SitesBLAST
Comparing 8501416 FitnessBrowser__Miya:8501416 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)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
64% identity, 100% coverage: 1:1012/1013 of query aligns to 2:977/977 of 4nmaA
- active site: N629 (= N664), K652 (= K687), E733 (= E768), C767 (= C802), E863 (= E898), A943 (≠ T978)
- binding flavin-adenine dinucleotide: D226 (= D249), M227 (= M250), Q258 (= Q283), R285 (= R310), V287 (= V312), K288 (= K313), G289 (= G314), A290 (= A315), Y291 (= Y316), W292 (= W317), W309 (= W334), T310 (= T335), I311 (≠ R336), K312 (= K337), S315 (= S340), A338 (= A363), S339 (= S364), H340 (= H365), N341 (= N366), Q365 (= Q390), L367 (= L392), E407 (= E432), S413 (= S438), F414 (= F439)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K208), Y388 (= Y413), Y400 (= Y425), R403 (= R428), R404 (= R429)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
64% identity, 100% coverage: 1:1012/1013 of query aligns to 3:979/979 of 4nmdA
- active site: N631 (= N664), K654 (= K687), E735 (= E768), C769 (= C802), E865 (= E898), A945 (≠ T978)
- binding dihydroflavine-adenine dinucleotide: D226 (= D249), M227 (= M250), V256 (= V281), Q258 (= Q283), R285 (= R310), V287 (= V312), K288 (= K313), G289 (= G314), A290 (= A315), W292 (= W317), W309 (= W334), T310 (= T335), I311 (≠ R336), K312 (= K337), S315 (= S340), A338 (= A363), S339 (= S364), H340 (= H365), N341 (= N366), Q365 (= Q390), V366 (= V391), L367 (= L392), Y388 (= Y413), F414 (= F439)
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
65% identity, 100% coverage: 5:1012/1013 of query aligns to 2:979/979 of 4nmfB
- active site: N631 (= N664), K654 (= K687), E735 (= E768), C769 (= C802), E865 (= E898), A945 (≠ T978)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K208), Y290 (= Y316), Y387 (= Y413), Y399 (= Y425), R402 (= R428), R403 (= R429)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K208), L366 (= L392), Y399 (= Y425), R402 (= R428)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K208), D225 (= D249), M226 (= M250), V255 (= V281), Q257 (= Q283), R284 (= R310), V286 (= V312), K287 (= K313), G288 (= G314), A289 (= A315), W291 (= W317), W308 (= W334), T309 (= T335), I310 (≠ R336), K311 (= K337), S314 (= S340), A337 (= A363), S338 (= S364), H339 (= H365), N340 (= N366), Q364 (= Q390), L366 (= L392), Y387 (= Y413), E406 (= E432), E411 (= E437), S412 (= S438), F413 (= F439)
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
64% identity, 100% coverage: 1:1012/1013 of query aligns to 3:980/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D249), M227 (= M250), V256 (= V281), Q258 (= Q283), R285 (= R310), V287 (= V312), K288 (= K313), G289 (= G314), A290 (= A315), Y291 (= Y316), W292 (= W317), W309 (= W334), T310 (= T335), I311 (≠ R336), K312 (= K337), S315 (= S340), A338 (= A363), S339 (= S364), H340 (= H365), N341 (= N366), L367 (= L392), Y388 (= Y413), E407 (= E432), S413 (= S438), F414 (= F439)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
64% identity, 100% coverage: 1:1012/1013 of query aligns to 3:972/972 of 4nmeA
- active site: N624 (= N664), K647 (= K687), E728 (= E768), C762 (= C802), E858 (= E898), A938 (≠ T978)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K208), D224 (= D249), M225 (= M250), V254 (= V281), Q256 (= Q283), R283 (= R310), V285 (= V312), K286 (= K313), G287 (= G314), A288 (= A315), W290 (= W317), W307 (= W334), T308 (= T335), I309 (≠ R336), K310 (= K337), S313 (= S340), A336 (= A363), S337 (= S364), H338 (= H365), N339 (= N366), Q363 (= Q390), L365 (= L392), Y383 (= Y413), E402 (= E432), F409 (= F439)
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
64% identity, 100% coverage: 5:1012/1013 of query aligns to 4:973/973 of 4nmfA
- active site: N625 (= N664), K648 (= K687), E729 (= E768), C763 (= C802), E859 (= E898), A939 (≠ T978)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K208), Y287 (= Y316), Y384 (= Y413), Y396 (= Y425), R399 (= R428), R400 (= R429)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K208), D222 (= D249), M223 (= M250), V252 (= V281), Q254 (= Q283), R281 (= R310), V283 (= V312), K284 (= K313), G285 (= G314), A286 (= A315), W288 (= W317), W305 (= W334), T306 (= T335), I307 (≠ R336), K308 (= K337), S311 (= S340), A334 (= A363), S335 (= S364), H336 (= H365), N337 (= N366), Q361 (= Q390), V362 (= V391), L363 (= L392), Y384 (= Y413), E403 (= E432), E408 (= E437), F410 (= F439)
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
61% identity, 99% coverage: 5:1011/1013 of query aligns to 3:941/941 of 4nmcA
- active site: N594 (= N664), K617 (= K687), E698 (= E768), C732 (= C802), E828 (= E898), A908 (≠ T978)
- binding flavin-adenine dinucleotide: D215 (= D249), M216 (= M250), V245 (= V281), Q247 (= Q283), R274 (= R310), V276 (= V312), K277 (= K313), G278 (= G314), A279 (= A315), W281 (= W317), W298 (= W334), T299 (= T335), I300 (≠ R336), K301 (= K337), S304 (= S340), A327 (= A363), S328 (= S364), H329 (= H365), N330 (= N366), L356 (= L392), Y377 (= Y413)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
47% identity, 99% coverage: 5:1006/1013 of query aligns to 6:959/959 of 5ur2B
- active site: N618 (= N664), K641 (= K687), E722 (= E768), C756 (= C802), E851 (= E898), T931 (= T978)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K208), D215 (= D249), M216 (= M250), Q249 (= Q283), V278 (= V312), K279 (= K313), G280 (= G314), A281 (= A315), W283 (= W317), Y300 (≠ W334), T301 (= T335), N302 (≠ R336), K303 (= K337), S306 (= S340), A329 (= A363), S330 (= S364), H331 (= H365), N332 (= N366), Q356 (= Q390), M357 (≠ V391), L358 (= L392), Y379 (= Y413), E398 (= E432), E403 (= E437), W405 (≠ F439)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2eiwA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding proline: E137 (= E618), F185 (= F665), S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2j5nA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding glycine: S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
- binding nicotinamide-adenine-dinucleotide: I180 (= I660), A181 (= A661), P182 (= P662), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), E210 (≠ S690), G240 (≠ S720), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), T289 (≠ M769), C322 (= C802), E417 (= E898), F419 (= F900)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2ej6A
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding d-proline: E137 (= E618), F185 (= F665), S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2eitA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding alanine: S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
- binding nicotinamide-adenine-dinucleotide: I180 (= I660), A181 (= A661), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), E210 (≠ S690), G240 (≠ S720), E241 (≠ S721), G244 (= G724), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), G290 (= G770), C322 (= C802), E417 (= E898), F419 (= F900)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2eiiA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding nicotinamide-adenine-dinucleotide: I180 (= I660), A181 (= A661), P182 (= P662), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), E210 (≠ S690), G240 (≠ S720), E241 (≠ S721), G244 (= G724), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), T289 (≠ M769), C322 (= C802), E417 (= E898), F419 (= F900)
- binding valine: E137 (= E618), F185 (= F665), S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2ehuA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding nicotinamide-adenine-dinucleotide: I180 (= I660), A181 (= A661), P182 (= P662), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), E210 (≠ S690), G240 (≠ S720), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), T289 (≠ M769), C322 (= C802), E417 (= E898), F419 (= F900)
- binding serine: F185 (= F665), C322 (= C802), S323 (= S803), G477 (= G958), A478 (= A959), F485 (= F966)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2ehqA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (= I660), A181 (= A661), P182 (= P662), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), A209 (≠ S689), E210 (≠ S690), V239 (≠ R719), G240 (≠ S720), E241 (≠ S721), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), T289 (≠ M769), C322 (= C802), E417 (= E898), F419 (= F900)
2bhqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound product glutamate. (see paper)
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2bhqA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding glutamic acid: F185 (= F665), I189 (= I669), K321 (= K801), C322 (= C802), S323 (= S803), T476 (= T957), G477 (= G958), A478 (= A959), F485 (= F966)
2bhpA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD. (see paper)
47% identity, 50% coverage: 486:995/1013 of query aligns to 5:514/516 of 2bhpA
- active site: N184 (= N664), K207 (= K687), E288 (= E768), C322 (= C802), E417 (= E898), T497 (= T978)
- binding nicotinamide-adenine-dinucleotide: I180 (= I660), A181 (= A661), P182 (= P662), W183 (= W663), N184 (= N664), I189 (= I669), K207 (= K687), E210 (≠ S690), G240 (≠ S720), E241 (≠ S721), F258 (= F738), T259 (= T739), G260 (= G740), S261 (= S741), V264 (= V744), E288 (= E768), T289 (≠ M769), C322 (= C802), E417 (= E898), F419 (= F900)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
33% identity, 86% coverage: 115:984/1013 of query aligns to 171:1008/1209 of 6x9cA
- active site: N687 (= N664), K710 (= K687), E790 (= E768), C824 (= C802), E920 (= E898), A1002 (≠ T978)
- binding dihydroflavine-adenine dinucleotide: D286 (= D249), A287 (≠ M250), V318 (= V281), Q320 (= Q283), R347 (= R310), V349 (= V312), K350 (= K313), G351 (= G314), A352 (= A315), Y353 (= Y316), W354 (= W317), F372 (≠ W334), T373 (= T335), R374 (= R336), K375 (= K337), T378 (≠ S340), A401 (= A363), T402 (≠ S364), H403 (= H365), N404 (= N366), Q427 (= Q390), C428 (≠ V391), E472 (= E432), S478 (= S438), F479 (= F439)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I660), S684 (≠ A661), P685 (= P662), W686 (= W663), N687 (= N664), K710 (= K687), E713 (≠ S690), G743 (≠ S720), G746 (= G724), A747 (≠ D725), F760 (= F738), G762 (= G740), S763 (= S741), V766 (= V744), E920 (= E898), F922 (= F900)
- binding proline: R823 (≠ K801), C824 (= C802), S825 (= S803), G982 (= G958), A983 (= A959), F990 (= F966)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
33% identity, 86% coverage: 115:984/1013 of query aligns to 174:1011/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D249), A290 (≠ M250), V321 (= V281), Q323 (= Q283), R350 (= R310), V352 (= V312), K353 (= K313), G354 (= G314), A355 (= A315), Y356 (= Y316), W357 (= W317), F375 (≠ W334), T376 (= T335), R377 (= R336), K378 (= K337), T381 (≠ S340), A404 (= A363), T405 (≠ S364), H406 (= H365), N407 (= N366), C431 (≠ V391), L432 (= L392), E475 (= E432), S481 (= S438), F482 (= F439)
- binding nicotinamide-adenine-dinucleotide: I686 (= I660), S687 (≠ A661), P688 (= P662), W689 (= W663), N690 (= N664), I695 (= I669), K713 (= K687), A715 (≠ S689), E716 (≠ S690), G746 (≠ S720), G749 (= G724), A750 (≠ D725), T764 (= T739), G765 (= G740), S766 (= S741), V769 (= V744), E793 (= E768), T794 (≠ M769), C827 (= C802), E923 (= E898), F925 (= F900), F993 (= F966)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y413), Y468 (= Y425), R471 (= R428), R472 (= R429)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
33% identity, 86% coverage: 115:984/1013 of query aligns to 176:1013/1218 of 6x9dA
- active site: N692 (= N664), K715 (= K687), E795 (= E768), C829 (= C802), E925 (= E898), A1007 (≠ T978)
- binding flavin-adenine dinucleotide: D291 (= D249), A292 (≠ M250), V323 (= V281), Q325 (= Q283), R352 (= R310), V354 (= V312), K355 (= K313), G356 (= G314), A357 (= A315), Y358 (= Y316), W359 (= W317), F377 (≠ W334), T378 (= T335), R379 (= R336), K380 (= K337), T383 (≠ S340), A406 (= A363), T407 (≠ S364), H408 (= H365), N409 (= N366), Q432 (= Q390), C433 (≠ V391), E477 (= E432), S483 (= S438), F484 (= F439)
- binding 4-hydroxyproline: E659 (= E618), F693 (= F665), I697 (= I669), R828 (≠ K801), S830 (= S803), G987 (= G958), A988 (= A959), F995 (= F966)
- binding nicotinamide-adenine-dinucleotide: I688 (= I660), S689 (≠ A661), P690 (= P662), W691 (= W663), N692 (= N664), I697 (= I669), K715 (= K687), A717 (≠ S689), E718 (≠ S690), G748 (≠ S720), G751 (= G724), A752 (≠ D725), T766 (= T739), G767 (= G740), S768 (= S741), V771 (= V744), E795 (= E768), T796 (≠ M769), C829 (= C802), E925 (= E898), F927 (= F900), F995 (= F966)
Query Sequence
>8501416 FitnessBrowser__Miya:8501416
MEQHLDARIVERGKEFFKSISGEAPSIFNKGFWTGKVMDWAMQNEGFKVQLFRFVDVLPY
LNTSEALTRHIREYFSADGADVPPVLKWGAGAAGFGGAFTGMLMGKFIRSNIEGMARTFI
IGENTKEAIKGLAKLRKEGFAFTVDLLGEATVSEEEADAYRDGYLEVLDAISREHAKWAP
LTDSTGSTTGPDASQDWGHTPKVNVSIKPSALYSQAKPGDVEGSVQGILSRLVPIYRKIV
EMGGFLCIDMEQLKYREMTLELFKRLRTMPEFRDYPHLSIVLQAYLRCTEHDLDELLAWG
RAERLPFGIRLVKGAYWDYETVMAKQNGWEIPVWTRKPESDICYEKLARRILENNDLVYF
ACASHNVRTISTVMETARALNVPAHRYEFQVLYGMAEPVRKGLKNVAGRVRLYCPYGELI
PGMAYLVRRLLENTANESFLRQSFVDGAELERLLENPQATLERELAAAPPPRSTPAAQPG
IDGLPPFVNESMLDLTIPANRAGFVNAIAEVRGKAGGVIPLFIGGKDVTTDDTIASTNPA
KPAEVIARVCQGGKPEVDAAIEAAQKAFPAWRDTSPADRAMFLHRAADIARRRMFELSAW
QVLEVGKQWDQAFHDVGEGIDFLDYYAHEMLRLGTPRRMGRAPGELNHLFYQPKGIAAVI
APWNFPFAIAIGMAAAAIVTGNPVIFKPSSIASRIGYNLTEIFREAGLPEGVFNYVPGRS
SVMGDYLVEHPQVSMICFTGSMEVGLRIQEKAAKVQPGQMQCKRVIAEMGGKNAIIIDDD
ADLDEAVLQVLYSAFGFQGQKCSACSRVIVLDPIYDRFVERLVKAAQAIKIGPSEDPANY
MGPVADASLQKNILEYVKVAEQEGKVLVKRTDIPAEGCYVPLTIVEGIKPHHRIAQEEIF
GPVLAVMRAGNFDEALAIANGTRFALTGGVFSRSPENLTKARREFRVGNLYLNRGSTGAM
VERQPFGGFKMSGVGSKTGGPDYLLQFMDPRCVTENTMRRGFAPIEEDDDWIG
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