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Comparing 208845 DVU3319 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase 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)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
66% identity, 100% coverage: 1:1005/1006 of query aligns to 1:977/977 of 4nmaA
- active site: N629 (= N657), K652 (= K680), E733 (= E761), C767 (= C795), E863 (= E891), A943 (≠ T971)
- binding flavin-adenine dinucleotide: D226 (= D245), M227 (= M246), Q258 (= Q279), R285 (= R306), V287 (= V308), K288 (= K309), G289 (= G310), A290 (= A311), Y291 (= Y312), W292 (= W313), W309 (= W330), T310 (= T331), I311 (≠ D332), K312 (= K333), S315 (= S336), A338 (= A359), S339 (= S360), H340 (= H361), N341 (= N362), Q365 (= Q386), L367 (= L388), E407 (= E428), S413 (= S434), F414 (= F435)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K204), Y388 (= Y409), Y400 (= Y421), R403 (= R424), R404 (= R425)
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
66% identity, 99% coverage: 6:1005/1006 of query aligns to 2:979/979 of 4nmfB
- active site: N631 (= N657), K654 (= K680), E735 (= E761), C769 (= C795), E865 (= E891), A945 (≠ T971)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K204), Y290 (= Y312), Y387 (= Y409), Y399 (= Y421), R402 (= R424), R403 (= R425)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K204), L366 (= L388), Y399 (= Y421), R402 (= R424)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K204), D225 (= D245), M226 (= M246), V255 (= V277), Q257 (= Q279), R284 (= R306), V286 (= V308), K287 (= K309), G288 (= G310), A289 (= A311), W291 (= W313), W308 (= W330), T309 (= T331), I310 (≠ D332), K311 (= K333), S314 (= S336), A337 (= A359), S338 (= S360), H339 (= H361), N340 (= N362), Q364 (= Q386), L366 (= L388), Y387 (= Y409), E406 (= E428), E411 (= E433), S412 (= S434), F413 (= F435)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
66% identity, 100% coverage: 1:1005/1006 of query aligns to 2:979/979 of 4nmdA
- active site: N631 (= N657), K654 (= K680), E735 (= E761), C769 (= C795), E865 (= E891), A945 (≠ T971)
- binding dihydroflavine-adenine dinucleotide: D226 (= D245), M227 (= M246), V256 (= V277), Q258 (= Q279), R285 (= R306), V287 (= V308), K288 (= K309), G289 (= G310), A290 (= A311), W292 (= W313), W309 (= W330), T310 (= T331), I311 (≠ D332), K312 (= K333), S315 (= S336), A338 (= A359), S339 (= S360), H340 (= H361), N341 (= N362), Q365 (= Q386), V366 (= V387), L367 (= L388), Y388 (= Y409), F414 (= F435)
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
66% identity, 100% coverage: 1:1005/1006 of query aligns to 2:980/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D245), M227 (= M246), V256 (= V277), Q258 (= Q279), R285 (= R306), V287 (= V308), K288 (= K309), G289 (= G310), A290 (= A311), Y291 (= Y312), W292 (= W313), W309 (= W330), T310 (= T331), I311 (≠ D332), K312 (= K333), S315 (= S336), A338 (= A359), S339 (= S360), H340 (= H361), N341 (= N362), L367 (= L388), Y388 (= Y409), E407 (= E428), S413 (= S434), F414 (= F435)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
66% identity, 100% coverage: 1:1005/1006 of query aligns to 2:972/972 of 4nmeA
- active site: N624 (= N657), K647 (= K680), E728 (= E761), C762 (= C795), E858 (= E891), A938 (≠ T971)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K204), D224 (= D245), M225 (= M246), V254 (= V277), Q256 (= Q279), R283 (= R306), V285 (= V308), K286 (= K309), G287 (= G310), A288 (= A311), W290 (= W313), W307 (= W330), T308 (= T331), I309 (≠ D332), K310 (= K333), S313 (= S336), A336 (= A359), S337 (= S360), H338 (= H361), N339 (= N362), Q363 (= Q386), L365 (= L388), Y383 (= Y409), E402 (= E428), F409 (= F435)
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
66% identity, 99% coverage: 6:1005/1006 of query aligns to 4:973/973 of 4nmfA
- active site: N625 (= N657), K648 (= K680), E729 (= E761), C763 (= C795), E859 (= E891), A939 (≠ T971)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K204), Y287 (= Y312), Y384 (= Y409), Y396 (= Y421), R399 (= R424), R400 (= R425)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K204), D222 (= D245), M223 (= M246), V252 (= V277), Q254 (= Q279), R281 (= R306), V283 (= V308), K284 (= K309), G285 (= G310), A286 (= A311), W288 (= W313), W305 (= W330), T306 (= T331), I307 (≠ D332), K308 (= K333), S311 (= S336), A334 (= A359), S335 (= S360), H336 (= H361), N337 (= N362), Q361 (= Q386), V362 (= V387), L363 (= L388), Y384 (= Y409), E403 (= E428), E408 (= E433), F410 (= F435)
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
63% identity, 99% coverage: 6:1004/1006 of query aligns to 3:941/941 of 4nmcA
- active site: N594 (= N657), K617 (= K680), E698 (= E761), C732 (= C795), E828 (= E891), A908 (≠ T971)
- binding flavin-adenine dinucleotide: D215 (= D245), M216 (= M246), V245 (= V277), Q247 (= Q279), R274 (= R306), V276 (= V308), K277 (= K309), G278 (= G310), A279 (= A311), W281 (= W313), W298 (= W330), T299 (= T331), I300 (≠ D332), K301 (= K333), S304 (= S336), A327 (= A359), S328 (= S360), H329 (= H361), N330 (= N362), L356 (= L388), Y377 (= Y409)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
47% identity, 99% coverage: 6:997/1006 of query aligns to 6:957/959 of 5ur2B
- active site: N618 (= N657), K641 (= K680), E722 (= E761), C756 (= C795), E851 (= E891), T931 (= T971)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K204), D215 (= D245), M216 (= M246), Q249 (= Q279), V278 (= V308), K279 (= K309), G280 (= G310), A281 (= A311), W283 (= W313), Y300 (≠ W330), T301 (= T331), N302 (≠ D332), K303 (= K333), S306 (= S336), A329 (= A359), S330 (= S360), H331 (= H361), N332 (= N362), Q356 (= Q386), M357 (≠ V387), L358 (= L388), Y379 (= Y409), E398 (= E428), E403 (= E433), W405 (≠ F435)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2eiwA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding proline: E137 (= E611), F185 (= F658), S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2j5nA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding glycine: S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
- binding nicotinamide-adenine-dinucleotide: I180 (= I653), A181 (= A654), P182 (= P655), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), E210 (≠ S683), G240 (≠ S713), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), T289 (≠ M762), C322 (= C795), E417 (= E891), F419 (= F893)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2ej6A
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding d-proline: E137 (= E611), F185 (= F658), S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2eitA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding alanine: S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
- binding nicotinamide-adenine-dinucleotide: I180 (= I653), A181 (= A654), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), E210 (≠ S683), G240 (≠ S713), E241 (≠ S714), G244 (= G717), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), G290 (= G763), C322 (= C795), E417 (= E891), F419 (= F893)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2eiiA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding nicotinamide-adenine-dinucleotide: I180 (= I653), A181 (= A654), P182 (= P655), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), E210 (≠ S683), G240 (≠ S713), E241 (≠ S714), G244 (= G717), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), T289 (≠ M762), C322 (= C795), E417 (= E891), F419 (= F893)
- binding valine: E137 (= E611), F185 (= F658), S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2ehuA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding nicotinamide-adenine-dinucleotide: I180 (= I653), A181 (= A654), P182 (= P655), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), E210 (≠ S683), G240 (≠ S713), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), T289 (≠ M762), C322 (= C795), E417 (= E891), F419 (= F893)
- binding serine: F185 (= F658), C322 (= C795), S323 (= S796), G477 (= G951), A478 (= A952), F485 (= F959)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2ehqA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (= I653), A181 (= A654), P182 (= P655), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), A209 (≠ S682), E210 (≠ S683), V239 (≠ R712), G240 (≠ S713), E241 (≠ S714), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), T289 (≠ M762), C322 (= C795), E417 (= E891), F419 (= F893)
2bhqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound product glutamate. (see paper)
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2bhqA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding glutamic acid: F185 (= F658), I189 (= I662), K321 (= K794), C322 (= C795), S323 (= S796), T476 (= T950), G477 (= G951), A478 (= A952), F485 (= F959)
2bhpA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD. (see paper)
48% identity, 51% coverage: 479:988/1006 of query aligns to 5:514/516 of 2bhpA
- active site: N184 (= N657), K207 (= K680), E288 (= E761), C322 (= C795), E417 (= E891), T497 (= T971)
- binding nicotinamide-adenine-dinucleotide: I180 (= I653), A181 (= A654), P182 (= P655), W183 (= W656), N184 (= N657), I189 (= I662), K207 (= K680), E210 (≠ S683), G240 (≠ S713), E241 (≠ S714), F258 (= F731), T259 (= T732), G260 (= G733), S261 (= S734), V264 (= V737), E288 (= E761), T289 (≠ M762), C322 (= C795), E417 (= E891), F419 (= F893)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
33% identity, 86% coverage: 116:977/1006 of query aligns to 172:1009/1214 of 6x9bA
- active site: N688 (= N657), K711 (= K680), E791 (= E761), C825 (= C795), E921 (= E891), A1003 (≠ T971)
- binding flavin-adenine dinucleotide: D287 (= D245), A288 (≠ M246), V319 (= V277), R348 (= R306), V350 (= V308), K351 (= K309), G352 (= G310), A353 (= A311), Y354 (= Y312), W355 (= W313), F373 (≠ W330), T374 (= T331), R375 (≠ D332), K376 (= K333), T379 (≠ S336), A402 (= A359), T403 (≠ S360), H404 (= H361), N405 (= N362), Q428 (= Q386), C429 (≠ V387), Y454 (= Y409), E473 (= E428), S479 (= S434), F480 (= F435)
- binding nicotinamide-adenine-dinucleotide: I684 (= I653), S685 (≠ A654), P686 (= P655), W687 (= W656), N688 (= N657), I693 (= I662), K711 (= K680), A713 (≠ S682), E714 (≠ S683), G744 (≠ S713), G747 (= G717), A748 (≠ D718), T762 (= T732), G763 (= G733), S764 (= S734), V767 (= V737), I771 (= I741), E791 (= E761), T792 (≠ M762), C825 (= C795), E921 (= E891), F923 (= F893)
- binding (4R)-4-hydroxy-D-proline: E655 (= E611), F689 (= F658), S826 (= S796), G983 (= G951), A984 (= A952), F991 (= F959)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
33% identity, 86% coverage: 116:977/1006 of query aligns to 172:1009/1214 of 6x9aA
- active site: N688 (= N657), K711 (= K680), E791 (= E761), C825 (= C795), E921 (= E891), A1003 (≠ T971)
- binding flavin-adenine dinucleotide: D287 (= D245), A288 (≠ M246), V319 (= V277), R348 (= R306), V350 (= V308), K351 (= K309), G352 (= G310), A353 (= A311), Y354 (= Y312), W355 (= W313), F373 (≠ W330), T374 (= T331), R375 (≠ D332), K376 (= K333), T379 (≠ S336), A402 (= A359), T403 (≠ S360), H404 (= H361), N405 (= N362), C429 (≠ V387), E473 (= E428), S479 (= S434), F480 (= F435)
- binding (4S)-4-hydroxy-D-proline: W555 (≠ G509), T556 (≠ Q510), E655 (= E611), F689 (= F658), R725 (≠ E694), S826 (= S796), G983 (= G951), A984 (= A952), F991 (= F959)
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: 116:977/1006 of query aligns to 174:1011/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D245), A290 (≠ M246), V321 (= V277), Q323 (= Q279), R350 (= R306), V352 (= V308), K353 (= K309), G354 (= G310), A355 (= A311), Y356 (= Y312), W357 (= W313), F375 (≠ W330), T376 (= T331), R377 (≠ D332), K378 (= K333), T381 (≠ S336), A404 (= A359), T405 (≠ S360), H406 (= H361), N407 (= N362), C431 (≠ V387), L432 (= L388), E475 (= E428), S481 (= S434), F482 (= F435)
- binding nicotinamide-adenine-dinucleotide: I686 (= I653), S687 (≠ A654), P688 (= P655), W689 (= W656), N690 (= N657), I695 (= I662), K713 (= K680), A715 (≠ S682), E716 (≠ S683), G746 (≠ S713), G749 (= G717), A750 (≠ D718), T764 (= T732), G765 (= G733), S766 (= S734), V769 (= V737), E793 (= E761), T794 (≠ M762), C827 (= C795), E923 (= E891), F925 (= F893), F993 (= F959)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y409), Y468 (= Y421), R471 (= R424), R472 (= R425)
Query Sequence
>208845 DVU3319 proline dehydrogenase/delta-1-pyrroline-5-carboxylate dehydrogenase
MDQQHLDGKVVERGKEFFRSISGEAPSIFNKGWWTGKVMDWAMQNEDFKVQLFRFVDVLP
YLNTSESLLRHIREYFATEDADIPPVLKWGAGKAGIGGALTAKLMGMTIRSNIEGMARQF
IIGDNSKEAVKGLAKLRKDGFTFTVDLLGEATVSEEESEAYAQGYHEVVDAIAREQEKWK
ALPGNGPVEGFDWGATPKVNVSIKPSALYSQAKPVDVEGSVRGILSRLVPIYRKVVAMGG
FLCIDMEQLKYKEMTLELFKRLRSDPEFRHYPHLSIVLQAYLRDTEKDLDDLLHWARSEK
LPIGIRLVKGAYWDYETVIAKQNGWEIPVWTDKPESDIAYEKLAHRILENSDIVYFACAS
HNVRTIAAVMETALALNVPEHRYEFQVLYGMAEPVRKGLKNVAGRVRLYCPYGELIPGMA
YLVRRLLENTANESFLRQSFAEGAALERLLENPQKTLHRLLAARPEPRAVEPGPGGLPPF
TNDAMIDFTVPDNRKAFVEALADVRSRFGQTVPLYIGGRDVTTADLIPTTNPAKPAEVVA
SICQAGRPEIDDAIAAAKKAALTWRDTSPADRAAYLRRAADICRKRIWELSAWQVVEVGK
QWDQAYHDVTEGIDFLEYYAREMLRLGAPRRMGRAPGEHNHLFYQPKGIAAVIAPWNFPF
AIAIGMASAAIVTGNPVIFKPSSISSRIGYNLAEVFREAGLPEGVFNYCPGRSSIMGDYL
VEHPDISLICFTGSMEVGLRIQEKAAKVQPGQRQCKRVIAEMGGKNATIIDDDADLDEAV
LQVLYSAFGFQGQKCSACSRVIVLDAIYDRFIERLVKAASSIHIGPSEDPSNYMGPVADA
TLQKNVSDYIRIAEEEGRVLLKRTDLPAEGCYVPLTIVGDIRPEHRIAQEEIFGPVLAVM
RAATFDEALSIANGTRFALTGAVFSRSPEHLDKARREFRVGNLYLNKGSTGALVERQPFG
GFAMSGVGSKTGGPDYLLQFMDPRVVTENTMRRGFTPIDEDDDWIV
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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