SitesBLAST
Comparing WP_040580775.1 NCBI__GCF_000385335.1:WP_040580775.1 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)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
62% identity, 99% coverage: 2:1015/1025 of query aligns to 6:983/983 of 3hazA
- active site: N652 (= N679), K675 (= K702), E752 (= E779), C786 (= C813), E878 (= E910), A960 (= A992)
- binding flavin-adenine dinucleotide: D272 (= D274), A273 (= A275), Q306 (= Q308), R333 (= R335), V335 (= V337), K336 (= K338), G337 (= G339), A338 (= A340), Y339 (= Y341), W340 (= W342), F358 (= F360), T359 (= T361), R360 (= R362), K361 (= K363), T364 (= T366), A387 (= A389), T388 (= T390), H389 (= H391), N390 (= N392), Y435 (= Y437), S460 (= S462), F461 (= F463)
- binding nicotinamide-adenine-dinucleotide: I648 (= I675), S649 (= S676), P650 (= P677), W651 (= W678), N652 (= N679), I657 (= I684), K675 (= K702), P676 (= P703), A677 (= A704), G708 (= G735), G711 (= G738), A712 (= A739), T726 (= T753), G727 (= G754), S728 (= S755), V731 (≠ T758), I735 (= I762), E752 (= E779), T753 (= T780), C786 (= C813), E878 (= E910), F880 (= F912), F948 (= F980)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
62% identity, 99% coverage: 2:1013/1025 of query aligns to 6:972/973 of 6bsnA
- active site: N643 (= N679), E743 (= E779), A777 (≠ C813), A951 (= A992)
- binding dihydroflavine-adenine dinucleotide: D269 (= D274), A270 (= A275), Q303 (= Q308), R330 (= R335), V332 (= V337), K333 (= K338), G334 (= G339), A335 (= A340), Y336 (= Y341), W337 (= W342), F355 (= F360), T356 (= T361), R357 (= R362), K358 (= K363), T361 (= T366), A384 (= A389), T385 (= T390), H386 (= H391), N387 (= N392), Y432 (= Y437), S457 (= S462), F458 (= F463)
- binding proline: M630 (≠ H666), W642 (= W678), F644 (= F680), G718 (= G754), R776 (= R812), S778 (= S814), F871 (= F912), I930 (= I971), G931 (= G972), A932 (= A973), F939 (= F980), A958 (≠ K999), R959 (= R1000), A961 (≠ M1002)
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: 13:1021/1025 of query aligns to 32:1036/1218 of 6x9dA
- active site: N692 (= N679), K715 (= K702), E795 (= E779), C829 (= C813), E925 (= E910), A1007 (= A992)
- binding flavin-adenine dinucleotide: D291 (= D274), A292 (= A275), V323 (≠ A306), Q325 (= Q308), R352 (= R335), V354 (= V337), K355 (= K338), G356 (= G339), A357 (= A340), Y358 (= Y341), W359 (= W342), F377 (= F360), T378 (= T361), R379 (= R362), K380 (= K363), T383 (= T366), A406 (= A389), T407 (= T390), H408 (= H391), N409 (= N392), Q432 (= Q412), C433 (≠ R413), E477 (= E456), S483 (= S462), F484 (= F463)
- binding 4-hydroxyproline: E659 (= E632), F693 (= F680), I697 (= I684), R828 (= R812), S830 (= S814), G987 (= G972), A988 (= A973), F995 (= F980)
- binding nicotinamide-adenine-dinucleotide: I688 (= I675), S689 (= S676), P690 (= P677), W691 (= W678), N692 (= N679), I697 (= I684), K715 (= K702), A717 (= A704), E718 (= E705), G748 (= G735), G751 (= G738), A752 (= A739), T766 (= T753), G767 (= G754), S768 (= S755), V771 (≠ T758), E795 (= E779), T796 (= T780), C829 (= C813), E925 (= E910), F927 (= F912), F995 (= F980)
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: 13:1021/1025 of query aligns to 32:1034/1216 of 6x99A
- active site: N690 (= N679), K713 (= K702), E793 (= E779), C827 (= C813), E923 (= E910), A1005 (= A992)
- binding d-proline: W557 (≠ S533), T558 (≠ V534), E657 (= E632), F691 (= F680), R727 (≠ L716), R826 (= R812), S828 (= S814), G985 (= G972), A986 (= A973), F993 (= F980)
- binding flavin-adenine dinucleotide: D289 (= D274), A290 (= A275), V321 (≠ A306), R350 (= R335), V352 (= V337), K353 (= K338), G354 (= G339), A355 (= A340), Y356 (= Y341), W357 (= W342), F375 (= F360), T376 (= T361), R377 (= R362), K378 (= K363), T381 (= T366), A404 (= A389), T405 (= T390), H406 (= H391), N407 (= N392), Q430 (= Q412), C431 (≠ R413), Y456 (= Y437), E475 (= E456), S481 (= S462), F482 (= F463)
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: 13:1021/1025 of query aligns to 32:1032/1214 of 6x9aA
- active site: N688 (= N679), K711 (= K702), E791 (= E779), C825 (= C813), E921 (= E910), A1003 (= A992)
- binding flavin-adenine dinucleotide: D287 (= D274), A288 (= A275), V319 (≠ A306), R348 (= R335), V350 (= V337), K351 (= K338), G352 (= G339), A353 (= A340), Y354 (= Y341), W355 (= W342), F373 (= F360), T374 (= T361), R375 (= R362), K376 (= K363), T379 (= T366), A402 (= A389), T403 (= T390), H404 (= H391), N405 (= N392), C429 (≠ R413), E473 (= E456), S479 (= S462), F480 (= F463)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ S533), T556 (≠ V534), E655 (= E632), F689 (= F680), R725 (≠ L716), S826 (= S814), G983 (= G972), A984 (= A973), F991 (= F980)
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: 13:1021/1025 of query aligns to 31:1031/1209 of 6x9cA
- active site: N687 (= N679), K710 (= K702), E790 (= E779), C824 (= C813), E920 (= E910), A1002 (= A992)
- binding dihydroflavine-adenine dinucleotide: D286 (= D274), A287 (= A275), V318 (≠ A306), Q320 (= Q308), R347 (= R335), V349 (= V337), K350 (= K338), G351 (= G339), A352 (= A340), Y353 (= Y341), W354 (= W342), F372 (= F360), T373 (= T361), R374 (= R362), K375 (= K363), T378 (= T366), A401 (= A389), T402 (= T390), H403 (= H391), N404 (= N392), Q427 (= Q412), C428 (≠ R413), E472 (= E456), S478 (= S462), F479 (= F463)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I675), S684 (= S676), P685 (= P677), W686 (= W678), N687 (= N679), K710 (= K702), E713 (= E705), G743 (= G735), G746 (= G738), A747 (= A739), F760 (= F752), G762 (= G754), S763 (= S755), V766 (≠ T758), E920 (= E910), F922 (= F912)
- binding proline: R823 (= R812), C824 (= C813), S825 (= S814), G982 (= G972), A983 (= A973), F990 (= F980)
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: 13:1021/1025 of query aligns to 32:1032/1214 of 6x9bA
- active site: N688 (= N679), K711 (= K702), E791 (= E779), C825 (= C813), E921 (= E910), A1003 (= A992)
- binding flavin-adenine dinucleotide: D287 (= D274), A288 (= A275), V319 (≠ A306), R348 (= R335), V350 (= V337), K351 (= K338), G352 (= G339), A353 (= A340), Y354 (= Y341), W355 (= W342), F373 (= F360), T374 (= T361), R375 (= R362), K376 (= K363), T379 (= T366), A402 (= A389), T403 (= T390), H404 (= H391), N405 (= N392), Q428 (= Q412), C429 (≠ R413), Y454 (= Y437), E473 (= E456), S479 (= S462), F480 (= F463)
- binding nicotinamide-adenine-dinucleotide: I684 (= I675), S685 (= S676), P686 (= P677), W687 (= W678), N688 (= N679), I693 (= I684), K711 (= K702), A713 (= A704), E714 (= E705), G744 (= G735), G747 (= G738), A748 (= A739), T762 (= T753), G763 (= G754), S764 (= S755), V767 (≠ T758), I771 (= I762), E791 (= E779), T792 (= T780), C825 (= C813), E921 (= E910), F923 (= F912)
- binding (4R)-4-hydroxy-D-proline: E655 (= E632), F689 (= F680), S826 (= S814), G983 (= G972), A984 (= A973), F991 (= F980)
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: 13:1021/1025 of query aligns to 32:1034/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D274), A290 (= A275), V321 (≠ A306), Q323 (= Q308), R350 (= R335), V352 (= V337), K353 (= K338), G354 (= G339), A355 (= A340), Y356 (= Y341), W357 (= W342), F375 (= F360), T376 (= T361), R377 (= R362), K378 (= K363), T381 (= T366), A404 (= A389), T405 (= T390), H406 (= H391), N407 (= N392), C431 (≠ R413), L432 (= L414), E475 (= E456), S481 (= S462), F482 (= F463)
- binding nicotinamide-adenine-dinucleotide: I686 (= I675), S687 (= S676), P688 (= P677), W689 (= W678), N690 (= N679), I695 (= I684), K713 (= K702), A715 (= A704), E716 (= E705), G746 (= G735), G749 (= G738), A750 (= A739), T764 (= T753), G765 (= G754), S766 (= S755), V769 (≠ T758), E793 (= E779), T794 (= T780), C827 (= C813), E923 (= E910), F925 (= F912), F993 (= F980)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y437), Y468 (= Y449), R471 (= R452), R472 (= R453)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 98% coverage: 13:1021/1025 of query aligns to 32:1035/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D274), A291 (= A275), V322 (≠ A306), Q324 (= Q308), R351 (= R335), V353 (= V337), K354 (= K338), G355 (= G339), A356 (= A340), Y357 (= Y341), W358 (= W342), F376 (= F360), T377 (= T361), R378 (= R362), K379 (= K363), T382 (= T366), A405 (= A389), T406 (= T390), H407 (= H391), N408 (= N392), C432 (≠ R413), L433 (= L414), E476 (= E456), S482 (= S462), F483 (= F463)
- binding nicotinamide-adenine-dinucleotide: I687 (= I675), S688 (= S676), P689 (= P677), W690 (= W678), N691 (= N679), I696 (= I684), K714 (= K702), E717 (= E705), G747 (= G735), G750 (= G738), T765 (= T753), G766 (= G754), S767 (= S755), V770 (≠ T758), I774 (= I762), E794 (= E779), T795 (= T780), C828 (= C813), E924 (= E910), F926 (= F912), F994 (= F980)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K233), Y457 (= Y437), Y469 (= Y449), R472 (= R452), R473 (= R453)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K233), D290 (= D274), Y457 (= Y437), Y469 (= Y449), R472 (= R452), R473 (= R453)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
48% identity, 98% coverage: 13:1021/1025 of query aligns to 32:1035/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I675), S688 (= S676), P689 (= P677), W690 (= W678), N691 (= N679), I696 (= I684), K714 (= K702), A716 (= A704), E717 (= E705), G747 (= G735), G750 (= G738), A751 (= A739), T765 (= T753), G766 (= G754), S767 (= S755), V770 (≠ T758), E794 (= E779), T795 (= T780), C828 (= C813), E924 (= E910), F926 (= F912), F994 (= F980)
- 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 (= D274), A291 (= A275), V322 (≠ A306), Q324 (= Q308), V353 (= V337), K354 (= K338), G355 (= G339), A356 (= A340), W358 (= W342), F376 (= F360), T377 (= T361), R378 (= R362), K379 (= K363), T382 (= T366), A405 (= A389), T406 (= T390), H407 (= H391), N408 (= N392), Q431 (= Q412), C432 (≠ R413), L433 (= L414), Y457 (= Y437), E476 (= E456)
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)
48% identity, 98% coverage: 13:1021/1025 of query aligns to 32:1035/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I675), S688 (= S676), P689 (= P677), W690 (= W678), N691 (= N679), K714 (= K702), E717 (= E705), G747 (= G735), G750 (= G738), A751 (= A739), F764 (= F752), G766 (= G754), S767 (= S755), V770 (≠ T758), T795 (= T780), G796 (= G781), C828 (= C813), E924 (= E910), F926 (= F912)
- 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 (= K233), D290 (= D274), A291 (= A275), V322 (≠ A306), Q324 (= Q308), R351 (= R335), V353 (= V337), K354 (= K338), G355 (= G339), A356 (= A340), Y357 (= Y341), W358 (= W342), F376 (= F360), T377 (= T361), R378 (= R362), K379 (= K363), T382 (= T366), A405 (= A389), T406 (= T390), H407 (= H391), N408 (= N392), Q431 (= Q412), C432 (≠ R413), L433 (= L414), Y457 (= Y437), S482 (= S462), F483 (= F463)
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: 13:1021/1025 of query aligns to 32:1027/1207 of 5kf6A
- active site: N683 (= N679), K706 (= K702), E786 (= E779), C820 (= C813), E916 (= E910), A998 (= A992)
- binding flavin-adenine dinucleotide: D282 (= D274), A283 (= A275), V314 (≠ A306), Q316 (= Q308), R343 (= R335), V345 (= V337), K346 (= K338), G347 (= G339), A348 (= A340), Y349 (= Y341), W350 (= W342), F368 (= F360), T369 (= T361), R370 (= R362), K371 (= K363), T374 (= T366), A397 (= A389), T398 (= T390), H399 (= H391), N400 (= N392), Q423 (= Q412), C424 (≠ R413), L425 (= L414), E468 (= E456), S474 (= S462), F475 (= F463)
- binding nicotinamide-adenine-dinucleotide: I679 (= I675), S680 (= S676), P681 (= P677), W682 (= W678), N683 (= N679), I688 (= I684), K706 (= K702), A708 (= A704), E709 (= E705), G739 (= G735), G742 (= G738), A743 (= A739), F756 (= F752), T757 (= T753), G758 (= G754), S759 (= S755), V762 (≠ T758), I766 (= I762), E786 (= E779), T787 (= T780), C820 (= C813), E916 (= E910), F918 (= F912), F986 (= F980)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K233), D282 (= D274), Y449 (= Y437), R464 (= R452), R465 (= R453)
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: 13:1021/1025 of query aligns to 32:1017/1197 of 6ufpA
- active site: N673 (= N679), K696 (= K702), E776 (= E779), C810 (= C813), E906 (= E910), A988 (= A992)
- binding dihydroflavine-adenine dinucleotide: D285 (= D274), A286 (= A275), V317 (≠ A306), Q319 (= Q308), R346 (= R335), V348 (= V337), K349 (= K338), G350 (= G339), A351 (= A340), W353 (= W342), F371 (= F360), T372 (= T361), R373 (= R362), K374 (= K363), T377 (= T366), A400 (= A389), T401 (= T390), H402 (= H391), N403 (= N392), Q426 (= Q412), C427 (≠ R413), L428 (= L414), S464 (= S462)
- binding nicotinamide-adenine-dinucleotide: I669 (= I675), P671 (= P677), W672 (= W678), N673 (= N679), I678 (= I684), K696 (= K702), E699 (= E705), G729 (= G735), G732 (= G738), F746 (= F752), T747 (= T753), G748 (= G754), S749 (= S755), V752 (≠ T758), E776 (= E779), T777 (= T780), C810 (= C813), E906 (= E910), F908 (= F912)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K233), D285 (= D274), Y439 (= Y437), Y451 (= Y449), R454 (= R452), R455 (= R453)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
32% identity, 84% coverage: 151:1011/1025 of query aligns to 81:950/959 of 5ur2B
- active site: N618 (= N679), K641 (= K702), E722 (= E779), C756 (= C813), E851 (= E910), T931 (≠ A992)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K233), D215 (= D274), M216 (≠ A275), Q249 (= Q308), V278 (= V337), K279 (= K338), G280 (= G339), A281 (= A340), W283 (= W342), Y300 (≠ F360), T301 (= T361), N302 (≠ R362), K303 (= K363), S306 (≠ T366), A329 (= A389), S330 (≠ T390), H331 (= H391), N332 (= N392), Q356 (= Q412), M357 (≠ R413), L358 (= L414), Y379 (= Y437), E398 (= E456), E403 (≠ S461), W405 (≠ F463)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
49% identity, 44% coverage: 36:485/1025 of query aligns to 40:481/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K233), Y433 (= Y437), R448 (= R452), R449 (= R453)
- binding flavin-adenine dinucleotide: D263 (= D274), A264 (= A275), V295 (≠ A306), Q297 (= Q308), R324 (= R335), V326 (= V337), K327 (= K338), G328 (= G339), A329 (= A340), Y330 (= Y341), W331 (= W342), Y349 (≠ F360), T350 (= T361), R351 (= R362), K352 (= K363), T355 (= T366), A378 (= A389), T379 (= T390), H380 (= H391), N381 (= N392), C405 (≠ R413), L406 (= L414), E452 (= E456), S458 (= S462)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
49% identity, 44% coverage: 36:485/1025 of query aligns to 40:477/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D274), A260 (= A275), V291 (≠ A306), Q293 (= Q308), R320 (= R335), V322 (= V337), K323 (= K338), G324 (= G339), A325 (= A340), Y326 (= Y341), W327 (= W342), Y345 (≠ F360), T346 (= T361), R347 (= R362), K348 (= K363), T351 (= T366), A374 (= A389), T375 (= T390), H376 (= H391), N377 (= N392), C401 (≠ R413), L402 (= L414), E448 (= E456), S454 (= S462)
- binding cyclopropanecarboxylic acid: K218 (= K233), Y429 (= Y437), Y441 (= Y449), R444 (= R452), R445 (= R453)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
49% identity, 44% coverage: 36:485/1025 of query aligns to 40:477/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D274), A260 (= A275), V291 (≠ A306), Q293 (= Q308), R320 (= R335), V322 (= V337), K323 (= K338), G324 (= G339), A325 (= A340), Y326 (= Y341), W327 (= W342), Y345 (≠ F360), T346 (= T361), R347 (= R362), K348 (= K363), T351 (= T366), A374 (= A389), T375 (= T390), H376 (= H391), N377 (= N392), C401 (≠ R413), L402 (= L414), E448 (= E456), S454 (= S462)
- binding cyclobutanecarboxylic acid: K218 (= K233), L402 (= L414), Y429 (= Y437), Y441 (= Y449), R444 (= R452), R445 (= R453)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
49% identity, 44% coverage: 36:485/1025 of query aligns to 40:477/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D274), A260 (= A275), V291 (≠ A306), Q293 (= Q308), R320 (= R335), V322 (= V337), K323 (= K338), G324 (= G339), A325 (= A340), Y326 (= Y341), W327 (= W342), Y345 (≠ F360), T346 (= T361), R347 (= R362), K348 (= K363), T351 (= T366), A374 (= A389), T375 (= T390), H376 (= H391), N377 (= N392), C401 (≠ R413), L402 (= L414), E448 (= E456), S454 (= S462)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K233), Y326 (= Y341), Y429 (= Y437), Y441 (= Y449), R444 (= R452), R445 (= R453)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
48% identity, 44% coverage: 36:485/1025 of query aligns to 41:469/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A275), V283 (≠ A306), Q285 (= Q308), R312 (= R335), V314 (= V337), K315 (= K338), G316 (= G339), A317 (= A340), Y318 (= Y341), W319 (= W342), Y337 (≠ F360), T338 (= T361), R339 (= R362), K340 (= K363), T343 (= T366), A366 (= A389), T367 (= T390), H368 (= H391), N369 (= N392), C393 (≠ R413), L394 (= L414), E440 (= E456), S446 (= S462), F447 (= F463)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K233), Y421 (= Y437), R436 (= R452), R437 (= R453)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
47% identity, 44% coverage: 36:485/1025 of query aligns to 40:447/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D274), A230 (= A275), V261 (≠ A306), Q263 (= Q308), R290 (= R335), V292 (= V337), K293 (= K338), G294 (= G339), A295 (= A340), Y296 (= Y341), W297 (= W342), Y315 (≠ F360), T316 (= T361), R317 (= R362), K318 (= K363), T321 (= T366), A344 (= A389), T345 (= T390), H346 (= H391), N347 (= N392), Q370 (= Q412), C371 (≠ R413), L372 (= L414), E418 (= E456), S424 (= S462)
Query Sequence
>WP_040580775.1 NCBI__GCF_000385335.1:WP_040580775.1
MPLFAAPYAEADEAIAPRLLAATDMDAAALARVDALASRLVSAIRSQSPRLGALEDFLRE
YSLSTDEGLALMVLAEALLRVPDDTTADRLIEDKLTHATFARHAAVSDALLVSASAWALG
VTARMLQKGETAQGIVASLVRRIGMSALRPAARQAMQILGAHFILGRNIEEGLAHSASGD
GRLYRYSFDMLGEGARTSADAVHYMDAYRHAIETIGRESGTASLPQRPGISVKLSALHPR
FELLSRLRVMDELVPRLGSLARLAKDHNLSFTVDAEEADRLELSLDVFAAVLADPALAGW
DGFGLAVQAYQKRAGAVLDYVFDLARRHDRRLMVRLVKGAYWDTEIKRAQERGLTDYPVF
TRKPMTDLNYLSCARQLLDARGHIFPQFATHNALTVASIVEYAGGVDGYEFQRLHGMGAD
LFKALRLDFPDAACRIYAPVGTYRDLLAYLVRRLLENGANSSFVAQVGDPSIPLDILLRH
PQTAIGAGIFRALPLPEDIHGLSRKSARGFEFGARQELDALCKAVGEAPGFYSVASIVAG
GATQQGPSRPVLSPIDGSMIGEVGESSPDLIDRAMRAAQDAFKLWSARPVEERALCLDRM
ADGLEAERSRFLALLQSEAGKTLDDALGELREAVDFCRYYAACARHLFSTSEIMPGPTGE
ENRLTHFGRGTFICISPWNFPLSIFLGQVAAALVAGNAVIAKPAEQTPLIASEAALLLHR
CSVPGAVLQLLPGDGSTGAALVASPHIAGVVFTGSTETAFAINRALAAKDGPIVPFIAET
GGINAMIVDATALPEQVTDDVIASAFRSAGQRCSALRLLCVQEDVADRVITMIAGAAAEL
VVGDPRDLSTHVGPVIDAAARDALETHIAAMKQSARVHFAGSVPAGAPARGFYVAPHIFE
LASVAELEREVFGPVLHVVRYKAAELDALLDAIAAKGYGLTLGIHSRIDATIEHIIARRL
AGNVYVNRSMIGAVVGTQPFGGFGLSGTGPKAGGPNYLKRFMLEETVSINTAAVGGNASL
MSQGG
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