SitesBLAST
Comparing 202865 SO3774 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase, putative (NCBI ptt file) 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)
48% identity, 97% coverage: 25:1046/1059 of query aligns to 9:983/983 of 3hazA
- active site: N652 (= N710), K675 (= K733), E752 (= E811), C786 (= C845), E878 (= E941), A960 (= A1023)
- binding flavin-adenine dinucleotide: D272 (= D300), A273 (= A301), Q306 (= Q334), R333 (= R361), V335 (= V363), K336 (= K364), G337 (= G365), A338 (= A366), Y339 (= Y367), W340 (= W368), F358 (≠ Y386), T359 (= T387), R360 (= R388), K361 (= K389), T364 (= T392), A387 (= A417), T388 (≠ S418), H389 (= H419), N390 (= N420), Y435 (= Y464), S460 (= S489), F461 (= F490)
- binding nicotinamide-adenine-dinucleotide: I648 (= I706), S649 (= S707), P650 (= P708), W651 (= W709), N652 (= N710), I657 (= I715), K675 (= K733), P676 (= P734), A677 (= A735), G708 (= G766), G711 (= G770), A712 (≠ N771), T726 (= T785), G727 (= G786), S728 (= S787), V731 (≠ T790), I735 (= I794), E752 (= E811), T753 (= T812), C786 (= C845), E878 (= E941), F880 (= F943), F948 (= F1011)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 96% coverage: 25:1044/1059 of query aligns to 9:972/973 of 6bsnA
- active site: N643 (= N710), E743 (= E811), A777 (≠ C845), A951 (= A1023)
- binding dihydroflavine-adenine dinucleotide: D269 (= D300), A270 (= A301), Q303 (= Q334), R330 (= R361), V332 (= V363), K333 (= K364), G334 (= G365), A335 (= A366), Y336 (= Y367), W337 (= W368), F355 (≠ Y386), T356 (= T387), R357 (= R388), K358 (= K389), T361 (= T392), A384 (= A417), T385 (≠ S418), H386 (= H419), N387 (= N420), Y432 (= Y464), S457 (= S489), F458 (= F490)
- binding proline: M630 (≠ L697), W642 (= W709), F644 (= F711), G718 (= G786), R776 (= R844), S778 (= S846), F871 (= F943), I930 (= I1002), G931 (= G1003), A932 (= A1004), F939 (= F1011), A958 (≠ T1030), R959 (= R1031), A961 (≠ V1033)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 18:1016/1216 of 6x99A
- active site: N690 (= N710), K713 (= K733), E793 (= E811), C827 (= C845), E923 (= E941), A1005 (= A1023)
- binding d-proline: W557 (= W563), T558 (≠ Q564), E657 (= E663), F691 (= F711), R727 (≠ Q747), R826 (= R844), S828 (= S846), G985 (= G1003), A986 (= A1004), F993 (= F1011)
- binding flavin-adenine dinucleotide: D289 (= D300), A290 (= A301), V321 (= V332), R350 (= R361), V352 (= V363), K353 (= K364), G354 (= G365), A355 (= A366), Y356 (= Y367), W357 (= W368), F375 (≠ Y386), T376 (= T387), R377 (= R388), K378 (= K389), T381 (= T392), A404 (= A417), T405 (≠ S418), H406 (= H419), N407 (= N420), Q430 (= Q439), C431 (≠ R440), Y456 (= Y464), E475 (= E483), S481 (= S489), F482 (= F490)
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, 96% coverage: 20:1034/1059 of query aligns to 18:1018/1218 of 6x9dA
- active site: N692 (= N710), K715 (= K733), E795 (= E811), C829 (= C845), E925 (= E941), A1007 (= A1023)
- binding flavin-adenine dinucleotide: D291 (= D300), A292 (= A301), V323 (= V332), Q325 (= Q334), R352 (= R361), V354 (= V363), K355 (= K364), G356 (= G365), A357 (= A366), Y358 (= Y367), W359 (= W368), F377 (≠ Y386), T378 (= T387), R379 (= R388), K380 (= K389), T383 (= T392), A406 (= A417), T407 (≠ S418), H408 (= H419), N409 (= N420), Q432 (= Q439), C433 (≠ R440), E477 (= E483), S483 (= S489), F484 (= F490)
- binding 4-hydroxyproline: E659 (= E663), F693 (= F711), I697 (= I715), R828 (= R844), S830 (= S846), G987 (= G1003), A988 (= A1004), F995 (= F1011)
- binding nicotinamide-adenine-dinucleotide: I688 (= I706), S689 (= S707), P690 (= P708), W691 (= W709), N692 (= N710), I697 (= I715), K715 (= K733), A717 (= A735), E718 (= E736), G748 (= G766), G751 (= G770), A752 (≠ N771), T766 (= T785), G767 (= G786), S768 (= S787), V771 (≠ T790), E795 (= E811), T796 (= T812), C829 (= C845), E925 (= E941), F927 (= F943), F995 (= F1011)
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, 96% coverage: 20:1034/1059 of query aligns to 18:1014/1214 of 6x9aA
- active site: N688 (= N710), K711 (= K733), E791 (= E811), C825 (= C845), E921 (= E941), A1003 (= A1023)
- binding flavin-adenine dinucleotide: D287 (= D300), A288 (= A301), V319 (= V332), R348 (= R361), V350 (= V363), K351 (= K364), G352 (= G365), A353 (= A366), Y354 (= Y367), W355 (= W368), F373 (≠ Y386), T374 (= T387), R375 (= R388), K376 (= K389), T379 (= T392), A402 (= A417), T403 (≠ S418), H404 (= H419), N405 (= N420), C429 (≠ R440), E473 (= E483), S479 (= S489), F480 (= F490)
- binding (4S)-4-hydroxy-D-proline: W555 (= W563), T556 (≠ Q564), E655 (= E663), F689 (= F711), R725 (≠ Q747), S826 (= S846), G983 (= G1003), A984 (= A1004), F991 (= F1011)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 18:1017/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D300), A291 (= A301), V322 (= V332), Q324 (= Q334), R351 (= R361), V353 (= V363), K354 (= K364), G355 (= G365), A356 (= A366), Y357 (= Y367), W358 (= W368), F376 (≠ Y386), T377 (= T387), R378 (= R388), K379 (= K389), T382 (= T392), A405 (= A417), T406 (≠ S418), H407 (= H419), N408 (= N420), C432 (≠ R440), L433 (= L441), E476 (= E483), S482 (= S489), F483 (= F490)
- binding nicotinamide-adenine-dinucleotide: I687 (= I706), S688 (= S707), P689 (= P708), W690 (= W709), N691 (= N710), I696 (= I715), K714 (= K733), E717 (= E736), G747 (= G766), G750 (= G770), T765 (= T785), G766 (= G786), S767 (= S787), V770 (≠ T790), I774 (= I794), E794 (= E811), T795 (= T812), C828 (= C845), E924 (= E941), F926 (= F943), F994 (= F1011)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K259), Y457 (= Y464), Y469 (= Y476), R472 (= R479), R473 (= R480)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K259), D290 (= D300), Y457 (= Y464), Y469 (= Y476), R472 (= R479), R473 (= R480)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 18:1017/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I706), S688 (= S707), P689 (= P708), W690 (= W709), N691 (= N710), I696 (= I715), K714 (= K733), A716 (= A735), E717 (= E736), G747 (= G766), G750 (= G770), A751 (≠ N771), T765 (= T785), G766 (= G786), S767 (= S787), V770 (≠ T790), E794 (= E811), T795 (= T812), C828 (= C845), E924 (= E941), F926 (= F943), F994 (= F1011)
- 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 (= D300), A291 (= A301), V322 (= V332), Q324 (= Q334), V353 (= V363), K354 (= K364), G355 (= G365), A356 (= A366), W358 (= W368), F376 (≠ Y386), T377 (= T387), R378 (= R388), K379 (= K389), T382 (= T392), A405 (= A417), T406 (≠ S418), H407 (= H419), N408 (= N420), Q431 (= Q439), C432 (≠ R440), L433 (= L441), Y457 (= Y464), E476 (= E483)
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, 96% coverage: 20:1034/1059 of query aligns to 18:1017/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I706), S688 (= S707), P689 (= P708), W690 (= W709), N691 (= N710), K714 (= K733), E717 (= E736), G747 (= G766), G750 (= G770), A751 (≠ N771), F764 (= F784), G766 (= G786), S767 (= S787), V770 (≠ T790), T795 (= T812), G796 (= G813), C828 (= C845), E924 (= E941), F926 (= F943)
- 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 (= K259), D290 (= D300), A291 (= A301), V322 (= V332), Q324 (= Q334), R351 (= R361), V353 (= V363), K354 (= K364), G355 (= G365), A356 (= A366), Y357 (= Y367), W358 (= W368), F376 (≠ Y386), T377 (= T387), R378 (= R388), K379 (= K389), T382 (= T392), A405 (= A417), T406 (≠ S418), H407 (= H419), N408 (= N420), Q431 (= Q439), C432 (≠ R440), L433 (= L441), Y457 (= Y464), S482 (= S489), F483 (= F490)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 17:1013/1209 of 6x9cA
- active site: N687 (= N710), K710 (= K733), E790 (= E811), C824 (= C845), E920 (= E941), A1002 (= A1023)
- binding dihydroflavine-adenine dinucleotide: D286 (= D300), A287 (= A301), V318 (= V332), Q320 (= Q334), R347 (= R361), V349 (= V363), K350 (= K364), G351 (= G365), A352 (= A366), Y353 (= Y367), W354 (= W368), F372 (≠ Y386), T373 (= T387), R374 (= R388), K375 (= K389), T378 (= T392), A401 (= A417), T402 (≠ S418), H403 (= H419), N404 (= N420), Q427 (= Q439), C428 (≠ R440), E472 (= E483), S478 (= S489), F479 (= F490)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I706), S684 (= S707), P685 (= P708), W686 (= W709), N687 (= N710), K710 (= K733), E713 (= E736), G743 (= G766), G746 (= G770), A747 (≠ N771), F760 (= F784), G762 (= G786), S763 (= S787), V766 (≠ T790), E920 (= E941), F922 (= F943)
- binding proline: R823 (= R844), C824 (= C845), S825 (= S846), G982 (= G1003), A983 (= A1004), F990 (= F1011)
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, 96% coverage: 20:1034/1059 of query aligns to 18:1014/1214 of 6x9bA
- active site: N688 (= N710), K711 (= K733), E791 (= E811), C825 (= C845), E921 (= E941), A1003 (= A1023)
- binding flavin-adenine dinucleotide: D287 (= D300), A288 (= A301), V319 (= V332), R348 (= R361), V350 (= V363), K351 (= K364), G352 (= G365), A353 (= A366), Y354 (= Y367), W355 (= W368), F373 (≠ Y386), T374 (= T387), R375 (= R388), K376 (= K389), T379 (= T392), A402 (= A417), T403 (≠ S418), H404 (= H419), N405 (= N420), Q428 (= Q439), C429 (≠ R440), Y454 (= Y464), E473 (= E483), S479 (= S489), F480 (= F490)
- binding nicotinamide-adenine-dinucleotide: I684 (= I706), S685 (= S707), P686 (= P708), W687 (= W709), N688 (= N710), I693 (= I715), K711 (= K733), A713 (= A735), E714 (= E736), G744 (= G766), G747 (= G770), A748 (≠ N771), T762 (= T785), G763 (= G786), S764 (= S787), V767 (≠ T790), I771 (= I794), E791 (= E811), T792 (= T812), C825 (= C845), E921 (= E941), F923 (= F943)
- binding (4R)-4-hydroxy-D-proline: E655 (= E663), F689 (= F711), S826 (= S846), G983 (= G1003), A984 (= A1004), F991 (= F1011)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 18:1016/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D300), A290 (= A301), V321 (= V332), Q323 (= Q334), R350 (= R361), V352 (= V363), K353 (= K364), G354 (= G365), A355 (= A366), Y356 (= Y367), W357 (= W368), F375 (≠ Y386), T376 (= T387), R377 (= R388), K378 (= K389), T381 (= T392), A404 (= A417), T405 (≠ S418), H406 (= H419), N407 (= N420), C431 (≠ R440), L432 (= L441), E475 (= E483), S481 (= S489), F482 (= F490)
- binding nicotinamide-adenine-dinucleotide: I686 (= I706), S687 (= S707), P688 (= P708), W689 (= W709), N690 (= N710), I695 (= I715), K713 (= K733), A715 (= A735), E716 (= E736), G746 (= G766), G749 (= G770), A750 (≠ N771), T764 (= T785), G765 (= G786), S766 (= S787), V769 (≠ T790), E793 (= E811), T794 (= T812), C827 (= C845), E923 (= E941), F925 (= F943), F993 (= F1011)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y464), Y468 (= Y476), R471 (= R479), R472 (= R480)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
48% identity, 96% coverage: 20:1034/1059 of query aligns to 18:1009/1207 of 5kf6A
- active site: N683 (= N710), K706 (= K733), E786 (= E811), C820 (= C845), E916 (= E941), A998 (= A1023)
- binding flavin-adenine dinucleotide: D282 (= D300), A283 (= A301), V314 (= V332), Q316 (= Q334), R343 (= R361), V345 (= V363), K346 (= K364), G347 (= G365), A348 (= A366), Y349 (= Y367), W350 (= W368), F368 (≠ Y386), T369 (= T387), R370 (= R388), K371 (= K389), T374 (= T392), A397 (= A417), T398 (≠ S418), H399 (= H419), N400 (= N420), Q423 (= Q439), C424 (≠ R440), L425 (= L441), E468 (= E483), S474 (= S489), F475 (= F490)
- binding nicotinamide-adenine-dinucleotide: I679 (= I706), S680 (= S707), P681 (= P708), W682 (= W709), N683 (= N710), I688 (= I715), K706 (= K733), A708 (= A735), E709 (= E736), G739 (= G766), G742 (= G770), A743 (≠ N771), F756 (= F784), T757 (= T785), G758 (= G786), S759 (= S787), V762 (≠ T790), I766 (= I794), E786 (= E811), T787 (= T812), C820 (= C845), E916 (= E941), F918 (= F943), F986 (= F1011)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K259), D282 (= D300), Y449 (= Y464), R464 (= R479), R465 (= R480)
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, 96% coverage: 20:1034/1059 of query aligns to 18:999/1197 of 6ufpA
- active site: N673 (= N710), K696 (= K733), E776 (= E811), C810 (= C845), E906 (= E941), A988 (= A1023)
- binding dihydroflavine-adenine dinucleotide: D285 (= D300), A286 (= A301), V317 (= V332), Q319 (= Q334), R346 (= R361), V348 (= V363), K349 (= K364), G350 (= G365), A351 (= A366), W353 (= W368), F371 (≠ Y386), T372 (= T387), R373 (= R388), K374 (= K389), T377 (= T392), A400 (= A417), T401 (≠ S418), H402 (= H419), N403 (= N420), Q426 (= Q439), C427 (≠ R440), L428 (= L441), S464 (= S489)
- binding nicotinamide-adenine-dinucleotide: I669 (= I706), P671 (= P708), W672 (= W709), N673 (= N710), I678 (= I715), K696 (= K733), E699 (= E736), G729 (= G766), G732 (= G770), F746 (= F784), T747 (= T785), G748 (= G786), S749 (= S787), V752 (≠ T790), E776 (= E811), T777 (= T812), C810 (= C845), E906 (= E941), F908 (= F943)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K259), D285 (= D300), Y439 (= Y464), Y451 (= Y476), R454 (= R479), R455 (= R480)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
34% identity, 86% coverage: 127:1041/1059 of query aligns to 23:949/959 of 5ur2B
- active site: N618 (= N710), K641 (= K733), E722 (= E811), C756 (= C845), E851 (= E941), T931 (≠ A1023)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K259), D215 (= D300), M216 (≠ A301), Q249 (= Q334), V278 (= V363), K279 (= K364), G280 (= G365), A281 (= A366), W283 (= W368), Y300 (= Y386), T301 (= T387), N302 (≠ R388), K303 (= K389), S306 (≠ T392), A329 (= A417), S330 (= S418), H331 (= H419), N332 (= N420), Q356 (= Q439), M357 (≠ R440), L358 (= L441), Y379 (= Y464), E398 (= E483), E403 (≠ T488), W405 (≠ F490)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
46% identity, 48% coverage: 23:528/1059 of query aligns to 7:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K259), Y433 (= Y464), R448 (= R479), R449 (= R480)
- binding flavin-adenine dinucleotide: D263 (= D300), A264 (= A301), V295 (= V332), Q297 (= Q334), R324 (= R361), V326 (= V363), K327 (= K364), G328 (= G365), A329 (= A366), Y330 (= Y367), W331 (= W368), Y349 (= Y386), T350 (= T387), R351 (= R388), K352 (= K389), T355 (= T392), A378 (= A417), T379 (≠ S418), H380 (= H419), N381 (= N420), C405 (≠ R440), L406 (= L441), E452 (= E483), S458 (= S489)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
46% identity, 48% coverage: 23:528/1059 of query aligns to 7:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D300), A260 (= A301), V291 (= V332), Q293 (= Q334), R320 (= R361), V322 (= V363), K323 (= K364), G324 (= G365), A325 (= A366), Y326 (= Y367), W327 (= W368), Y345 (= Y386), T346 (= T387), R347 (= R388), K348 (= K389), T351 (= T392), A374 (= A417), T375 (≠ S418), H376 (= H419), N377 (= N420), C401 (≠ R440), L402 (= L441), E448 (= E483), S454 (= S489)
- binding cyclopropanecarboxylic acid: K218 (= K259), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
46% identity, 48% coverage: 23:528/1059 of query aligns to 7:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D300), A260 (= A301), V291 (= V332), Q293 (= Q334), R320 (= R361), V322 (= V363), K323 (= K364), G324 (= G365), A325 (= A366), Y326 (= Y367), W327 (= W368), Y345 (= Y386), T346 (= T387), R347 (= R388), K348 (= K389), T351 (= T392), A374 (= A417), T375 (≠ S418), H376 (= H419), N377 (= N420), C401 (≠ R440), L402 (= L441), E448 (= E483), S454 (= S489)
- binding cyclobutanecarboxylic acid: K218 (= K259), L402 (= L441), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
46% identity, 48% coverage: 23:528/1059 of query aligns to 7:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D300), A260 (= A301), V291 (= V332), Q293 (= Q334), R320 (= R361), V322 (= V363), K323 (= K364), G324 (= G365), A325 (= A366), Y326 (= Y367), W327 (= W368), Y345 (= Y386), T346 (= T387), R347 (= R388), K348 (= K389), T351 (= T392), A374 (= A417), T375 (≠ S418), H376 (= H419), N377 (= N420), C401 (≠ R440), L402 (= L441), E448 (= E483), S454 (= S489)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K259), Y326 (= Y367), Y429 (= Y464), Y441 (= Y476), R444 (= R479), R445 (= R480)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
33% identity, 83% coverage: 173:1046/1059 of query aligns to 85:968/979 of 4nmdA
- active site: N631 (= N710), K654 (= K733), E735 (= E811), C769 (= C845), E865 (= E941), A945 (= A1023)
- binding dihydroflavine-adenine dinucleotide: D226 (= D300), M227 (≠ A301), V256 (= V332), Q258 (= Q334), R285 (= R361), V287 (= V363), K288 (= K364), G289 (= G365), A290 (= A366), W292 (= W368), W309 (≠ Y386), T310 (= T387), I311 (≠ R388), K312 (= K389), S315 (≠ T392), A338 (= A417), S339 (= S418), H340 (= H419), N341 (= N420), Q365 (= Q439), V366 (≠ R440), L367 (= L441), Y388 (= Y464), F414 (= F490)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
33% identity, 82% coverage: 174:1046/1059 of query aligns to 86:966/977 of 4nmaA
- active site: N629 (= N710), K652 (= K733), E733 (= E811), C767 (= C845), E863 (= E941), A943 (= A1023)
- binding flavin-adenine dinucleotide: D226 (= D300), M227 (≠ A301), Q258 (= Q334), R285 (= R361), V287 (= V363), K288 (= K364), G289 (= G365), A290 (= A366), Y291 (= Y367), W292 (= W368), W309 (≠ Y386), T310 (= T387), I311 (≠ R388), K312 (= K389), S315 (≠ T392), A338 (= A417), S339 (= S418), H340 (= H419), N341 (= N420), Q365 (= Q439), L367 (= L441), E407 (= E483), S413 (= S489), F414 (= F490)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K259), Y388 (= Y464), Y400 (= Y476), R403 (= R479), R404 (= R480)
Query Sequence
>202865 SO3774 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase, putative (NCBI ptt file)
MFKASEVLAGRYDSANLDELFKAVTDNYIVDEEQYLSELIKLVPSSDEAIERVTRRAHEL
VNKVRQFEKKGLMVGIDAFLQQYSLETQEGIILMCLAEALLRIPDAATADALIEDKLSGA
KWDEHLSKSDSVLVNASTWGLMLTGKIVSLDKKIDGSSSNLLGRLVNRLGEPVIRQAMMA
AMKIMGKQFVLGRTMKEALKNSEDKRKLGYTHSYDMLGEAALTRKDAEKYFTDYANAITE
LGAQSYNESESPRPTISIKLSALHPRYEVANEDRVLTELYDTVIRLIKLARGLNIGISID
AEEVDRLELSLKLFQKLFNSEATKGWGLLGIVVQAYSKRALPVLVWLTRLAKEQGDEIPV
RLVKGAYWDSELKWAQQAGEAAYPLYTRKAGTDVSYLACARYLLSDATRGAIYPQFASHN
AQTVAAISDMAGDRNHEFQRLHGMGQELYDTILSEAGAKAVRIYAPIGAHKDLLPYLVRR
LLENGANTSFVHKLVDPKTPIESLVVHPLKTLTSYKTLANNKIVLPIDIFGSDRKNSKGL
NMNIISEAEPFFAALDKFKSTQWQAGPLVNGQPLTGEHKTIVSPFDTTQTVGQVAFADKA
AIEQAVSSAHAAFGSWTRTPVEVRASALQKLADLLEENREELIALCTREAGKSIQDGIDE
VREAVDFCRYYAVQAKKLMSKPELLPGPTGELNELFLQGRGVFVCISPWNFPLAIFLGQV
SAALAAGNTVVAKPAEQTSIIGYRAVQLAHQAGIPTDVLQYLPGTGATVGNALTADERIG
GVCFTGSTGTAKLINRTLANREGAIIPLIAETGGQNAMVVDSTSQPEQVVNDVVSSSFTS
AGQRCSALRVLFLQEDIADRVIDVLQGAMDELVIGNPSSIKTDVGPVIDATAKANLDAHI
DHIKQVGKLIKQMSLPAGTENGHFVAPTAVEIDSIKVLEKEHFGPILHVIRYKASELAHV
IDEINSTGFGLTLGIHSRNEGHALEVADKVNVGNVYINRNQIGAVVGVQPFGGQGLSGTG
PKAGGPHYLTRFVTEKTRTNNITAIGGNATLLSLGDSDA
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