742 (= G782), A743 (= A783), F756 (= F796), T757 (= T797), G758 (= G798), S759 (= S799), V762 (= V802), I766 (≠ L806), E786 (= E826), T787 (= T827), C820 (= C860), E916 (= E958), F918 (= F960), F986 (= F1028)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K263), D282 (= D304), Y449 (= Y483), R464 (= R498), R465 (= R499)
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)
59% identity, 99% coverage: 6:1258/1261 of query aligns to 3:1196/1197 of 6ufpA
- active site: N673 (= N722), K696 (= K745), E776 (= E826), C810 (= C860), E906 (= E958), A988 (= A1040)
- binding dihydroflavine-adenine dinucleotide: D285 (= D304), A286 (= A305), V317 (= V336), Q319 (= Q338), R346 (= R365), V348 (= V367), K349 (= K368), G350 (= G369), A351 (= A370), W353 (= W372), F371 (≠ Y390), T372 (= T391), R373 (= R392), K374 (= K393), T377 (= T396), A400 (= A419), T401 (= T420), H402 (= H421), N403 (= N422), Q426 (= Q445), C427 (= C446), L428 (= L447), S464 (= S508)
- binding nicotinamide-adenine-dinucleotide: I669 (= I718), P671 (= P720), W672 (= W721), N673 (= N722), I678 (= I727), K696 (= K745), E699 (= E748), G729 (= G778), G732 (= G782), F746 (= F796), T747 (= T797), G748 (= G798), S749 (= S799), V752 (= V802), E776 (= E826), T777 (= T827), C810 (= C860), E906 (= E958), F908 (= F960)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K263), D285 (= D304), Y439 (= Y483), Y451 (= Y495), R454 (= R498), R455 (= R499)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
48% identity, 80% coverage: 39:1053/1261 of query aligns to 18:973/983 of 3hazA
- active site: N652 (= N722), K675 (= K745), E752 (= E826), C786 (= C860), E878 (= E958), A960 (= A1040)
- binding flavin-adenine dinucleotide: D272 (= D304), A273 (= A305), Q306 (= Q338), R333 (= R365), V335 (= V367), K336 (= K368), G337 (= G369), A338 (= A370), Y339 (= Y371), W340 (= W372), F358 (≠ Y390), T359 (= T391), R360 (= R392), K361 (= K393), T364 (= T396), A387 (= A419), T388 (= T420), H389 (= H421), N390 (= N422), Y435 (= Y483), S460 (= S508), F461 (= F509)
- binding nicotinamide-adenine-dinucleotide: I648 (= I718), S649 (= S719), P650 (= P720), W651 (= W721), N652 (= N722), I657 (= I727), K675 (= K745), P676 (= P746), A677 (= A747), G708 (= G778), G711 (= G782), A712 (= A783), T726 (= T797), G727 (= G798), S728 (= S799), V731 (= V802), I735 (≠ L806), E752 (= E826), T753 (= T827), C786 (= C860), E878 (= E958), F880 (= F960), F948 (= F1028)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
47% identity, 81% coverage: 37:1053/1261 of query aligns to 16:964/973 of 6bsnA
- active site: N643 (= N722), E743 (= E826), A777 (≠ C860), A951 (= A1040)
- binding dihydroflavine-adenine dinucleotide: D269 (= D304), A270 (= A305), Q303 (= Q338), R330 (= R365), V332 (= V367), K333 (= K368), G334 (= G369), A335 (= A370), Y336 (= Y371), W337 (= W372), F355 (≠ Y390), T356 (= T391), R357 (= R392), K358 (= K393), T361 (= T396), A384 (= A419), T385 (= T420), H386 (= H421), N387 (= N422), Y432 (= Y483), S457 (= S508), F458 (= F509)
- binding proline: M630 (vs. gap), W642 (= W721), F644 (= F723), G718 (= G798), R776 (= R859), S778 (= S861), F871 (= F960), I930 (≠ V1019), G931 (= G1020), A932 (= A1021), F939 (= F1028), A958 (≠ L1047), R959 (= R1048), A961 (≠ L1050)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
74% identity, 42% coverage: 27:551/1261 of query aligns to 6:501/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K263), Y433 (= Y483), R448 (= R498), R449 (= R499)
- binding flavin-adenine dinucleotide: D263 (= D304), A264 (= A305), V295 (= V336), Q297 (= Q338), R324 (= R365), V326 (= V367), K327 (= K368), G328 (= G369), A329 (= A370), Y330 (= Y371), W331 (= W372), Y349 (= Y390), T350 (= T391), R351 (= R392), K352 (= K393), T355 (= T396), A378 (= A419), T379 (= T420), H380 (= H421), N381 (= N422), C405 (= C446), L406 (= L447), E452 (= E502), S458 (= S508)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
73% identity, 42% coverage: 27:551/1261 of query aligns to 6:497/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D304), A260 (= A305), V291 (= V336), Q293 (= Q338), R320 (= R365), V322 (= V367), K323 (= K368), G324 (= G369), A325 (= A370), Y326 (= Y371), W327 (= W372), Y345 (= Y390), T346 (= T391), R347 (= R392), K348 (= K393), T351 (= T396), A374 (= A419), T375 (= T420), H376 (= H421), N377 (= N422), C401 (= C446), L402 (= L447), E448 (= E502), S454 (= S508)
- binding cyclopropanecarboxylic acid: K218 (= K263), Y429 (= Y483), Y441 (= Y495), R444 (= R498), R445 (= R499)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
73% identity, 42% coverage: 27:551/1261 of query aligns to 6:497/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D304), A260 (= A305), V291 (= V336), Q293 (= Q338), R320 (= R365), V322 (= V367), K323 (= K368), G324 (= G369), A325 (= A370), Y326 (= Y371), W327 (= W372), Y345 (= Y390), T346 (= T391), R347 (= R392), K348 (= K393), T351 (= T396), A374 (= A419), T375 (= T420), H376 (= H421), N377 (= N422), C401 (= C446), L402 (= L447), E448 (= E502), S454 (= S508)
- binding cyclobutanecarboxylic acid: K218 (= K263), L402 (= L447), Y429 (= Y483), Y441 (= Y495), R444 (= R498), R445 (= R499)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
73% identity, 42% coverage: 27:551/1261 of query aligns to 6:497/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D304), A260 (= A305), V291 (= V336), Q293 (= Q338), R320 (= R365), V322 (= V367), K323 (= K368), G324 (= G369), A325 (= A370), Y326 (= Y371), W327 (= W372), Y345 (= Y390), T346 (= T391), R347 (= R392), K348 (= K393), T351 (= T396), A374 (= A419), T375 (= T420), H376 (= H421), N377 (= N422), C401 (= C446), L402 (= L447), E448 (= E502), S454 (= S508)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K263), Y326 (= Y371), Y429 (= Y483), Y441 (= Y495), R444 (= R498), R445 (= R499)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
72% identity, 42% coverage: 27:551/1261 of query aligns to 7:489/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A305), V283 (= V336), Q285 (= Q338), R312 (= R365), V314 (= V367), K315 (= K368), G316 (= G369), A317 (= A370), Y318 (= Y371), W319 (= W372), Y337 (= Y390), T338 (= T391), R339 (= R392), K340 (= K393), T343 (= T396), A366 (= A419), T367 (= T420), H368 (= H421), N369 (= N422), C393 (= C446), L394 (= L447), E440 (= E502), S446 (= S508), F447 (= F509)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K263), Y421 (= Y483), R436 (= R498), R437 (= R499)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
68% identity, 42% coverage: 27:551/1261 of query aligns to 6:466/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D304), A229 (= A305), V260 (= V336), Q262 (= Q338), V291 (= V367), K292 (= K368), G293 (= G369), A294 (= A370), Y295 (= Y371), W296 (= W372), Y314 (= Y390), T315 (= T391), R316 (= R392), K317 (= K393), T320 (= T396), A343 (= A419), T344 (= T420), H345 (= H421), N346 (= N422), C370 (= C446), L371 (= L447), E417 (= E502), S423 (= S508), F424 (= F509)
- binding proline: K187 (= K263), L371 (= L447), Y410 (= Y495), R413 (= R498), R414 (= R499)
3e2qA Crystal structure reduced puta86-630 mutant y540s complexed with trans-4-hydroxy-l-proline (see paper)
68% identity, 42% coverage: 27:551/1261 of query aligns to 6:466/468 of 3e2qA
- binding flavin-adenine dinucleotide: D228 (= D304), A229 (= A305), V260 (= V336), Q262 (= Q338), V291 (= V367), K292 (= K368), G293 (= G369), A294 (= A370), Y295 (= Y371), W296 (= W372), Y314 (= Y390), T315 (= T391), R316 (= R392), K317 (= K393), T320 (= T396), A343 (= A419), T344 (= T420), H345 (= H421), N346 (= N422), Q369 (= Q445), C370 (= C446), L371 (= L447), E417 (= E502), S423 (= S508), F424 (= F509)
- binding 4-hydroxyproline: D143 (= D219), K187 (= K263), D228 (= D304), Y410 (= Y495), R413 (= R498), R414 (= R499)
Query Sequence
>Ac3H11_2850 FitnessBrowser__acidovorax_3H11:Ac3H11_2850
MTLPTAPFADFAPRTPLANPLRAAITAAITAATRHPEPEALAPLLAQARLPADQAAAAEQ
LALRIAKALRERKASAGRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIR
DKISHGQWDAHLGKSPSLFVNAATWGLLITGKLVATHSEGSLGNSLSRLIGKGGEPLIRK
GVDMAMRMMGEQFVTGETIDEALRNARTMEAEGFRYSYDMLGEAALTSEDAKRYYSSYEQ
AIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQFGRVMDELYPLVLRLTALAKQYDIG
LNIDAEETDRLELSLDLLERLCHEPTLAGWNGIGFVIQAYQKRCPFVIDCVVDLARRTQR
RLMVRLVKGAYWDSEIKRAQVDGLKDYPVYTRKVHTDISYIACAKKLLAAPEAVYPQFAT
HNAETVATIYQLAGSNYYAGQYEFQCLHGMGEPLYEQVVGAITAGKLGREIGKGGLGRPC
RIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADETIALDELVKSPVQVVDQQAATEGT
AGLPHPRIPLPAALYGAHRSNSRGLDLSNENTLTELAATLQATASHAWTAAPLLAADVPA
GTTQPVRNPADHNDVVGQVQEATTADVDQALVHAQAAATSWAATPPAERAAALLRTADLL
EERIQPLMGLLMREAGKSASNAVAEVREAVDFLRYYAAQVQSTFDNATHIPLGPVACISP
WNFPLAIFMGQVAAALAAGNPVLAKPAEQTPLIAAEAVRLLWQAGVPRAAVQLLPGQGET
VGARLIGDARVMGVMFTGSTEVARILQRTVAGRLDAAGRPIPLIAETGGQNAMIVDSSAL
VEQVVGDAVSSAFDSAGQRCSALRVLCVQEEAADRVVEMLQGAMGELRVGNPGELRVDVG
PVIDAEAQAGIAQHIEKFKAQGHRVFQHPNHVSAISAPGTFVPPTLIELNHIGELQREVF
GPVLHLVRYARSDLDQLLDQINATGYGLTQGVHTRIDETIARVVNRAHAGNVYVNRNMVG
AVVGVQPFGGEGLSGTGPKAGGPLYLLRLLSQRPADALARTFAEADRTSPHDTERRERHL
APLATLQQWAHNQGNLALAGHCQRFAQETQSGTSRTLPGPTGERNVYTLAPRARVLCLAH
SVDDLLVQTAAVLASGGTALWPHAHAGLRAKLPTHVQAQVMLQDNTLSDGSVALDAVLHH
GDAPSLQAVCTTLARRPGPIVGVTALQPGAADIPLERLLIERALSVNTAAAGGNASLMTI
G
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