SitesBLAST
Comparing GFF2744 FitnessBrowser__Marino:GFF2744 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)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1216/1218 of 6x9dA
- active site: N692 (= N684), K715 (= K707), E795 (= E785), C829 (= C819), E925 (= E912), A1007 (= A994)
- binding flavin-adenine dinucleotide: D291 (= D288), A292 (= A289), V323 (= V320), Q325 (= Q322), R352 (= R349), V354 (= V351), K355 (= K352), G356 (= G353), A357 (= A354), Y358 (= Y355), W359 (= W356), F377 (= F374), T378 (= T375), R379 (= R376), K380 (= K377), T383 (≠ S380), A406 (= A403), T407 (= T404), H408 (= H405), N409 (= N406), Q432 (= Q428), C433 (≠ R429), E477 (= E471), S483 (= S477), F484 (= F478)
- binding 4-hydroxyproline: E659 (= E652), F693 (= F685), I697 (= I689), R828 (= R818), S830 (= S820), G987 (= G974), A988 (= A975), F995 (= F982)
- binding nicotinamide-adenine-dinucleotide: I688 (= I680), S689 (= S681), P690 (= P682), W691 (= W683), N692 (= N684), I697 (= I689), K715 (= K707), A717 (= A709), E718 (= E710), G748 (= G740), G751 (= G744), A752 (= A745), T766 (= T759), G767 (= G760), S768 (= S761), V771 (≠ T764), E795 (= E785), T796 (= T786), C829 (= C819), E925 (= E912), F927 (= F914), F995 (= F982)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1215/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), R351 (= R349), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), Y357 (= Y355), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (≠ S380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), C432 (≠ R429), L433 (= L430), E476 (= E471), S482 (= S477), F483 (= F478)
- binding nicotinamide-adenine-dinucleotide: I687 (= I680), S688 (= S681), P689 (= P682), W690 (= W683), N691 (= N684), I696 (= I689), K714 (= K707), E717 (= E710), G747 (= G740), G750 (= G744), T765 (= T759), G766 (= G760), S767 (= S761), V770 (≠ T764), I774 (= I768), E794 (= E785), T795 (= T786), C828 (= C819), E924 (= E912), F926 (= F914), F994 (= F982)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K247), Y457 (= Y452), Y469 (= Y464), R472 (= R467), R473 (= R468)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K247), D290 (= D288), Y457 (= Y452), Y469 (= Y464), R472 (= R467), R473 (= R468)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1215/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I680), S688 (= S681), P689 (= P682), W690 (= W683), N691 (= N684), I696 (= I689), K714 (= K707), A716 (= A709), E717 (= E710), G747 (= G740), G750 (= G744), A751 (= A745), T765 (= T759), G766 (= G760), S767 (= S761), V770 (≠ T764), E794 (= E785), T795 (= T786), C828 (= C819), E924 (= E912), F926 (= F914), F994 (= F982)
- 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 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (≠ S380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), Q431 (= Q428), C432 (≠ R429), L433 (= L430), Y457 (= Y452), E476 (= E471)
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
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1215/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I680), S688 (= S681), P689 (= P682), W690 (= W683), N691 (= N684), K714 (= K707), E717 (= E710), G747 (= G740), G750 (= G744), A751 (= A745), F764 (= F758), G766 (= G760), S767 (= S761), V770 (≠ T764), T795 (= T786), G796 (= G787), C828 (= C819), E924 (= E912), F926 (= F914)
- 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 (= K247), D290 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), R351 (= R349), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), Y357 (= Y355), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (≠ S380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), Q431 (= Q428), C432 (≠ R429), L433 (= L430), Y457 (= Y452), S482 (= S477), F483 (= F478)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1214/1216 of 6x99A
- active site: N690 (= N684), K713 (= K707), E793 (= E785), C827 (= C819), E923 (= E912), A1005 (= A994)
- binding d-proline: W557 (= W552), T558 (≠ K553), E657 (= E652), F691 (= F685), R727 (≠ E721), R826 (= R818), S828 (= S820), G985 (= G974), A986 (= A975), F993 (= F982)
- binding flavin-adenine dinucleotide: D289 (= D288), A290 (= A289), V321 (= V320), R350 (= R349), V352 (= V351), K353 (= K352), G354 (= G353), A355 (= A354), Y356 (= Y355), W357 (= W356), F375 (= F374), T376 (= T375), R377 (= R376), K378 (= K377), T381 (≠ S380), A404 (= A403), T405 (= T404), H406 (= H405), N407 (= N406), Q430 (= Q428), C431 (≠ R429), Y456 (= Y452), E475 (= E471), S481 (= S477), F482 (= F478)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1214/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D288), A290 (= A289), V321 (= V320), Q323 (= Q322), R350 (= R349), V352 (= V351), K353 (= K352), G354 (= G353), A355 (= A354), Y356 (= Y355), W357 (= W356), F375 (= F374), T376 (= T375), R377 (= R376), K378 (= K377), T381 (≠ S380), A404 (= A403), T405 (= T404), H406 (= H405), N407 (= N406), C431 (≠ R429), L432 (= L430), E475 (= E471), S481 (= S477), F482 (= F478)
- binding nicotinamide-adenine-dinucleotide: I686 (= I680), S687 (= S681), P688 (= P682), W689 (= W683), N690 (= N684), I695 (= I689), K713 (= K707), A715 (= A709), E716 (= E710), G746 (= G740), G749 (= G744), A750 (= A745), T764 (= T759), G765 (= G760), S766 (= S761), V769 (≠ T764), E793 (= E785), T794 (= T786), C827 (= C819), E923 (= E912), F925 (= F914), F993 (= F982)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y452), Y468 (= Y464), R471 (= R467), R472 (= R468)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1212/1214 of 6x9aA
- active site: N688 (= N684), K711 (= K707), E791 (= E785), C825 (= C819), E921 (= E912), A1003 (= A994)
- binding flavin-adenine dinucleotide: D287 (= D288), A288 (= A289), V319 (= V320), R348 (= R349), V350 (= V351), K351 (= K352), G352 (= G353), A353 (= A354), Y354 (= Y355), W355 (= W356), F373 (= F374), T374 (= T375), R375 (= R376), K376 (= K377), T379 (≠ S380), A402 (= A403), T403 (= T404), H404 (= H405), N405 (= N406), C429 (≠ R429), E473 (= E471), S479 (= S477), F480 (= F478)
- binding (4S)-4-hydroxy-D-proline: W555 (= W552), T556 (≠ K553), E655 (= E652), F689 (= F685), R725 (≠ E721), S826 (= S820), G983 (= G974), A984 (= A975), F991 (= F982)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1212/1214 of 6x9bA
- active site: N688 (= N684), K711 (= K707), E791 (= E785), C825 (= C819), E921 (= E912), A1003 (= A994)
- binding flavin-adenine dinucleotide: D287 (= D288), A288 (= A289), V319 (= V320), R348 (= R349), V350 (= V351), K351 (= K352), G352 (= G353), A353 (= A354), Y354 (= Y355), W355 (= W356), F373 (= F374), T374 (= T375), R375 (= R376), K376 (= K377), T379 (≠ S380), A402 (= A403), T403 (= T404), H404 (= H405), N405 (= N406), Q428 (= Q428), C429 (≠ R429), Y454 (= Y452), E473 (= E471), S479 (= S477), F480 (= F478)
- binding nicotinamide-adenine-dinucleotide: I684 (= I680), S685 (= S681), P686 (= P682), W687 (= W683), N688 (= N684), I693 (= I689), K711 (= K707), A713 (= A709), E714 (= E710), G744 (= G740), G747 (= G744), A748 (= A745), T762 (= T759), G763 (= G760), S764 (= S761), V767 (≠ T764), I771 (= I768), E791 (= E785), T792 (= T786), C825 (= C819), E921 (= E912), F923 (= F914)
- binding (4R)-4-hydroxy-D-proline: E655 (= E652), F689 (= F685), S826 (= S820), G983 (= G974), A984 (= A975), F991 (= F982)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
45% identity, 100% coverage: 1:1204/1209 of query aligns to 11:1209/1209 of 6x9cA
- active site: N687 (= N684), K710 (= K707), E790 (= E785), C824 (= C819), E920 (= E912), A1002 (= A994)
- binding dihydroflavine-adenine dinucleotide: D286 (= D288), A287 (= A289), V318 (= V320), Q320 (= Q322), R347 (= R349), V349 (= V351), K350 (= K352), G351 (= G353), A352 (= A354), Y353 (= Y355), W354 (= W356), F372 (= F374), T373 (= T375), R374 (= R376), K375 (= K377), T378 (≠ S380), A401 (= A403), T402 (= T404), H403 (= H405), N404 (= N406), Q427 (= Q428), C428 (≠ R429), E472 (= E471), S478 (= S477), F479 (= F478)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I680), S684 (= S681), P685 (= P682), W686 (= W683), N687 (= N684), K710 (= K707), E713 (= E710), G743 (= G740), G746 (= G744), A747 (= A745), F760 (= F758), G762 (= G760), S763 (= S761), V766 (≠ T764), E920 (= E912), F922 (= F914)
- binding proline: R823 (= R818), C824 (= C819), S825 (= S820), G982 (= G974), A983 (= A975), F990 (= F982)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1207/1207 of 5kf6A
- active site: N683 (= N684), K706 (= K707), E786 (= E785), C820 (= C819), E916 (= E912), A998 (= A994)
- binding flavin-adenine dinucleotide: D282 (= D288), A283 (= A289), V314 (= V320), Q316 (= Q322), R343 (= R349), V345 (= V351), K346 (= K352), G347 (= G353), A348 (= A354), Y349 (= Y355), W350 (= W356), F368 (= F374), T369 (= T375), R370 (= R376), K371 (= K377), T374 (≠ S380), A397 (= A403), T398 (= T404), H399 (= H405), N400 (= N406), Q423 (= Q428), C424 (≠ R429), L425 (= L430), E468 (= E471), S474 (= S477), F475 (= F478)
- binding nicotinamide-adenine-dinucleotide: I679 (= I680), S680 (= S681), P681 (= P682), W682 (= W683), N683 (= N684), I688 (= I689), K706 (= K707), A708 (= A709), E709 (= E710), G739 (= G740), G742 (= G744), A743 (= A745), F756 (= F758), T757 (= T759), G758 (= G760), S759 (= S761), V762 (≠ T764), I766 (= I768), E786 (= E785), T787 (= T786), C820 (= C819), E916 (= E912), F918 (= F914), F986 (= F982)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K247), D282 (= D288), Y449 (= Y452), R464 (= R467), R465 (= R468)
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)
45% identity, 100% coverage: 1:1206/1209 of query aligns to 12:1197/1197 of 6ufpA
- active site: N673 (= N684), K696 (= K707), E776 (= E785), C810 (= C819), E906 (= E912), A988 (= A994)
- binding dihydroflavine-adenine dinucleotide: D285 (= D288), A286 (= A289), V317 (= V320), Q319 (= Q322), R346 (= R349), V348 (= V351), K349 (= K352), G350 (= G353), A351 (= A354), W353 (= W356), F371 (= F374), T372 (= T375), R373 (= R376), K374 (= K377), T377 (≠ S380), A400 (= A403), T401 (= T404), H402 (= H405), N403 (= N406), Q426 (= Q428), C427 (≠ R429), L428 (= L430), S464 (= S477)
- binding nicotinamide-adenine-dinucleotide: I669 (= I680), P671 (= P682), W672 (= W683), N673 (= N684), I678 (= I689), K696 (= K707), E699 (= E710), G729 (= G740), G732 (= G744), F746 (= F758), T747 (= T759), G748 (= G760), S749 (= S761), V752 (≠ T764), E776 (= E785), T777 (= T786), C810 (= C819), E906 (= E912), F908 (= F914)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K247), D285 (= D288), Y439 (= Y452), Y451 (= Y464), R454 (= R467), R455 (= R468)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
46% identity, 82% coverage: 22:1009/1209 of query aligns to 12:975/983 of 3hazA
- active site: N652 (= N684), K675 (= K707), E752 (= E785), C786 (= C819), E878 (= E912), A960 (= A994)
- binding flavin-adenine dinucleotide: D272 (= D288), A273 (= A289), Q306 (= Q322), R333 (= R349), V335 (= V351), K336 (= K352), G337 (= G353), A338 (= A354), Y339 (= Y355), W340 (= W356), F358 (= F374), T359 (= T375), R360 (= R376), K361 (= K377), T364 (≠ S380), A387 (= A403), T388 (= T404), H389 (= H405), N390 (= N406), Y435 (= Y452), S460 (= S477), F461 (= F478)
- binding nicotinamide-adenine-dinucleotide: I648 (= I680), S649 (= S681), P650 (= P682), W651 (= W683), N652 (= N684), I657 (= I689), K675 (= K707), P676 (= P708), A677 (= A709), G708 (= G740), G711 (= G744), A712 (= A745), T726 (= T759), G727 (= G760), S728 (= S761), V731 (≠ T764), I735 (= I768), E752 (= E785), T753 (= T786), C786 (= C819), E878 (= E912), F880 (= F914), F948 (= F982)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
46% identity, 82% coverage: 22:1009/1209 of query aligns to 12:966/973 of 6bsnA
- active site: N643 (= N684), E743 (= E785), A777 (≠ C819), A951 (= A994)
- binding dihydroflavine-adenine dinucleotide: D269 (= D288), A270 (= A289), Q303 (= Q322), R330 (= R349), V332 (= V351), K333 (= K352), G334 (= G353), A335 (= A354), Y336 (= Y355), W337 (= W356), F355 (= F374), T356 (= T375), R357 (= R376), K358 (= K377), T361 (≠ S380), A384 (= A403), T385 (= T404), H386 (= H405), N387 (= N406), Y432 (= Y452), S457 (= S477), F458 (= F478)
- binding proline: M630 (vs. gap), W642 (= W683), F644 (= F685), G718 (= G760), R776 (= R818), S778 (= S820), F871 (= F914), I930 (= I973), G931 (= G974), A932 (= A975), F939 (= F982), A958 (≠ R1001), R959 (= R1002), A961 (≠ L1004)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
48% identity, 42% coverage: 14:515/1209 of query aligns to 4:496/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K247), Y433 (= Y452), R448 (= R467), R449 (= R468)
- binding flavin-adenine dinucleotide: D263 (= D288), A264 (= A289), V295 (= V320), Q297 (= Q322), R324 (= R349), V326 (= V351), K327 (= K352), G328 (= G353), A329 (= A354), Y330 (= Y355), W331 (= W356), Y349 (≠ F374), T350 (= T375), R351 (= R376), K352 (= K377), T355 (≠ S380), A378 (= A403), T379 (= T404), H380 (= H405), N381 (= N406), C405 (≠ R429), L406 (= L430), E452 (= E471), S458 (= S477)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
48% identity, 42% coverage: 14:515/1209 of query aligns to 4:492/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (≠ S380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R429), L402 (= L430), E448 (= E471), S454 (= S477)
- binding cyclopropanecarboxylic acid: K218 (= K247), Y429 (= Y452), Y441 (= Y464), R444 (= R467), R445 (= R468)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
48% identity, 42% coverage: 14:515/1209 of query aligns to 4:492/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (≠ S380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R429), L402 (= L430), E448 (= E471), S454 (= S477)
- binding cyclobutanecarboxylic acid: K218 (= K247), L402 (= L430), Y429 (= Y452), Y441 (= Y464), R444 (= R467), R445 (= R468)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
48% identity, 42% coverage: 14:515/1209 of query aligns to 4:492/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (≠ S380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R429), L402 (= L430), E448 (= E471), S454 (= S477)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K247), Y326 (= Y355), Y429 (= Y452), Y441 (= Y464), R444 (= R467), R445 (= R468)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
47% identity, 42% coverage: 14:515/1209 of query aligns to 5:484/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A289), V283 (= V320), Q285 (= Q322), R312 (= R349), V314 (= V351), K315 (= K352), G316 (= G353), A317 (= A354), Y318 (= Y355), W319 (= W356), Y337 (≠ F374), T338 (= T375), R339 (= R376), K340 (= K377), T343 (≠ S380), A366 (= A403), T367 (= T404), H368 (= H405), N369 (= N406), C393 (≠ R429), L394 (= L430), E440 (= E471), S446 (= S477), F447 (= F478)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K247), Y421 (= Y452), R436 (= R467), R437 (= R468)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
32% identity, 69% coverage: 174:1009/1209 of query aligns to 89:946/959 of 5ur2B
- active site: N618 (= N684), K641 (= K707), E722 (= E785), C756 (= C819), E851 (= E912), T931 (≠ A994)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K247), D215 (= D288), M216 (≠ A289), Q249 (= Q322), V278 (= V351), K279 (= K352), G280 (= G353), A281 (= A354), W283 (= W356), Y300 (≠ F374), T301 (= T375), N302 (≠ R376), K303 (= K377), S306 (= S380), A329 (= A403), S330 (≠ T404), H331 (= H405), N332 (= N406), Q356 (= Q428), M357 (≠ R429), L358 (= L430), Y379 (= Y452), E398 (= E471), E403 (≠ S476), W405 (≠ F478)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
46% identity, 42% coverage: 14:515/1209 of query aligns to 4:462/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D288), A230 (= A289), V261 (= V320), Q263 (= Q322), R290 (= R349), V292 (= V351), K293 (= K352), G294 (= G353), A295 (= A354), Y296 (= Y355), W297 (= W356), Y315 (≠ F374), T316 (= T375), R317 (= R376), K318 (= K377), T321 (≠ S380), A344 (= A403), T345 (= T404), H346 (= H405), N347 (= N406), Q370 (= Q428), C371 (≠ R429), L372 (= L430), E418 (= E471), S424 (= S477)
Query Sequence
>GFF2744 FitnessBrowser__Marino:GFF2744
MRPQQSQTPELVDSRQAIRDYYLADEHKVIHEMIAGAQLSQAERDAISARAAELVRSVRK
NAKSTIMEKFLAEYGLTTKEGVALMCLAEALLRVPDNTTIHELIEDKITSGAWGTHVGKA
SSGLINTATVALLMTSNLLKDSERNTVGETLRKLLKRFGEPVIRTVAGQAMKEMGRQFVL
GRDIDEAQDEAKEYMAKGYTYSYDMLGEAARTDDDAKRYYDSYSNAIDSIAKASKGDVRK
NPGISVKLSALLARYEYGNKERVMNELLPRARELVKKAAAANMGFNIDAEEQDRLDLSLD
VIEELVADPELAGWDGFGVVVQAYGKRSSFVLDWLYGLAEKYDRKFMVRLVKGAYWDAEI
KRAQVMGLNGFPVFTRKACSDVSFLSCATKLLNMTNRIYPQFATHNAHSVSAILEMAKTK
GVDNYEFQRLHGMGESLHNEVLKVSGVPCRIYAPVGPHKDLLAYLVRRLLENGANSSFVN
QIVDKRITPEEIAKDPIVSVEEMGNNISSKAIVHPFKLFGDQRRNSKGWDITDPVTVNEI
EKGRGAYKDYRWKGGPLIAGEVAGTEIQVVRNPADPDDLVGHVTQASDADVDTAITSAAA
AFESWSAKSAEERAACVRKVGDLYEENYAELFALTTREAGKSLLDAVAEIREAVDFSQYY
ANEAIRYKDSGDARGVMCCISPWNFPLAIFTGQILANLAAGNTVVAKPAEQTSLLAIRAV
ELMHQAGIPKDAIQLVPGTGATVGAALTSDSRVSGVCFTGSTATAQRINKVMTENMAPDA
PLVAETGGLNAMIVDSTALPEQVVRDVLASSFQSAGQRCSALRMLYVQRDIADGLLEMLY
GAMEELGIGDPWLLSTDVGPVIDENARKKIVDHCEKFERNGKLLKKMKVPEKGLFVSPAV
LSVSGIEELEEEIFGPVLHVATFEAKNIDKVVDDINAKGYGLTFGIHSRVDRRVERITSR
IKVGNTYVNRNQIGAIVGSQPFGGEGLSGTGPKAGGPQYVRRFLKGETVEREADSNARKV
DAKQLQKLIGQLDKLKASRPEARMDAIRPIFGNVPEPLDAHVEALPGPTGETNRLSNHAR
GVVLCLGPDKETALEQAGTALSQGNKVVVIAPGTQDVVDQANKAGLPIVGAQGLLEPEAL
ATIDGFEAVVSCGDQPLLKAYREALAKRDGALLPLITEHTLDQRFVIERHLCVDTTAAGG
NASLIAASE
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