SitesBLAST
Comparing GFF1160 PGA1_c11750 bifunctional protein PutA 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)
48% identity, 98% coverage: 15:1154/1158 of query aligns to 9:1215/1218 of 6x9dA
- active site: N692 (= N680), K715 (= K703), E795 (= E780), C829 (= C814), E925 (= E907), A1007 (= A989)
- binding flavin-adenine dinucleotide: D291 (= D297), A292 (= A298), V323 (= V329), Q325 (= Q331), R352 (= R358), V354 (= V360), K355 (= K361), G356 (= G362), A357 (= A363), Y358 (= Y364), W359 (= W365), F377 (= F383), T378 (= T384), R379 (≠ H385), K380 (= K386), T383 (= T389), A406 (= A412), T407 (= T413), H408 (= H414), N409 (= N415), Q432 (= Q437), C433 (≠ R438), E477 (= E480), S483 (= S486), F484 (= F487)
- binding 4-hydroxyproline: E659 (= E652), F693 (= F681), I697 (= I685), R828 (= R813), S830 (= S815), G987 (= G969), A988 (= A970), F995 (= F977)
- binding nicotinamide-adenine-dinucleotide: I688 (= I676), S689 (= S677), P690 (= P678), W691 (= W679), N692 (= N680), I697 (= I685), K715 (= K703), A717 (= A705), E718 (= E706), G748 (= G736), G751 (= G739), A752 (≠ G740), T766 (= T754), G767 (= G755), S768 (= S756), V771 (≠ T759), E795 (= E780), T796 (= T781), C829 (= C814), E925 (= E907), F927 (= F909), F995 (= F977)
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: 15:1154/1158 of query aligns to 9:1211/1214 of 6x9aA
- active site: N688 (= N680), K711 (= K703), E791 (= E780), C825 (= C814), E921 (= E907), A1003 (= A989)
- binding flavin-adenine dinucleotide: D287 (= D297), A288 (= A298), V319 (= V329), R348 (= R358), V350 (= V360), K351 (= K361), G352 (= G362), A353 (= A363), Y354 (= Y364), W355 (= W365), F373 (= F383), T374 (= T384), R375 (≠ H385), K376 (= K386), T379 (= T389), A402 (= A412), T403 (= T413), H404 (= H414), N405 (= N415), C429 (≠ R438), E473 (= E480), S479 (= S486), F480 (= F487)
- binding (4S)-4-hydroxy-D-proline: W555 (= W556), T556 (≠ A557), E655 (= E652), F689 (= F681), R725 (≠ S717), S826 (= S815), G983 (= G969), A984 (= A970), F991 (= F977)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
48% identity, 98% coverage: 15:1154/1158 of query aligns to 9:1214/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I676), S688 (= S677), P689 (= P678), W690 (= W679), N691 (= N680), K714 (= K703), E717 (= E706), G747 (= G736), G750 (= G739), A751 (≠ G740), F764 (= F753), G766 (= G755), S767 (= S756), V770 (≠ T759), T795 (= T781), G796 (= G782), C828 (= C814), E924 (= E907), F926 (= F909)
- 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 (= K256), D290 (= D297), A291 (= A298), V322 (= V329), Q324 (= Q331), R351 (= R358), V353 (= V360), K354 (= K361), G355 (= G362), A356 (= A363), Y357 (= Y364), W358 (= W365), F376 (= F383), T377 (= T384), R378 (≠ H385), K379 (= K386), T382 (= T389), A405 (= A412), T406 (= T413), H407 (= H414), N408 (= N415), Q431 (= Q437), C432 (≠ R438), L433 (= L439), Y457 (= Y461), S482 (= S486), F483 (= F487)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 98% coverage: 15:1154/1158 of query aligns to 9:1214/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D297), A291 (= A298), V322 (= V329), Q324 (= Q331), R351 (= R358), V353 (= V360), K354 (= K361), G355 (= G362), A356 (= A363), Y357 (= Y364), W358 (= W365), F376 (= F383), T377 (= T384), R378 (≠ H385), K379 (= K386), T382 (= T389), A405 (= A412), T406 (= T413), H407 (= H414), N408 (= N415), C432 (≠ R438), L433 (= L439), E476 (= E480), S482 (= S486), F483 (= F487)
- binding nicotinamide-adenine-dinucleotide: I687 (= I676), S688 (= S677), P689 (= P678), W690 (= W679), N691 (= N680), I696 (= I685), K714 (= K703), E717 (= E706), G747 (= G736), G750 (= G739), T765 (= T754), G766 (= G755), S767 (= S756), V770 (≠ T759), I774 (= I763), E794 (= E780), T795 (= T781), C828 (= C814), E924 (= E907), F926 (= F909), F994 (= F977)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K256), Y457 (= Y461), Y469 (= Y473), R472 (= R476), R473 (= R477)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K256), D290 (= D297), Y457 (= Y461), Y469 (= Y473), R472 (= R476), R473 (= R477)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
48% identity, 98% coverage: 15:1154/1158 of query aligns to 9:1214/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I676), S688 (= S677), P689 (= P678), W690 (= W679), N691 (= N680), I696 (= I685), K714 (= K703), A716 (= A705), E717 (= E706), G747 (= G736), G750 (= G739), A751 (≠ G740), T765 (= T754), G766 (= G755), S767 (= S756), V770 (≠ T759), E794 (= E780), T795 (= T781), C828 (= C814), E924 (= E907), F926 (= F909), F994 (= F977)
- 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 (= D297), A291 (= A298), V322 (= V329), Q324 (= Q331), V353 (= V360), K354 (= K361), G355 (= G362), A356 (= A363), W358 (= W365), F376 (= F383), T377 (= T384), R378 (≠ H385), K379 (= K386), T382 (= T389), A405 (= A412), T406 (= T413), H407 (= H414), N408 (= N415), Q431 (= Q437), C432 (≠ R438), L433 (= L439), Y457 (= Y461), E476 (= E480)
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
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 98% coverage: 15:1154/1158 of query aligns to 9:1213/1216 of 6x99A
- active site: N690 (= N680), K713 (= K703), E793 (= E780), C827 (= C814), E923 (= E907), A1005 (= A989)
- binding d-proline: W557 (= W556), T558 (≠ A557), E657 (= E652), F691 (= F681), R727 (≠ S717), R826 (= R813), S828 (= S815), G985 (= G969), A986 (= A970), F993 (= F977)
- binding flavin-adenine dinucleotide: D289 (= D297), A290 (= A298), V321 (= V329), R350 (= R358), V352 (= V360), K353 (= K361), G354 (= G362), A355 (= A363), Y356 (= Y364), W357 (= W365), F375 (= F383), T376 (= T384), R377 (≠ H385), K378 (= K386), T381 (= T389), A404 (= A412), T405 (= T413), H406 (= H414), N407 (= N415), Q430 (= Q437), C431 (≠ R438), Y456 (= Y461), E475 (= E480), S481 (= S486), F482 (= F487)
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: 15:1154/1158 of query aligns to 9:1211/1214 of 6x9bA
- active site: N688 (= N680), K711 (= K703), E791 (= E780), C825 (= C814), E921 (= E907), A1003 (= A989)
- binding flavin-adenine dinucleotide: D287 (= D297), A288 (= A298), V319 (= V329), R348 (= R358), V350 (= V360), K351 (= K361), G352 (= G362), A353 (= A363), Y354 (= Y364), W355 (= W365), F373 (= F383), T374 (= T384), R375 (≠ H385), K376 (= K386), T379 (= T389), A402 (= A412), T403 (= T413), H404 (= H414), N405 (= N415), Q428 (= Q437), C429 (≠ R438), Y454 (= Y461), E473 (= E480), S479 (= S486), F480 (= F487)
- binding nicotinamide-adenine-dinucleotide: I684 (= I676), S685 (= S677), P686 (= P678), W687 (= W679), N688 (= N680), I693 (= I685), K711 (= K703), A713 (= A705), E714 (= E706), G744 (= G736), G747 (= G739), A748 (≠ G740), T762 (= T754), G763 (= G755), S764 (= S756), V767 (≠ T759), I771 (= I763), E791 (= E780), T792 (= T781), C825 (= C814), E921 (= E907), F923 (= F909)
- binding (4R)-4-hydroxy-D-proline: E655 (= E652), F689 (= F681), S826 (= S815), G983 (= G969), A984 (= A970), F991 (= F977)
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: 15:1154/1158 of query aligns to 9:1213/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D297), A290 (= A298), V321 (= V329), Q323 (= Q331), R350 (= R358), V352 (= V360), K353 (= K361), G354 (= G362), A355 (= A363), Y356 (= Y364), W357 (= W365), F375 (= F383), T376 (= T384), R377 (≠ H385), K378 (= K386), T381 (= T389), A404 (= A412), T405 (= T413), H406 (= H414), N407 (= N415), C431 (≠ R438), L432 (= L439), E475 (= E480), S481 (= S486), F482 (= F487)
- binding nicotinamide-adenine-dinucleotide: I686 (= I676), S687 (= S677), P688 (= P678), W689 (= W679), N690 (= N680), I695 (= I685), K713 (= K703), A715 (= A705), E716 (= E706), G746 (= G736), G749 (= G739), A750 (≠ G740), T764 (= T754), G765 (= G755), S766 (= S756), V769 (≠ T759), E793 (= E780), T794 (= T781), C827 (= C814), E923 (= E907), F925 (= F909), F993 (= F977)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y461), Y468 (= Y473), R471 (= R476), R472 (= R477)
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: 15:1153/1158 of query aligns to 8:1209/1209 of 6x9cA
- active site: N687 (= N680), K710 (= K703), E790 (= E780), C824 (= C814), E920 (= E907), A1002 (= A989)
- binding dihydroflavine-adenine dinucleotide: D286 (= D297), A287 (= A298), V318 (= V329), Q320 (= Q331), R347 (= R358), V349 (= V360), K350 (= K361), G351 (= G362), A352 (= A363), Y353 (= Y364), W354 (= W365), F372 (= F383), T373 (= T384), R374 (≠ H385), K375 (= K386), T378 (= T389), A401 (= A412), T402 (= T413), H403 (= H414), N404 (= N415), Q427 (= Q437), C428 (≠ R438), E472 (= E480), S478 (= S486), F479 (= F487)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I676), S684 (= S677), P685 (= P678), W686 (= W679), N687 (= N680), K710 (= K703), E713 (= E706), G743 (= G736), G746 (= G739), A747 (≠ G740), F760 (= F753), G762 (= G755), S763 (= S756), V766 (≠ T759), E920 (= E907), F922 (= F909)
- binding proline: R823 (= R813), C824 (= C814), S825 (= S815), G982 (= G969), A983 (= A970), F990 (= F977)
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: 15:1154/1158 of query aligns to 9:1206/1207 of 5kf6A
- active site: N683 (= N680), K706 (= K703), E786 (= E780), C820 (= C814), E916 (= E907), A998 (= A989)
- binding flavin-adenine dinucleotide: D282 (= D297), A283 (= A298), V314 (= V329), Q316 (= Q331), R343 (= R358), V345 (= V360), K346 (= K361), G347 (= G362), A348 (= A363), Y349 (= Y364), W350 (= W365), F368 (= F383), T369 (= T384), R370 (≠ H385), K371 (= K386), T374 (= T389), A397 (= A412), T398 (= T413), H399 (= H414), N400 (= N415), Q423 (= Q437), C424 (≠ R438), L425 (= L439), E468 (= E480), S474 (= S486), F475 (= F487)
- binding nicotinamide-adenine-dinucleotide: I679 (= I676), S680 (= S677), P681 (= P678), W682 (= W679), N683 (= N680), I688 (= I685), K706 (= K703), A708 (= A705), E709 (= E706), G739 (= G736), G742 (= G739), A743 (≠ G740), F756 (= F753), T757 (= T754), G758 (= G755), S759 (= S756), V762 (≠ T759), I766 (= I763), E786 (= E780), T787 (= T781), C820 (= C814), E916 (= E907), F918 (= F909), F986 (= F977)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K256), D282 (= D297), Y449 (= Y461), R464 (= R476), R465 (= R477)
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: 15:1154/1158 of query aligns to 9:1196/1197 of 6ufpA
- active site: N673 (= N680), K696 (= K703), E776 (= E780), C810 (= C814), E906 (= E907), A988 (= A989)
- binding dihydroflavine-adenine dinucleotide: D285 (= D297), A286 (= A298), V317 (= V329), Q319 (= Q331), R346 (= R358), V348 (= V360), K349 (= K361), G350 (= G362), A351 (= A363), W353 (= W365), F371 (= F383), T372 (= T384), R373 (≠ H385), K374 (= K386), T377 (= T389), A400 (= A412), T401 (= T413), H402 (= H414), N403 (= N415), Q426 (= Q437), C427 (≠ R438), L428 (= L439), S464 (= S486)
- binding nicotinamide-adenine-dinucleotide: I669 (= I676), P671 (= P678), W672 (= W679), N673 (= N680), I678 (= I685), K696 (= K703), E699 (= E706), G729 (= G736), G732 (= G739), F746 (= F753), T747 (= T754), G748 (= G755), S749 (= S756), V752 (≠ T759), E776 (= E780), T777 (= T781), C810 (= C814), E906 (= E907), F908 (= F909)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K256), D285 (= D297), Y439 (= Y461), Y451 (= Y473), R454 (= R476), R455 (= R477)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
49% identity, 83% coverage: 35:999/1158 of query aligns to 15:970/983 of 3hazA
- active site: N652 (= N680), K675 (= K703), E752 (= E780), C786 (= C814), E878 (= E907), A960 (= A989)
- binding flavin-adenine dinucleotide: D272 (= D297), A273 (= A298), Q306 (= Q331), R333 (= R358), V335 (= V360), K336 (= K361), G337 (= G362), A338 (= A363), Y339 (= Y364), W340 (= W365), F358 (= F383), T359 (= T384), R360 (≠ H385), K361 (= K386), T364 (= T389), A387 (= A412), T388 (= T413), H389 (= H414), N390 (= N415), Y435 (= Y461), S460 (= S486), F461 (= F487)
- binding nicotinamide-adenine-dinucleotide: I648 (= I676), S649 (= S677), P650 (= P678), W651 (= W679), N652 (= N680), I657 (= I685), K675 (= K703), P676 (= P704), A677 (= A705), G708 (= G736), G711 (= G739), A712 (≠ G740), T726 (= T754), G727 (= G755), S728 (= S756), V731 (≠ T759), I735 (= I763), E752 (= E780), T753 (= T781), C786 (= C814), E878 (= E907), F880 (= F909), F948 (= F977)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
49% identity, 83% coverage: 35:999/1158 of query aligns to 15:961/973 of 6bsnA
- active site: N643 (= N680), E743 (= E780), A777 (≠ C814), A951 (= A989)
- binding dihydroflavine-adenine dinucleotide: D269 (= D297), A270 (= A298), Q303 (= Q331), R330 (= R358), V332 (= V360), K333 (= K361), G334 (= G362), A335 (= A363), Y336 (= Y364), W337 (= W365), F355 (= F383), T356 (= T384), R357 (≠ H385), K358 (= K386), T361 (= T389), A384 (= A412), T385 (= T413), H386 (= H414), N387 (= N415), Y432 (= Y461), S457 (= S486), F458 (= F487)
- binding proline: M630 (vs. gap), W642 (= W679), F644 (= F681), G718 (= G755), R776 (= R813), S778 (= S815), F871 (= F909), I930 (= I968), G931 (= G969), A932 (= A970), F939 (= F977), A958 (≠ M996), R959 (= R997), A961 (≠ C999)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
53% identity, 38% coverage: 75:512/1158 of query aligns to 59:484/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K256), Y433 (= Y461), R448 (= R476), R449 (= R477)
- binding flavin-adenine dinucleotide: D263 (= D297), A264 (= A298), V295 (= V329), Q297 (= Q331), R324 (= R358), V326 (= V360), K327 (= K361), G328 (= G362), A329 (= A363), Y330 (= Y364), W331 (= W365), Y349 (≠ F383), T350 (= T384), R351 (≠ H385), K352 (= K386), T355 (= T389), A378 (= A412), T379 (= T413), H380 (= H414), N381 (= N415), C405 (≠ R438), L406 (= L439), E452 (= E480), S458 (= S486)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
53% identity, 38% coverage: 75:512/1158 of query aligns to 59:480/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D297), A260 (= A298), V291 (= V329), Q293 (= Q331), R320 (= R358), V322 (= V360), K323 (= K361), G324 (= G362), A325 (= A363), Y326 (= Y364), W327 (= W365), Y345 (≠ F383), T346 (= T384), R347 (≠ H385), K348 (= K386), T351 (= T389), A374 (= A412), T375 (= T413), H376 (= H414), N377 (= N415), C401 (≠ R438), L402 (= L439), E448 (= E480), S454 (= S486)
- binding cyclopropanecarboxylic acid: K218 (= K256), Y429 (= Y461), Y441 (= Y473), R444 (= R476), R445 (= R477)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
53% identity, 38% coverage: 75:512/1158 of query aligns to 59:480/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D297), A260 (= A298), V291 (= V329), Q293 (= Q331), R320 (= R358), V322 (= V360), K323 (= K361), G324 (= G362), A325 (= A363), Y326 (= Y364), W327 (= W365), Y345 (≠ F383), T346 (= T384), R347 (≠ H385), K348 (= K386), T351 (= T389), A374 (= A412), T375 (= T413), H376 (= H414), N377 (= N415), C401 (≠ R438), L402 (= L439), E448 (= E480), S454 (= S486)
- binding cyclobutanecarboxylic acid: K218 (= K256), L402 (= L439), Y429 (= Y461), Y441 (= Y473), R444 (= R476), R445 (= R477)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
53% identity, 38% coverage: 75:512/1158 of query aligns to 59:480/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D297), A260 (= A298), V291 (= V329), Q293 (= Q331), R320 (= R358), V322 (= V360), K323 (= K361), G324 (= G362), A325 (= A363), Y326 (= Y364), W327 (= W365), Y345 (≠ F383), T346 (= T384), R347 (≠ H385), K348 (= K386), T351 (= T389), A374 (= A412), T375 (= T413), H376 (= H414), N377 (= N415), C401 (≠ R438), L402 (= L439), E448 (= E480), S454 (= S486)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K256), Y326 (= Y364), Y429 (= Y461), Y441 (= Y473), R444 (= R476), R445 (= R477)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
52% identity, 38% coverage: 75:512/1158 of query aligns to 60:472/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A298), V283 (= V329), Q285 (= Q331), R312 (= R358), V314 (= V360), K315 (= K361), G316 (= G362), A317 (= A363), Y318 (= Y364), W319 (= W365), Y337 (≠ F383), T338 (= T384), R339 (≠ H385), K340 (= K386), T343 (= T389), A366 (= A412), T367 (= T413), H368 (= H414), N369 (= N415), C393 (≠ R438), L394 (= L439), E440 (= E480), S446 (= S486), F447 (= F487)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K256), Y421 (= Y461), R436 (= R476), R437 (= R477)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
50% identity, 38% coverage: 75:512/1158 of query aligns to 59:450/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D297), A230 (= A298), V261 (= V329), Q263 (= Q331), R290 (= R358), V292 (= V360), K293 (= K361), G294 (= G362), A295 (= A363), Y296 (= Y364), W297 (= W365), Y315 (≠ F383), T316 (= T384), R317 (≠ H385), K318 (= K386), T321 (= T389), A344 (= A412), T345 (= T413), H346 (= H414), N347 (= N415), Q370 (= Q437), C371 (≠ R438), L372 (= L439), E418 (= E480), S424 (= S486)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
50% identity, 38% coverage: 75:512/1158 of query aligns to 59:449/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D297), A229 (= A298), V260 (= V329), Q262 (= Q331), V291 (= V360), K292 (= K361), G293 (= G362), A294 (= A363), Y295 (= Y364), W296 (= W365), Y314 (≠ F383), T315 (= T384), R316 (≠ H385), K317 (= K386), T320 (= T389), A343 (= A412), T344 (= T413), H345 (= H414), N346 (= N415), C370 (≠ R438), L371 (= L439), E417 (= E480), S423 (= S486), F424 (= F487)
- binding proline: K187 (= K256), L371 (= L439), Y410 (= Y473), R413 (= R476), R414 (= R477)
Query Sequence
>GFF1160 PGA1_c11750 bifunctional protein PutA
MTAPQSKTTPEMPSAPTPEYSDALRYRIDAGTYVDQAQMRDQLFALANLDATDRSTISAN
AAALVRDIRGHSSPGLMEVFLAEYGLSTDEGVALMCLAEALLRVPDADTIDALIEDKIAP
SEWGKHLGKSTSSLVNASTWALMLTGKVLDEKRSPVSALRGAMKRLGEPVIRTAVSRAMK
EMGRQFVLGETIEGAMKRAAGMEAKGYTYSYDMLGEAARTEADAARYHLAYSRAISAIAA
ACNSADIRQNPGISVKLSALHPRYELAQETSVKEQLVPRLQALALLAKAAGMGLNVDAEE
ADRLSLSLEVIEEVISDPALAGWDGFGVVVQAYGPRTGAALDALYDMANRYDRRLMVRLV
KGAYWDTEVKRAQVEGVDGFPVFTHKSLTDVSYIANARKLLSITDRIYPQFATHNAHTVS
AILHMAKDTDKGAYEFQRLHGMGETLHNMVLEQNQTHCRIYAPVGAHRDLLAYLVRRLLE
NGANSSFVNQIVDENVPPELVAADPFAQVEDLTANLRKGPDLFQPERPNSIGFDLGHAPT
LAAIDAARAPWKSHSWAAEPLLAKAPETATTTDEPVRNPADLTTVGRVQTAGQAEIETAL
SAATPWNASAETRAEVLNRAADLYEANYGELFALLTREAGKTLPDCVAELREAVDFLRYY
AARISAEPPVGVFTCISPWNFPLAIFSGQIAAALAVGNAVLAKPAEQTPLIAHRAISLLH
EAGVPRSALQLLPGAGAVGGALTSDARVGGVAFTGSTATALKIRAAMAEHLRPGAPLIAE
TGGLNAMIVDSTALPEQAVQSIIESAFQSAGQRCSALRCLYLQEDIADNVLKMLKGAMDA
LHLGDPWNLSTDSGPVIDETARAGILAHIDAARAEGRVLKEMTAPQGGTFVAPTLIEITG
IQALEQEIFGPVLHVVRFKSQDLDQIIRDINATGYGLTFGLHTRIDDRVQYICDRIHAGN
LYVNRNQIGAIVGSQPFGGEGLSGTGPKAGGPFYMMRFCAPDRQKSVDSWPSDAPAMTML
PAPTGQPMQEITTSLPGPTGESNRLSQLARPPLLCLGPGPQAVVAQARAVHALGGTAIEA
TGPLDMRQLLTMEGTSGVIWWGDETTAREIESWLARRNGPILPLIPGLPDKARVQAERHV
CVDTTAAGGNAALLGGMG
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