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Comparing WP_084058850.1 NCBI__GCF_900176285.1:WP_084058850.1 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)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
55% identity, 100% coverage: 1:991/994 of query aligns to 2:969/977 of 4nmaA
- active site: N629 (= N651), K652 (= K674), E733 (= E755), C767 (= C789), E863 (= E885), A943 (= A965)
- binding flavin-adenine dinucleotide: D226 (= D240), M227 (= M241), Q258 (= Q274), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), Y291 (= Y307), W292 (= W308), W309 (≠ Y325), T310 (= T326), I311 (≠ N327), K312 (= K328), S315 (≠ T331), A338 (= A354), S339 (= S355), H340 (= H356), N341 (= N357), Q365 (= Q381), L367 (= L383), E407 (= E423), S413 (= S429), F414 (= F430)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K199), Y388 (= Y404), Y400 (= Y416), R403 (= R419), R404 (= R420)
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
55% identity, 100% coverage: 1:991/994 of query aligns to 3:971/979 of 4nmdA
- active site: N631 (= N651), K654 (= K674), E735 (= E755), C769 (= C789), E865 (= E885), A945 (= A965)
- binding dihydroflavine-adenine dinucleotide: D226 (= D240), M227 (= M241), V256 (= V272), Q258 (= Q274), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), W292 (= W308), W309 (≠ Y325), T310 (= T326), I311 (≠ N327), K312 (= K328), S315 (≠ T331), A338 (= A354), S339 (= S355), H340 (= H356), N341 (= N357), Q365 (= Q381), V366 (≠ I382), L367 (= L383), Y388 (= Y404), F414 (= F430)
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
55% identity, 99% coverage: 4:991/994 of query aligns to 1:971/979 of 4nmfB
- active site: N631 (= N651), K654 (= K674), E735 (= E755), C769 (= C789), E865 (= E885), A945 (= A965)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K199), Y290 (= Y307), Y387 (= Y404), Y399 (= Y416), R402 (= R419), R403 (= R420)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K199), L366 (= L383), Y399 (= Y416), R402 (= R419)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K199), D225 (= D240), M226 (= M241), V255 (= V272), Q257 (= Q274), R284 (= R301), V286 (= V303), K287 (= K304), G288 (= G305), A289 (= A306), W291 (= W308), W308 (≠ Y325), T309 (= T326), I310 (≠ N327), K311 (= K328), S314 (≠ T331), A337 (= A354), S338 (= S355), H339 (= H356), N340 (= N357), Q364 (= Q381), L366 (= L383), Y387 (= Y404), E406 (= E423), E411 (= E428), S412 (= S429), F413 (= F430)
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
54% identity, 100% coverage: 1:991/994 of query aligns to 3:972/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D240), M227 (= M241), V256 (= V272), Q258 (= Q274), R285 (= R301), V287 (= V303), K288 (= K304), G289 (= G305), A290 (= A306), Y291 (= Y307), W292 (= W308), W309 (≠ Y325), T310 (= T326), I311 (≠ N327), K312 (= K328), S315 (≠ T331), A338 (= A354), S339 (= S355), H340 (= H356), N341 (= N357), L367 (= L383), Y388 (= Y404), E407 (= E423), S413 (= S429), F414 (= F430)
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
55% identity, 97% coverage: 24:991/994 of query aligns to 18:965/973 of 4nmfA
- active site: N625 (= N651), K648 (= K674), E729 (= E755), C763 (= C789), E859 (= E885), A939 (= A965)
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K199), Y287 (= Y307), Y384 (= Y404), Y396 (= Y416), R399 (= R419), R400 (= R420)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K199), D222 (= D240), M223 (= M241), V252 (= V272), Q254 (= Q274), R281 (= R301), V283 (= V303), K284 (= K304), G285 (= G305), A286 (= A306), W288 (= W308), W305 (≠ Y325), T306 (= T326), I307 (≠ N327), K308 (= K328), S311 (≠ T331), A334 (= A354), S335 (= S355), H336 (= H356), N337 (= N357), Q361 (= Q381), V362 (≠ I382), L363 (= L383), Y384 (= Y404), E403 (= E423), E408 (= E428), F410 (= F430)
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
54% identity, 100% coverage: 1:991/994 of query aligns to 3:964/972 of 4nmeA
- active site: N624 (= N651), K647 (= K674), E728 (= E755), C762 (= C789), E858 (= E885), A938 (= A965)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K199), D224 (= D240), M225 (= M241), V254 (= V272), Q256 (= Q274), R283 (= R301), V285 (= V303), K286 (= K304), G287 (= G305), A288 (= A306), W290 (= W308), W307 (≠ Y325), T308 (= T326), I309 (≠ N327), K310 (= K328), S313 (≠ T331), A336 (= A354), S337 (= S355), H338 (= H356), N339 (= N357), Q363 (= Q381), L365 (= L383), Y383 (= Y404), E402 (= E423), F409 (= F430)
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
54% identity, 95% coverage: 47:991/994 of query aligns to 19:934/941 of 4nmcA
- active site: N594 (= N651), K617 (= K674), E698 (= E755), C732 (= C789), E828 (= E885), A908 (= A965)
- binding flavin-adenine dinucleotide: D215 (= D240), M216 (= M241), V245 (= V272), Q247 (= Q274), R274 (= R301), V276 (= V303), K277 (= K304), G278 (= G305), A279 (= A306), W281 (= W308), W298 (≠ Y325), T299 (= T326), I300 (≠ N327), K301 (= K328), S304 (≠ T331), A327 (= A354), S328 (= S355), H329 (= H356), N330 (= N357), L356 (= L383), Y377 (= Y404)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
48% identity, 99% coverage: 3:991/994 of query aligns to 4:957/959 of 5ur2B
- active site: N618 (= N651), K641 (= K674), E722 (= E755), C756 (= C789), E851 (= E885), T931 (≠ A965)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K199), D215 (= D240), M216 (= M241), Q249 (= Q274), V278 (= V303), K279 (= K304), G280 (= G305), A281 (= A306), W283 (= W308), Y300 (= Y325), T301 (= T326), N302 (= N327), K303 (= K328), S306 (≠ T331), A329 (= A354), S330 (= S355), H331 (= H356), N332 (= N357), Q356 (= Q381), M357 (≠ I382), L358 (= L383), Y379 (= Y404), E398 (= E423), E403 (= E428), W405 (≠ F430)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2eiwA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding proline: E137 (= E605), F185 (= F652), S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2j5nA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding glycine: S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ V647), A181 (= A648), P182 (= P649), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), E210 (≠ S677), G240 (= G707), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), T289 (≠ M756), C322 (= C789), E417 (= E885), F419 (= F887)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2ej6A
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding d-proline: E137 (= E605), F185 (= F652), S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2eitA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding alanine: S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ V647), A181 (= A648), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), E210 (≠ S677), G240 (= G707), E241 (≠ A708), G244 (= G711), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), G290 (= G757), C322 (= C789), E417 (= E885), F419 (= F887)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2eiiA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ V647), A181 (= A648), P182 (= P649), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), E210 (≠ S677), G240 (= G707), E241 (≠ A708), G244 (= G711), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), T289 (≠ M756), C322 (= C789), E417 (= E885), F419 (= F887)
- binding valine: E137 (= E605), F185 (= F652), S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2ehuA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ V647), A181 (= A648), P182 (= P649), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), E210 (≠ S677), G240 (= G707), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), T289 (≠ M756), C322 (= C789), E417 (= E885), F419 (= F887)
- binding serine: F185 (= F652), C322 (= C789), S323 (= S790), G477 (= G945), A478 (= A946), F485 (= F953)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2ehqA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (≠ V647), A181 (= A648), P182 (= P649), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), A209 (= A676), E210 (≠ S677), V239 (≠ P706), G240 (= G707), E241 (≠ A708), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), T289 (≠ M756), C322 (= C789), E417 (= E885), F419 (= F887)
2bhqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound product glutamate. (see paper)
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2bhqA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding glutamic acid: F185 (= F652), I189 (= I656), K321 (= K788), C322 (= C789), S323 (= S790), T476 (= T944), G477 (= G945), A478 (= A946), F485 (= F953)
2bhpA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD. (see paper)
49% identity, 51% coverage: 473:982/994 of query aligns to 5:514/516 of 2bhpA
- active site: N184 (= N651), K207 (= K674), E288 (= E755), C322 (= C789), E417 (= E885), T497 (≠ A965)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ V647), A181 (= A648), P182 (= P649), W183 (= W650), N184 (= N651), I189 (= I656), K207 (= K674), E210 (≠ S677), G240 (= G707), E241 (≠ A708), F258 (= F725), T259 (= T726), G260 (= G727), S261 (= S728), V264 (= V731), E288 (= E755), T289 (≠ M756), C322 (= C789), E417 (= E885), F419 (= F887)
9dl8A Bifunctional protein PutA (see paper)
33% identity, 86% coverage: 114:971/994 of query aligns to 168:1005/1206 of 9dl8A
- binding (4-methoxyphenyl)methanol: K242 (= K199), D283 (= D240), A284 (≠ M241), A349 (= A306), Y350 (= Y307), Y450 (= Y404), R466 (= R420)
- binding flavin-adenine dinucleotide: D283 (= D240), A284 (≠ M241), V315 (= V272), Q317 (= Q274), R344 (= R301), V346 (= V303), K347 (= K304), G348 (= G305), A349 (= A306), Y350 (= Y307), W351 (= W308), F369 (≠ Y325), T370 (= T326), R371 (≠ N327), K372 (= K328), T375 (= T331), A398 (= A354), T399 (≠ S355), H400 (= H356), N401 (= N357), C425 (≠ I382), E469 (= E423), S475 (= S429), F476 (= F430)
- binding nicotinamide-adenine-dinucleotide: I680 (≠ V647), S681 (≠ A648), P682 (= P649), W683 (= W650), N684 (= N651), I689 (= I656), K707 (= K674), E710 (≠ S677), G740 (= G707), G743 (= G711), F757 (= F725), T758 (= T726), G759 (= G727), S760 (= S728), V763 (= V731), E787 (= E755), T788 (≠ M756), C821 (= C789), E917 (= E885), F919 (= F887), F987 (= F953)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
33% identity, 86% coverage: 114:971/994 of query aligns to 167:1004/1207 of 5kf6A
- active site: N683 (= N651), K706 (= K674), E786 (= E755), C820 (= C789), E916 (= E885), A998 (= A965)
- binding flavin-adenine dinucleotide: D282 (= D240), A283 (≠ M241), V314 (= V272), Q316 (= Q274), R343 (= R301), V345 (= V303), K346 (= K304), G347 (= G305), A348 (= A306), Y349 (= Y307), W350 (= W308), F368 (≠ Y325), T369 (= T326), R370 (≠ N327), K371 (= K328), T374 (= T331), A397 (= A354), T398 (≠ S355), H399 (= H356), N400 (= N357), Q423 (= Q381), C424 (≠ I382), L425 (= L383), E468 (= E423), S474 (= S429), F475 (= F430)
- binding nicotinamide-adenine-dinucleotide: I679 (≠ V647), S680 (≠ A648), P681 (= P649), W682 (= W650), N683 (= N651), I688 (= I656), K706 (= K674), A708 (= A676), E709 (≠ S677), G739 (= G707), G742 (= G711), A743 (≠ D712), F756 (= F725), T757 (= T726), G758 (= G727), S759 (= S728), V762 (= V731), I766 (= I735), E786 (= E755), T787 (≠ M756), C820 (= C789), E916 (= E885), F918 (= F887), F986 (= F953)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K199), D282 (= D240), Y449 (= Y404), R464 (= R419), R465 (= R420)
9e0cA Bifunctional protein PutA (see paper)
33% identity, 86% coverage: 114:971/994 of query aligns to 174:1011/1216 of 9e0cA
- binding (1-benzofuran-5-yl)methanol: K248 (= K199), D289 (= D240), Y356 (= Y307), Y456 (= Y404)
- binding flavin-adenine dinucleotide: D289 (= D240), A290 (≠ M241), V321 (= V272), R350 (= R301), V352 (= V303), K353 (= K304), G354 (= G305), A355 (= A306), Y356 (= Y307), W357 (= W308), F375 (≠ Y325), T376 (= T326), R377 (≠ N327), K378 (= K328), T381 (= T331), A404 (= A354), T405 (≠ S355), H406 (= H356), N407 (= N357), Q430 (= Q381), C431 (≠ I382), E475 (= E423), S481 (= S429), F482 (= F430)
- binding nicotinamide-adenine-dinucleotide: I686 (≠ V647), S687 (≠ A648), P688 (= P649), W689 (= W650), N690 (= N651), I695 (= I656), K713 (= K674), A715 (= A676), E716 (≠ S677), G746 (= G707), G749 (= G711), A750 (≠ D712), F763 (= F725), T764 (= T726), G765 (= G727), S766 (= S728), V769 (= V731), I773 (= I735), E793 (= E755), T794 (≠ M756), C827 (= C789), E923 (= E885), F925 (= F887), F993 (= F953)
Query Sequence
>WP_084058850.1 NCBI__GCF_900176285.1:WP_084058850.1
MGNDLEKRIRQTGLWLFQLIEDETPSIFKKDYWTGKVMEWCMQNEAFKVEMFRFVDVFPY
LTRPESVAKHLQEYFCRPDQSFPVALQWGLRHLSPTSMAAKMVAKSMAKNIANMGLQFIA
GADAAEALPVLEKMRGQGLAFTADLLGEAVVSRQEEEEYLGRYLDLFDVLGKAAEGWEAL
GGAADLDWGWSPKVNVSIKPSAMYSQMNACAFDYSVDRAKERLRPIFRRAMEQGAFVCLD
MEHTALKNITLGLYKSLMEEAEFRGYPHTGLVIQAYLRDSEADLRDLIGWAKKNKQPVTV
RLVKGAYWDAEYIWARQNHWPIRVYTNKYHTDANFEKLARLLMENHAQVRFACASHNIRS
LAYVIELSKDLRVPEDRIEYQILYGMAEPVRTALKKAGLPLRLYTPIGEMIPGMAYLVRR
LLENTSNESFLRLSFSEGVSREELLRNPVDLAAEHPEAPHPARSVPDYGDKGPFENEPPW
DWTLAEVRQAFEKTLRKLPKEFPVKVPLVINDKKVQTQETFSSTNPNRTDQVVGVVASAG
EKKAREAVAAAKEAFAAWRDTPPRERAEYLFRAAQAARSRRYELAALQVYEVGKSWKEAD
GDVCEAIDFLEYYGREMIRLGAPRRMGNVPGEVSHLFYEPRGVAAVVAPWNFPFAISVGM
TSAALVTGNTVVYKPASQSPVIGYWLYRIFQEAKLPKGVLNFLPGPGAKIGDFLVTHPDV
AMIAFTGSKEVGLRIIERAAKTPPDAHFVKNVVAEMGGKNAIIIDADADLDEAVVHVLHS
AFGYQGQKCSACSRLIVLEENYHKLLERLRAAAESLELGPVEDAKNVMGAVIDAKAREKI
LEYIEIGKREGKVLVERPVEGSNGYFVPLTIFTDIRPEHRLAQEEIFGPVLSVMKVRDFD
EALEVANSTQYALTGAVFSRSPENIEKARRRFRVGNLYINRGSTGAIVERHPFGGFKMSG
VGSKAGGPDYLLQFMVPRNVAENTMRRGFAPRDA
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