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Comparing WP_036264374.1 NCBI__GCF_000746085.1:WP_036264374.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
60% identity, 98% coverage: 8:1023/1033 of query aligns to 6:983/983 of 3hazA
- active site: N652 (= N687), K675 (= K710), E752 (= E787), C786 (= C821), E878 (= E918), A960 (= A1000)
- binding flavin-adenine dinucleotide: D272 (= D281), A273 (= A282), Q306 (= Q315), R333 (= R342), V335 (= V344), K336 (= K345), G337 (= G346), A338 (= A347), Y339 (= Y348), W340 (= W349), F358 (= F367), T359 (= T368), R360 (= R369), K361 (= K370), T364 (= T373), A387 (= A396), T388 (= T397), H389 (= H398), N390 (= N399), Y435 (= Y444), S460 (= S469), F461 (= F470)
- binding nicotinamide-adenine-dinucleotide: I648 (= I683), S649 (= S684), P650 (= P685), W651 (= W686), N652 (= N687), I657 (= I692), K675 (= K710), P676 (= P711), A677 (= A712), G708 (= G743), G711 (= G746), A712 (= A747), T726 (= T761), G727 (= G762), S728 (= S763), V731 (≠ T766), I735 (= I770), E752 (= E787), T753 (= T788), C786 (= C821), E878 (= E918), F880 (= F920), F948 (= F988)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
60% identity, 98% coverage: 8:1021/1033 of query aligns to 6:972/973 of 6bsnA
- active site: N643 (= N687), E743 (= E787), A777 (≠ C821), A951 (= A1000)
- binding dihydroflavine-adenine dinucleotide: D269 (= D281), A270 (= A282), Q303 (= Q315), R330 (= R342), V332 (= V344), K333 (= K345), G334 (= G346), A335 (= A347), Y336 (= Y348), W337 (= W349), F355 (= F367), T356 (= T368), R357 (= R369), K358 (= K370), T361 (= T373), A384 (= A396), T385 (= T397), H386 (= H398), N387 (= N399), Y432 (= Y444), S457 (= S469), F458 (= F470)
- binding proline: M630 (≠ C674), W642 (= W686), F644 (= F688), G718 (= G762), R776 (= R820), S778 (= S822), F871 (= F920), I930 (= I979), G931 (= G980), A932 (= A981), F939 (= F988), A958 (≠ D1007), R959 (= R1008), A961 (≠ C1010)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 55:1033/1214 of 6x9bA
- active site: N688 (= N687), K711 (= K710), E791 (= E787), C825 (= C821), E921 (= E918), A1003 (= A1000)
- binding flavin-adenine dinucleotide: D287 (= D281), A288 (= A282), V319 (≠ A313), R348 (= R342), V350 (= V344), K351 (= K345), G352 (= G346), A353 (= A347), Y354 (= Y348), W355 (= W349), F373 (= F367), T374 (= T368), R375 (= R369), K376 (= K370), T379 (= T373), A402 (= A396), T403 (= T397), H404 (= H398), N405 (= N399), Q428 (= Q419), C429 (≠ R420), Y454 (= Y444), E473 (= E463), S479 (= S469), F480 (= F470)
- binding nicotinamide-adenine-dinucleotide: I684 (= I683), S685 (= S684), P686 (= P685), W687 (= W686), N688 (= N687), I693 (= I692), K711 (= K710), A713 (= A712), E714 (= E713), G744 (= G743), G747 (= G746), A748 (= A747), T762 (= T761), G763 (= G762), S764 (= S763), V767 (≠ T766), I771 (= I770), E791 (= E787), T792 (= T788), C825 (= C821), E921 (= E918), F923 (= F920)
- binding (4R)-4-hydroxy-D-proline: E655 (= E640), F689 (= F688), S826 (= S822), G983 (= G980), A984 (= A981), F991 (= F988)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 55:1033/1214 of 6x9aA
- active site: N688 (= N687), K711 (= K710), E791 (= E787), C825 (= C821), E921 (= E918), A1003 (= A1000)
- binding flavin-adenine dinucleotide: D287 (= D281), A288 (= A282), V319 (≠ A313), R348 (= R342), V350 (= V344), K351 (= K345), G352 (= G346), A353 (= A347), Y354 (= Y348), W355 (= W349), F373 (= F367), T374 (= T368), R375 (= R369), K376 (= K370), T379 (= T373), A402 (= A396), T403 (= T397), H404 (= H398), N405 (= N399), C429 (≠ R420), E473 (= E463), S479 (= S469), F480 (= F470)
- binding (4S)-4-hydroxy-D-proline: W555 (vs. gap), T556 (vs. gap), E655 (= E640), F689 (= F688), R725 (≠ S724), S826 (= S822), G983 (= G980), A984 (= A981), F991 (= F988)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 55:1035/1216 of 6x99A
- active site: N690 (= N687), K713 (= K710), E793 (= E787), C827 (= C821), E923 (= E918), A1005 (= A1000)
- binding d-proline: W557 (vs. gap), T558 (vs. gap), E657 (= E640), F691 (= F688), R727 (≠ S724), R826 (= R820), S828 (= S822), G985 (= G980), A986 (= A981), F993 (= F988)
- binding flavin-adenine dinucleotide: D289 (= D281), A290 (= A282), V321 (≠ A313), R350 (= R342), V352 (= V344), K353 (= K345), G354 (= G346), A355 (= A347), Y356 (= Y348), W357 (= W349), F375 (= F367), T376 (= T368), R377 (= R369), K378 (= K370), T381 (= T373), A404 (= A396), T405 (= T397), H406 (= H398), N407 (= N399), Q430 (= Q419), C431 (≠ R420), Y456 (= Y444), E475 (= E463), S481 (= S469), F482 (= F470)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 54:1032/1209 of 6x9cA
- active site: N687 (= N687), K710 (= K710), E790 (= E787), C824 (= C821), E920 (= E918), A1002 (= A1000)
- binding dihydroflavine-adenine dinucleotide: D286 (= D281), A287 (= A282), V318 (≠ A313), Q320 (= Q315), R347 (= R342), V349 (= V344), K350 (= K345), G351 (= G346), A352 (= A347), Y353 (= Y348), W354 (= W349), F372 (= F367), T373 (= T368), R374 (= R369), K375 (= K370), T378 (= T373), A401 (= A396), T402 (= T397), H403 (= H398), N404 (= N399), Q427 (= Q419), C428 (≠ R420), E472 (= E463), S478 (= S469), F479 (= F470)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I683), S684 (= S684), P685 (= P685), W686 (= W686), N687 (= N687), K710 (= K710), E713 (= E713), G743 (= G743), G746 (= G746), A747 (= A747), F760 (≠ I760), G762 (= G762), S763 (= S763), V766 (≠ T766), E920 (= E918), F922 (= F920)
- binding proline: R823 (= R820), C824 (= C821), S825 (= S822), G982 (= G980), A983 (= A981), F990 (= F988)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
50% identity, 94% coverage: 59:1030/1033 of query aligns to 70:1037/1218 of 6x9dA
- active site: N692 (= N687), K715 (= K710), E795 (= E787), C829 (= C821), E925 (= E918), A1007 (= A1000)
- binding flavin-adenine dinucleotide: D291 (= D281), A292 (= A282), V323 (≠ A313), Q325 (= Q315), R352 (= R342), V354 (= V344), K355 (= K345), G356 (= G346), A357 (= A347), Y358 (= Y348), W359 (= W349), F377 (= F367), T378 (= T368), R379 (= R369), K380 (= K370), T383 (= T373), A406 (= A396), T407 (= T397), H408 (= H398), N409 (= N399), Q432 (= Q419), C433 (≠ R420), E477 (= E463), S483 (= S469), F484 (= F470)
- binding 4-hydroxyproline: E659 (= E640), F693 (= F688), I697 (= I692), R828 (= R820), S830 (= S822), G987 (= G980), A988 (= A981), F995 (= F988)
- binding nicotinamide-adenine-dinucleotide: I688 (= I683), S689 (= S684), P690 (= P685), W691 (= W686), N692 (= N687), I697 (= I692), K715 (= K710), A717 (= A712), E718 (= E713), G748 (= G743), G751 (= G746), A752 (= A747), T766 (= T761), G767 (= G762), S768 (= S763), V771 (≠ T766), E795 (= E787), T796 (= T788), C829 (= C821), E925 (= E918), F927 (= F920), F995 (= F988)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
50% identity, 94% coverage: 59:1030/1033 of query aligns to 70:1035/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D281), A290 (= A282), V321 (≠ A313), Q323 (= Q315), R350 (= R342), V352 (= V344), K353 (= K345), G354 (= G346), A355 (= A347), Y356 (= Y348), W357 (= W349), F375 (= F367), T376 (= T368), R377 (= R369), K378 (= K370), T381 (= T373), A404 (= A396), T405 (= T397), H406 (= H398), N407 (= N399), C431 (≠ R420), L432 (= L421), E475 (= E463), S481 (= S469), F482 (= F470)
- binding nicotinamide-adenine-dinucleotide: I686 (= I683), S687 (= S684), P688 (= P685), W689 (= W686), N690 (= N687), I695 (= I692), K713 (= K710), A715 (= A712), E716 (= E713), G746 (= G743), G749 (= G746), A750 (= A747), T764 (= T761), G765 (= G762), S766 (= S763), V769 (≠ T766), E793 (= E787), T794 (= T788), C827 (= C821), E923 (= E918), F925 (= F920), F993 (= F988)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y444), Y468 (= Y456), R471 (= R459), R472 (= R460)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
50% identity, 94% coverage: 59:1030/1033 of query aligns to 70:1036/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I683), S688 (= S684), P689 (= P685), W690 (= W686), N691 (= N687), K714 (= K710), E717 (= E713), G747 (= G743), G750 (= G746), A751 (= A747), F764 (≠ I760), G766 (= G762), S767 (= S763), V770 (≠ T766), T795 (= T788), G796 (= G789), C828 (= C821), E924 (= E918), F926 (= F920)
- 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 (= K240), D290 (= D281), A291 (= A282), V322 (≠ A313), Q324 (= Q315), R351 (= R342), V353 (= V344), K354 (= K345), G355 (= G346), A356 (= A347), Y357 (= Y348), W358 (= W349), F376 (= F367), T377 (= T368), R378 (= R369), K379 (= K370), T382 (= T373), A405 (= A396), T406 (= T397), H407 (= H398), N408 (= N399), Q431 (= Q419), C432 (≠ R420), L433 (= L421), Y457 (= Y444), S482 (= S469), F483 (= F470)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
50% identity, 94% coverage: 59:1030/1033 of query aligns to 70:1036/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D281), A291 (= A282), V322 (≠ A313), Q324 (= Q315), R351 (= R342), V353 (= V344), K354 (= K345), G355 (= G346), A356 (= A347), Y357 (= Y348), W358 (= W349), F376 (= F367), T377 (= T368), R378 (= R369), K379 (= K370), T382 (= T373), A405 (= A396), T406 (= T397), H407 (= H398), N408 (= N399), C432 (≠ R420), L433 (= L421), E476 (= E463), S482 (= S469), F483 (= F470)
- binding nicotinamide-adenine-dinucleotide: I687 (= I683), S688 (= S684), P689 (= P685), W690 (= W686), N691 (= N687), I696 (= I692), K714 (= K710), E717 (= E713), G747 (= G743), G750 (= G746), T765 (= T761), G766 (= G762), S767 (= S763), V770 (≠ T766), I774 (= I770), E794 (= E787), T795 (= T788), C828 (= C821), E924 (= E918), F926 (= F920), F994 (= F988)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K240), Y457 (= Y444), Y469 (= Y456), R472 (= R459), R473 (= R460)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K240), D290 (= D281), Y457 (= Y444), Y469 (= Y456), R472 (= R459), R473 (= R460)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
50% identity, 94% coverage: 59:1030/1033 of query aligns to 70:1036/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I683), S688 (= S684), P689 (= P685), W690 (= W686), N691 (= N687), I696 (= I692), K714 (= K710), A716 (= A712), E717 (= E713), G747 (= G743), G750 (= G746), A751 (= A747), T765 (= T761), G766 (= G762), S767 (= S763), V770 (≠ T766), E794 (= E787), T795 (= T788), C828 (= C821), E924 (= E918), F926 (= F920), F994 (= F988)
- 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 (= D281), A291 (= A282), V322 (≠ A313), Q324 (= Q315), V353 (= V344), K354 (= K345), G355 (= G346), A356 (= A347), W358 (= W349), F376 (= F367), T377 (= T368), R378 (= R369), K379 (= K370), T382 (= T373), A405 (= A396), T406 (= T397), H407 (= H398), N408 (= N399), Q431 (= Q419), C432 (≠ R420), L433 (= L421), Y457 (= Y444), E476 (= E463)
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
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)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 55:1018/1197 of 6ufpA
- active site: N673 (= N687), K696 (= K710), E776 (= E787), C810 (= C821), E906 (= E918), A988 (= A1000)
- binding dihydroflavine-adenine dinucleotide: D285 (= D281), A286 (= A282), V317 (≠ A313), Q319 (= Q315), R346 (= R342), V348 (= V344), K349 (= K345), G350 (= G346), A351 (= A347), W353 (= W349), F371 (= F367), T372 (= T368), R373 (= R369), K374 (= K370), T377 (= T373), A400 (= A396), T401 (= T397), H402 (= H398), N403 (= N399), Q426 (= Q419), C427 (≠ R420), L428 (= L421), S464 (= S469)
- binding nicotinamide-adenine-dinucleotide: I669 (= I683), P671 (= P685), W672 (= W686), N673 (= N687), I678 (= I692), K696 (= K710), E699 (= E713), G729 (= G743), G732 (= G746), F746 (≠ I760), T747 (= T761), G748 (= G762), S749 (= S763), V752 (≠ T766), E776 (= E787), T777 (= T788), C810 (= C821), E906 (= E918), F908 (= F920)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K240), D285 (= D281), Y439 (= Y444), Y451 (= Y456), R454 (= R459), R455 (= R460)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
49% identity, 96% coverage: 43:1030/1033 of query aligns to 55:1028/1207 of 5kf6A
- active site: N683 (= N687), K706 (= K710), E786 (= E787), C820 (= C821), E916 (= E918), A998 (= A1000)
- binding flavin-adenine dinucleotide: D282 (= D281), A283 (= A282), V314 (≠ A313), Q316 (= Q315), R343 (= R342), V345 (= V344), K346 (= K345), G347 (= G346), A348 (= A347), Y349 (= Y348), W350 (= W349), F368 (= F367), T369 (= T368), R370 (= R369), K371 (= K370), T374 (= T373), A397 (= A396), T398 (= T397), H399 (= H398), N400 (= N399), Q423 (= Q419), C424 (≠ R420), L425 (= L421), E468 (= E463), S474 (= S469), F475 (= F470)
- binding nicotinamide-adenine-dinucleotide: I679 (= I683), S680 (= S684), P681 (= P685), W682 (= W686), N683 (= N687), I688 (= I692), K706 (= K710), A708 (= A712), E709 (= E713), G739 (= G743), G742 (= G746), A743 (= A747), F756 (≠ I760), T757 (= T761), G758 (= G762), S759 (= S763), V762 (≠ T766), I766 (= I770), E786 (= E787), T787 (= T788), C820 (= C821), E916 (= E918), F918 (= F920), F986 (= F988)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K240), D282 (= D281), Y449 (= Y444), R464 (= R459), R465 (= R460)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
45% identity, 48% coverage: 9:508/1033 of query aligns to 7:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K240), Y433 (= Y444), R448 (= R459), R449 (= R460)
- binding flavin-adenine dinucleotide: D263 (= D281), A264 (= A282), V295 (≠ A313), Q297 (= Q315), R324 (= R342), V326 (= V344), K327 (= K345), G328 (= G346), A329 (= A347), Y330 (= Y348), W331 (= W349), Y349 (≠ F367), T350 (= T368), R351 (= R369), K352 (= K370), T355 (= T373), A378 (= A396), T379 (= T397), H380 (= H398), N381 (= N399), C405 (≠ R420), L406 (= L421), E452 (= E463), S458 (= S469)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
45% identity, 48% coverage: 9:508/1033 of query aligns to 7:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D281), A260 (= A282), V291 (≠ A313), Q293 (= Q315), R320 (= R342), V322 (= V344), K323 (= K345), G324 (= G346), A325 (= A347), Y326 (= Y348), W327 (= W349), Y345 (≠ F367), T346 (= T368), R347 (= R369), K348 (= K370), T351 (= T373), A374 (= A396), T375 (= T397), H376 (= H398), N377 (= N399), C401 (≠ R420), L402 (= L421), E448 (= E463), S454 (= S469)
- binding cyclopropanecarboxylic acid: K218 (= K240), Y429 (= Y444), Y441 (= Y456), R444 (= R459), R445 (= R460)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
45% identity, 48% coverage: 9:508/1033 of query aligns to 7:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D281), A260 (= A282), V291 (≠ A313), Q293 (= Q315), R320 (= R342), V322 (= V344), K323 (= K345), G324 (= G346), A325 (= A347), Y326 (= Y348), W327 (= W349), Y345 (≠ F367), T346 (= T368), R347 (= R369), K348 (= K370), T351 (= T373), A374 (= A396), T375 (= T397), H376 (= H398), N377 (= N399), C401 (≠ R420), L402 (= L421), E448 (= E463), S454 (= S469)
- binding cyclobutanecarboxylic acid: K218 (= K240), L402 (= L421), Y429 (= Y444), Y441 (= Y456), R444 (= R459), R445 (= R460)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
45% identity, 48% coverage: 9:508/1033 of query aligns to 7:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D281), A260 (= A282), V291 (≠ A313), Q293 (= Q315), R320 (= R342), V322 (= V344), K323 (= K345), G324 (= G346), A325 (= A347), Y326 (= Y348), W327 (= W349), Y345 (≠ F367), T346 (= T368), R347 (= R369), K348 (= K370), T351 (= T373), A374 (= A396), T375 (= T397), H376 (= H398), N377 (= N399), C401 (≠ R420), L402 (= L421), E448 (= E463), S454 (= S469)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K240), Y326 (= Y348), Y429 (= Y444), Y441 (= Y456), R444 (= R459), R445 (= R460)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
45% identity, 48% coverage: 9:508/1033 of query aligns to 8:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A282), V283 (≠ A313), Q285 (= Q315), R312 (= R342), V314 (= V344), K315 (= K345), G316 (= G346), A317 (= A347), Y318 (= Y348), W319 (= W349), Y337 (≠ F367), T338 (= T368), R339 (= R369), K340 (= K370), T343 (= T373), A366 (= A396), T367 (= T397), H368 (= H398), N369 (= N399), C393 (≠ R420), L394 (= L421), E440 (= E463), S446 (= S469), F447 (= F470)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K240), Y421 (= Y444), R436 (= R459), R437 (= R460)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
44% identity, 48% coverage: 9:508/1033 of query aligns to 7:469/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D281), A230 (= A282), V261 (≠ A313), Q263 (= Q315), R290 (= R342), V292 (= V344), K293 (= K345), G294 (= G346), A295 (= A347), Y296 (= Y348), W297 (= W349), Y315 (≠ F367), T316 (= T368), R317 (= R369), K318 (= K370), T321 (= T373), A344 (= A396), T345 (= T397), H346 (= H398), N347 (= N399), Q370 (= Q419), C371 (≠ R420), L372 (= L421), E418 (= E463), S424 (= S469)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
30% identity, 85% coverage: 145:1019/1033 of query aligns to 69:950/959 of 5ur2B
- active site: N618 (= N687), K641 (= K710), E722 (= E787), C756 (= C821), E851 (= E918), T931 (≠ A1000)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K240), D215 (= D281), M216 (≠ A282), Q249 (= Q315), V278 (= V344), K279 (= K345), G280 (= G346), A281 (= A347), W283 (= W349), Y300 (≠ F367), T301 (= T368), N302 (≠ R369), K303 (= K370), S306 (≠ T373), A329 (= A396), S330 (≠ T397), H331 (= H398), N332 (= N399), Q356 (= Q419), M357 (≠ R420), L358 (= L421), Y379 (= Y444), E398 (= E463), E403 (≠ S468), W405 (≠ F470)
Query Sequence
>WP_036264374.1 NCBI__GCF_000746085.1:WP_036264374.1
MTTELGLPAFCAPYAPADALLAAKLLQDARLGDEAEARIDGLASRLIASVRRRSIRIGGL
EDLLREYSLSSEEGLALMVLAEALLRVPDDFTADRLIEDKLASAHWSSHAGGSEALLVSA
AAWALGISARVIEKGKCAEGVVAVLARRIGMGALRAAARQAMALMGSHFVFGQTIEDALY
RAGSAAGWSYRHSFDMLGEGARTMDDAERYYAAYAHAIEAIGVLAEPASSLAARPGISVK
LSALHPRYEAQSRARVLAELTPLVLELACAAKRHDLNFTIDAEEADRLELSLDIVDRLLS
DPTLKDWSGFGLAVQAYQKRASNVIDHVAASARCFNRRLTLRLVKGAYWDSEIKRAQERG
LADYPVFTRKAMTDLNYIACARRLLSLRETIYPQFATHNALSIATIIELAGGVEGYEFQR
LHGMGDDLSAALRSEFPQAACRIYAPVGAHENLLAYLVRRLLENGANSSFVARLGDPHVP
AAELLIRPQTIIGEATNARPPFLPLPEDLHPGRKTAKGVEFGDRQEIGALMAAIAREAGA
FEAAPIVSGAAREGAARAIASPIDGSSIGLVREAAPGLLQEAMREARGGFKIWSRTPVGL
RAACLDRAAQELEAQAPRWLHLLQIEAGKTLEDAIGEWREAIDFCRYYAQEARRRFASPA
PMPGPTGEDNRLFCHGRGVFVCISPWNFPLSIFLGQIAAALAAGNSVLAKPAEQTPLIAA
QAVSLLYRAGVPASVLHLLPGDGDVGAALVALDGVAGVAITGSMDTATKINRSLAAKSGP
IAQLIAETGGVNAMIADATALPEQVCDDVVASAFRSAGQRCSALRLLCLQEDVADRMIAM
IKGAARELLVGDPRALGVHVGPVIDLAAKRSLEAHIEDMRACAIVHYAGRAPSTAPPRGF
YLAPHIFELSSVSDLRREAFGPILHVARYKASELGGLLDSIEAAGFGLTLGVHSRIDAVI
DEIVERRLAGNCYVNRNMIGAVVGTQPFGGFGLSGTGPKAGGPHYLDRFCVEQTVTINTA
AVGGNASLINAGQ
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