SitesBLAST
Comparing WP_050461642.1 NCBI__GCF_001189915.1:WP_050461642.1 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)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1217/1218 of 6x9dA
- active site: N692 (= N699), K715 (= K722), E795 (= E803), C829 (= C837), E925 (= E933), A1007 (= A1015)
- binding flavin-adenine dinucleotide: D291 (= D303), A292 (= A304), V323 (= V335), Q325 (= Q337), R352 (= R364), V354 (= V366), K355 (= K367), G356 (= G368), A357 (= A369), Y358 (= Y370), W359 (= W371), F377 (≠ Y389), T378 (= T390), R379 (= R391), K380 (= K392), T383 (= T395), A406 (= A418), T407 (= T419), H408 (= H420), N409 (= N421), Q432 (= Q443), C433 (= C444), E477 (= E488), S483 (= S494), F484 (= F495)
- binding 4-hydroxyproline: E659 (= E668), F693 (= F700), I697 (= I704), R828 (= R836), S830 (= S838), G987 (= G995), A988 (= A996), F995 (= F1003)
- binding nicotinamide-adenine-dinucleotide: I688 (= I695), S689 (= S696), P690 (= P697), W691 (= W698), N692 (= N699), I697 (= I704), K715 (= K722), A717 (= A724), E718 (= E725), G748 (= G755), G751 (= G759), A752 (= A760), T766 (= T774), G767 (= G775), S768 (= S776), V771 (= V779), E795 (= E803), T796 (= T804), C829 (= C837), E925 (= E933), F927 (= F935), F995 (= F1003)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1215/1216 of 6x99A
- active site: N690 (= N699), K713 (= K722), E793 (= E803), C827 (= C837), E923 (= E933), A1005 (= A1015)
- binding d-proline: W557 (= W568), T558 (≠ Q569), E657 (= E668), F691 (= F700), R727 (≠ Q736), R826 (= R836), S828 (= S838), G985 (= G995), A986 (= A996), F993 (= F1003)
- binding flavin-adenine dinucleotide: D289 (= D303), A290 (= A304), V321 (= V335), R350 (= R364), V352 (= V366), K353 (= K367), G354 (= G368), A355 (= A369), Y356 (= Y370), W357 (= W371), F375 (≠ Y389), T376 (= T390), R377 (= R391), K378 (= K392), T381 (= T395), A404 (= A418), T405 (= T419), H406 (= H420), N407 (= N421), Q430 (= Q443), C431 (= C444), Y456 (= Y469), E475 (= E488), S481 (= S494), F482 (= F495)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), K714 (= K722), E717 (= E725), G747 (= G755), G750 (= G759), A751 (= A760), F764 (= F773), G766 (= G775), S767 (= S776), V770 (= V779), T795 (= T804), G796 (= G805), C828 (= C837), E924 (= E933), F926 (= F935)
- 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 (= K262), D290 (= D303), A291 (= A304), V322 (= V335), Q324 (= Q337), R351 (= R364), V353 (= V366), K354 (= K367), G355 (= G368), A356 (= A369), Y357 (= Y370), W358 (= W371), F376 (≠ Y389), T377 (= T390), R378 (= R391), K379 (= K392), T382 (= T395), A405 (= A418), T406 (= T419), H407 (= H420), N408 (= N421), Q431 (= Q443), C432 (= C444), L433 (= L445), Y457 (= Y469), S482 (= S494), F483 (= F495)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1216/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D303), A291 (= A304), V322 (= V335), Q324 (= Q337), R351 (= R364), V353 (= V366), K354 (= K367), G355 (= G368), A356 (= A369), Y357 (= Y370), W358 (= W371), F376 (≠ Y389), T377 (= T390), R378 (= R391), K379 (= K392), T382 (= T395), A405 (= A418), T406 (= T419), H407 (= H420), N408 (= N421), C432 (= C444), L433 (= L445), E476 (= E488), S482 (= S494), F483 (= F495)
- binding nicotinamide-adenine-dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), I696 (= I704), K714 (= K722), E717 (= E725), G747 (= G755), G750 (= G759), T765 (= T774), G766 (= G775), S767 (= S776), V770 (= V779), I774 (= I783), E794 (= E803), T795 (= T804), C828 (= C837), E924 (= E933), F926 (= F935), F994 (= F1003)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K262), Y457 (= Y469), Y469 (= Y481), R472 (= R484), R473 (= R485)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K262), D290 (= D303), 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)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1216/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I695), S688 (= S696), P689 (= P697), W690 (= W698), N691 (= N699), I696 (= I704), K714 (= K722), A716 (= A724), E717 (= E725), G747 (= G755), G750 (= G759), A751 (= A760), T765 (= T774), G766 (= G775), S767 (= S776), V770 (= V779), E794 (= E803), T795 (= T804), C828 (= C837), E924 (= E933), F926 (= F935), F994 (= F1003)
- 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 (= D303), A291 (= A304), V322 (= V335), Q324 (= Q337), V353 (= V366), K354 (= K367), G355 (= G368), A356 (= A369), W358 (= W371), F376 (≠ Y389), T377 (= T390), R378 (= R391), K379 (= K392), T382 (= T395), A405 (= A418), T406 (= T419), H407 (= H420), N408 (= N421), Q431 (= Q443), C432 (= C444), L433 (= L445), 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
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1213/1214 of 6x9bA
- active site: N688 (= N699), K711 (= K722), E791 (= E803), C825 (= C837), E921 (= E933), A1003 (= A1015)
- binding flavin-adenine dinucleotide: D287 (= D303), A288 (= A304), V319 (= V335), R348 (= R364), V350 (= V366), K351 (= K367), G352 (= G368), A353 (= A369), Y354 (= Y370), W355 (= W371), F373 (≠ Y389), T374 (= T390), R375 (= R391), K376 (= K392), T379 (= T395), A402 (= A418), T403 (= T419), H404 (= H420), N405 (= N421), Q428 (= Q443), C429 (= C444), Y454 (= Y469), E473 (= E488), S479 (= S494), F480 (= F495)
- binding nicotinamide-adenine-dinucleotide: I684 (= I695), S685 (= S696), P686 (= P697), W687 (= W698), N688 (= N699), I693 (= I704), K711 (= K722), A713 (= A724), E714 (= E725), G744 (= G755), G747 (= G759), A748 (= A760), T762 (= T774), G763 (= G775), S764 (= S776), V767 (= V779), I771 (= I783), E791 (= E803), T792 (= T804), C825 (= C837), E921 (= E933), F923 (= F935)
- binding (4R)-4-hydroxy-D-proline: E655 (= E668), F689 (= F700), S826 (= S838), G983 (= G995), A984 (= A996), F991 (= F1003)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1213/1214 of 6x9aA
- active site: N688 (= N699), K711 (= K722), E791 (= E803), C825 (= C837), E921 (= E933), A1003 (= A1015)
- binding flavin-adenine dinucleotide: D287 (= D303), A288 (= A304), V319 (= V335), R348 (= R364), V350 (= V366), K351 (= K367), G352 (= G368), A353 (= A369), Y354 (= Y370), W355 (= W371), F373 (≠ Y389), T374 (= T390), R375 (= R391), K376 (= K392), T379 (= T395), A402 (= A418), T403 (= T419), H404 (= H420), N405 (= N421), C429 (= C444), E473 (= E488), S479 (= S494), F480 (= F495)
- binding (4S)-4-hydroxy-D-proline: W555 (= W568), T556 (≠ Q569), E655 (= E668), F689 (= F700), R725 (≠ Q736), S826 (= S838), G983 (= G995), A984 (= A996), F991 (= F1003)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
58% identity, 99% coverage: 8:1216/1218 of query aligns to 1:1215/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D303), A290 (= A304), V321 (= V335), Q323 (= Q337), R350 (= R364), V352 (= V366), K353 (= K367), G354 (= G368), A355 (= A369), Y356 (= Y370), W357 (= W371), F375 (≠ Y389), T376 (= T390), R377 (= R391), K378 (= K392), T381 (= T395), A404 (= A418), T405 (= T419), H406 (= H420), N407 (= N421), C431 (= C444), L432 (= L445), E475 (= E488), S481 (= S494), F482 (= F495)
- binding nicotinamide-adenine-dinucleotide: I686 (= I695), S687 (= S696), P688 (= P697), W689 (= W698), N690 (= N699), I695 (= I704), K713 (= K722), A715 (= A724), E716 (= E725), G746 (= G755), G749 (= G759), A750 (= A760), T764 (= T774), G765 (= G775), S766 (= S776), V769 (= V779), E793 (= E803), T794 (= T804), C827 (= C837), E923 (= E933), F925 (= F935), F993 (= F1003)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y469), Y468 (= Y481), R471 (= R484), R472 (= R485)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
58% identity, 99% coverage: 9:1213/1218 of query aligns to 1:1209/1209 of 6x9cA
- active site: N687 (= N699), K710 (= K722), E790 (= E803), C824 (= C837), E920 (= E933), A1002 (= A1015)
- binding dihydroflavine-adenine dinucleotide: D286 (= D303), A287 (= A304), V318 (= V335), Q320 (= Q337), R347 (= R364), V349 (= V366), K350 (= K367), G351 (= G368), A352 (= A369), Y353 (= Y370), W354 (= W371), F372 (≠ Y389), T373 (= T390), R374 (= R391), K375 (= K392), T378 (= T395), A401 (= A418), T402 (= T419), H403 (= H420), N404 (= N421), Q427 (= Q443), C428 (= C444), E472 (= E488), S478 (= S494), F479 (= F495)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I695), S684 (= S696), P685 (= P697), W686 (= W698), N687 (= N699), K710 (= K722), E713 (= E725), G743 (= G755), G746 (= G759), A747 (= A760), F760 (= F773), G762 (= G775), S763 (= S776), V766 (= V779), E920 (= E933), F922 (= F935)
- binding proline: R823 (= R836), C824 (= C837), S825 (= S838), G982 (= G995), A983 (= A996), F990 (= F1003)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
58% identity, 99% coverage: 8:1214/1218 of query aligns to 1:1206/1207 of 5kf6A
- active site: N683 (= N699), K706 (= K722), E786 (= E803), C820 (= C837), E916 (= E933), A998 (= A1015)
- binding flavin-adenine dinucleotide: D282 (= D303), A283 (= A304), V314 (= V335), Q316 (= Q337), R343 (= R364), V345 (= V366), K346 (= K367), G347 (= G368), A348 (= A369), Y349 (= Y370), W350 (= W371), F368 (≠ Y389), T369 (= T390), R370 (= R391), K371 (= K392), T374 (= T395), A397 (= A418), T398 (= T419), H399 (= H420), N400 (= N421), Q423 (= Q443), C424 (= C444), L425 (= L445), E468 (= E488), S474 (= S494), F475 (= F495)
- binding nicotinamide-adenine-dinucleotide: I679 (= I695), S680 (= S696), P681 (= P697), W682 (= W698), N683 (= N699), I688 (= I704), K706 (= K722), A708 (= A724), E709 (= E725), G739 (= G755), G742 (= G759), A743 (= A760), F756 (= F773), T757 (= T774), G758 (= G775), S759 (= S776), V762 (= V779), I766 (= I783), E786 (= E803), T787 (= T804), C820 (= C837), E916 (= E933), F918 (= F935), F986 (= F1003)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K262), D282 (= D303), 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)
58% identity, 99% coverage: 8:1214/1218 of query aligns to 1:1196/1197 of 6ufpA
- active site: N673 (= N699), K696 (= K722), E776 (= E803), C810 (= C837), E906 (= E933), A988 (= A1015)
- binding dihydroflavine-adenine dinucleotide: D285 (= D303), A286 (= A304), V317 (= V335), Q319 (= Q337), R346 (= R364), V348 (= V366), K349 (= K367), G350 (= G368), A351 (= A369), W353 (= W371), F371 (≠ Y389), T372 (= T390), R373 (= R391), K374 (= K392), T377 (= T395), A400 (= A418), T401 (= T419), H402 (= H420), N403 (= N421), Q426 (= Q443), C427 (= C444), L428 (= L445), S464 (= S494)
- binding nicotinamide-adenine-dinucleotide: I669 (= I695), P671 (= P697), W672 (= W698), N673 (= N699), I678 (= I704), K696 (= K722), E699 (= E725), G729 (= G755), G732 (= G759), F746 (= F773), T747 (= T774), G748 (= G775), S749 (= S776), V752 (= V779), E776 (= E803), T777 (= T804), C810 (= C837), E906 (= E933), F908 (= F935)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K262), D285 (= D303), Y439 (= Y469), Y451 (= Y481), R454 (= R484), R455 (= R485)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
48% identity, 82% coverage: 31:1024/1218 of query aligns to 8:969/983 of 3hazA
- active site: N652 (= N699), K675 (= K722), E752 (= E803), C786 (= C837), E878 (= E933), A960 (= A1015)
- binding flavin-adenine dinucleotide: D272 (= D303), A273 (= A304), Q306 (= Q337), R333 (= R364), V335 (= V366), K336 (= K367), G337 (= G368), A338 (= A369), Y339 (= Y370), W340 (= W371), F358 (≠ Y389), T359 (= T390), R360 (= R391), K361 (= K392), T364 (= T395), A387 (= A418), T388 (= T419), H389 (= H420), N390 (= N421), Y435 (= Y469), S460 (= S494), F461 (= F495)
- binding nicotinamide-adenine-dinucleotide: I648 (= I695), S649 (= S696), P650 (= P697), W651 (= W698), N652 (= N699), I657 (= I704), K675 (= K722), P676 (= P723), A677 (= A724), G708 (= G755), G711 (= G759), A712 (= A760), T726 (= T774), G727 (= G775), S728 (= S776), V731 (= V779), I735 (= I783), E752 (= E803), T753 (= T804), C786 (= C837), E878 (= E933), F880 (= F935), F948 (= F1003)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 82% coverage: 31:1024/1218 of query aligns to 8:960/973 of 6bsnA
- active site: N643 (= N699), E743 (= E803), A777 (≠ C837), A951 (= A1015)
- binding dihydroflavine-adenine dinucleotide: D269 (= D303), A270 (= A304), Q303 (= Q337), R330 (= R364), V332 (= V366), K333 (= K367), G334 (= G368), A335 (= A369), Y336 (= Y370), W337 (= W371), F355 (≠ Y389), T356 (= T390), R357 (= R391), K358 (= K392), T361 (= T395), A384 (= A418), T385 (= T419), H386 (= H420), N387 (= N421), Y432 (= Y469), S457 (= S494), F458 (= F495)
- binding proline: M630 (≠ W689), W642 (= W698), F644 (= F700), G718 (= G775), R776 (= R836), S778 (= S838), F871 (= F935), I930 (≠ V994), G931 (= G995), A932 (= A996), F939 (= F1003), A958 (≠ K1022), R959 (= R1023)
Sites not aligning to the query:
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
65% identity, 42% coverage: 28:533/1218 of query aligns to 5:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K262), Y433 (= Y469), R448 (= R484), R449 (= R485)
- binding flavin-adenine dinucleotide: D263 (= D303), A264 (= A304), V295 (= V335), Q297 (= Q337), R324 (= R364), V326 (= V366), K327 (= K367), G328 (= G368), A329 (= A369), Y330 (= Y370), W331 (= W371), Y349 (= Y389), T350 (= T390), R351 (= R391), K352 (= K392), T355 (= T395), A378 (= A418), T379 (= T419), H380 (= H420), N381 (= N421), C405 (= C444), L406 (= L445), E452 (= E488), S458 (= S494)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
64% identity, 42% coverage: 28:533/1218 of query aligns to 5:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D303), A260 (= A304), V291 (= V335), Q293 (= Q337), R320 (= R364), V322 (= V366), K323 (= K367), G324 (= G368), A325 (= A369), Y326 (= Y370), W327 (= W371), Y345 (= Y389), T346 (= T390), R347 (= R391), K348 (= K392), T351 (= T395), A374 (= A418), T375 (= T419), H376 (= H420), N377 (= N421), C401 (= C444), L402 (= L445), E448 (= E488), S454 (= S494)
- binding cyclopropanecarboxylic acid: K218 (= K262), 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)
64% identity, 42% coverage: 28:533/1218 of query aligns to 5:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D303), A260 (= A304), V291 (= V335), Q293 (= Q337), R320 (= R364), V322 (= V366), K323 (= K367), G324 (= G368), A325 (= A369), Y326 (= Y370), W327 (= W371), Y345 (= Y389), T346 (= T390), R347 (= R391), K348 (= K392), T351 (= T395), A374 (= A418), T375 (= T419), H376 (= H420), N377 (= N421), C401 (= C444), L402 (= L445), E448 (= E488), S454 (= S494)
- binding cyclobutanecarboxylic acid: K218 (= K262), L402 (= L445), 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)
64% identity, 42% coverage: 28:533/1218 of query aligns to 5:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D303), A260 (= A304), V291 (= V335), Q293 (= Q337), R320 (= R364), V322 (= V366), K323 (= K367), G324 (= G368), A325 (= A369), Y326 (= Y370), W327 (= W371), Y345 (= Y389), T346 (= T390), R347 (= R391), K348 (= K392), T351 (= T395), A374 (= A418), T375 (= T419), H376 (= H420), N377 (= N421), C401 (= C444), L402 (= L445), E448 (= E488), S454 (= S494)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K262), Y326 (= Y370), Y429 (= Y469), Y441 (= Y481), R444 (= R484), R445 (= R485)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
63% identity, 42% coverage: 28:533/1218 of query aligns to 6:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A304), V283 (= V335), Q285 (= Q337), R312 (= R364), V314 (= V366), K315 (= K367), G316 (= G368), A317 (= A369), Y318 (= Y370), W319 (= W371), Y337 (= Y389), T338 (= T390), R339 (= R391), K340 (= K392), T343 (= T395), A366 (= A418), T367 (= T419), H368 (= H420), N369 (= N421), C393 (= C444), L394 (= L445), E440 (= E488), S446 (= S494), F447 (= F495)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K262), Y421 (= Y469), R436 (= R484), R437 (= R485)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
60% identity, 42% coverage: 28:533/1218 of query aligns to 5:469/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D303), A230 (= A304), V261 (= V335), Q263 (= Q337), R290 (= R364), V292 (= V366), K293 (= K367), G294 (= G368), A295 (= A369), Y296 (= Y370), W297 (= W371), Y315 (= Y389), T316 (= T390), R317 (= R391), K318 (= K392), T321 (= T395), A344 (= A418), T345 (= T419), H346 (= H420), N347 (= N421), Q370 (= Q443), C371 (= C444), L372 (= L445), E418 (= E488), S424 (= S494)
1tiwA Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) complexed with l-tetrahydro-2-furoic acid (see paper)
59% identity, 42% coverage: 28:533/1218 of query aligns to 6:459/459 of 1tiwA
- binding flavin-adenine dinucleotide: D219 (= D303), A220 (= A304), V251 (= V335), Q253 (= Q337), R280 (= R364), V282 (= V366), K283 (= K367), G284 (= G368), A285 (= A369), Y286 (= Y370), W287 (= W371), Y305 (= Y389), T306 (= T390), R307 (= R391), K308 (= K392), T311 (= T395), A334 (= A418), T335 (= T419), H336 (= H420), N337 (= N421), Q360 (= Q443), C361 (= C444), L362 (= L445), E408 (= E488), S414 (= S494)
- binding tetrahydrofuran-2-carboxylic acid: K178 (= K262), D219 (= D303), Y389 (= Y469), R404 (= R484), R405 (= R485)
Query Sequence
>WP_050461642.1 NCBI__GCF_001189915.1:WP_050461642.1
MTATSQISPSPAFEAFQQALLPAPTPLQAAITSVYRRDETAAVQWLLTQIQSNDQWTDAT
HTLAHTLVQAVRTKRTRASGVDALMHEFSLSSEEGVALMCLAEALLRIPDHQTADRLIAD
KISKGDWRRHLGESPSLFVNAATWGLLITGKLVSTNSENSLTSALTRLINKGGEPLIRKG
VDLAMRMLGNQFVTGQTIAEALSNSRENEKRGYRYSYDMLGEAALTGHDADYYYRCYEEA
IHAIGRASNGRGIKDGPGISVKLSALHPRYSRAQHARVMGELLPRLKQLLVLAKSYNIGL
NIDAEEADRLELSLNLMEVLAFDPDLDGFEGIGFVVQAYQKRCPFVIDYLVDLARRSGRK
LMVRLVKGAYWDSEIKRAQVDGLSGYPVYTRKVHTDLSYLVCAQKLLASTAVIYPQFATH
NAHTLAAIYTWAQQHQITDYEFQCLHGMGETLYDQVVGDDKLGKACRIYAPVGSHQTLLA
YLVRRLLENGANSSFVNQIVDEAVAIDTLIADPVEAVRQTGGAAHAQIPLPRDLYGEERK
NSGGIDLSNEDSLRDLGREFAQLAGHEWQAGPLLQGRVTATPDLDILNPADHRDRVGRVA
EANGDDVETALAAATDYAPQWQALPATERAQMLERAADLLEQHRVELMALAVREAGKSLP
NAIAEVREAVDFLRYYAVQSQRDGNVLAWGPVVCISPWNFPLAIFVGEISAALAAGNVVL
AKPAEQTPLIAHRAVQLLHAAGIPLAALQFLPGRGETVGARLTSDERVKGVIFTGSTEVA
QLINRTLAKRVKDEHGDLPLIAETGGQNALIVDSSALPEQVVQDVLSSAFDSAGQRCSAL
RVLCLQHDIADKTMTMLKGAMEELRIGRPDRLVTDIGPVIDAEARDQLLAHIEQMRGQGC
KVYQLPLDEQTGYGTFVPPTVIEIDSLAQLQREVFGPVLHVLRYRRDELPQLIDAINATG
YGLTLGVHSRIDETINFVAGRAHVGNIYVNRNIVGAVVGVQPFGGEGKSGTGPKAGGPLY
LKRLQRQPQPLTPTVAEAAPSTTLAVLLEWAATHGHAKLATLGNSYVAESLLDTTLALPG
PTGERNTLSFAARGKMLCIATSVPALLNQLAAVLATGNTAVVDAATAQYLPAGLPEMVRQ
QVIVSDQPGTLALHLALVDAPACVQWRAQLAARDGALVPLIVTTDDAPIALWRLVAERAL
CINTTAAGGNASLMTLEV
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