SitesBLAST
Comparing WP_019865045.1 NCBI__GCF_000384075.1:WP_019865045.1 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)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
35% identity, 65% coverage: 229:694/715 of query aligns to 78:540/546 of D9J041
- C122 (= C275) modified: Disulfide link with 127, Redox-active
- C127 (= C280) modified: Disulfide link with 122, Redox-active
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
36% identity, 63% coverage: 237:690/715 of query aligns to 2:450/454 of 5x1yB
- active site: A13 (= A247), V37 (≠ M271), C41 (= C275), C46 (= C280), S49 (= S283), A74 (≠ P308), G75 (≠ P309), Y178 (≠ A416), E182 (= E420), A318 (= A556), A437 (≠ H677), Y439 (= Y679), E444 (= E684)
- binding flavin-adenine dinucleotide: I9 (= I243), G12 (= G246), I32 (= I266), E33 (= E267), R34 (≠ K268), G39 (= G273), T40 (≠ D274), C41 (= C275), G45 (= G279), C46 (= C280), K50 (= K284), A114 (= A348), T138 (= T376), G139 (= G377), Y178 (≠ A416), R266 (= R504), G305 (= G543), D306 (= D544), F313 (= F551), V314 (≠ T552), A317 (= A555)
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
32% identity, 66% coverage: 235:707/715 of query aligns to 167:630/631 of P16171
- Y264 (≠ S332) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y679) mutation to F: 10-fold decrease in activity. 300-fold decrease in activity; when associated with F-264.; mutation to H: 2-fold decrease in activity.
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
34% identity, 76% coverage: 166:707/715 of query aligns to 21:560/561 of P00392
- A110 (≠ V251) binding FAD
- G130 (≠ H269) binding FAD
- T135 (≠ D274) binding FAD
- C136 (= C275) modified: Disulfide link with 141, Redox-active
- C141 (= C280) modified: Disulfide link with 136, Redox-active
- K145 (= K284) binding FAD
- A211 (= A348) binding FAD
- D403 (= D544) binding FAD
- V411 (≠ T552) binding FAD
- C558 (= C705) binding Hg(2+)
- C559 (≠ L706) binding Hg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
35% identity, 64% coverage: 239:696/715 of query aligns to 5:457/466 of 4k8dA
- active site: G13 (≠ A247), I37 (≠ M271), C41 (= C275), C46 (= C280), S49 (= S283), V75 (≠ P308), P76 (= P309), V185 (≠ A416), E189 (= E420), A320 (= A556), F438 (≠ H677), Y440 (= Y679), E445 (= E684)
- binding flavin-adenine dinucleotide: I9 (= I243), G10 (= G244), G12 (= G246), A14 (≠ G248), E33 (= E267), R34 (≠ K268), G39 (= G273), T40 (≠ D274), C41 (= C275), G45 (= G279), C46 (= C280), K50 (= K284), E115 (≠ T347), A116 (= A348), T145 (= T376), G146 (= G377), R268 (= R504), G307 (= G543), D308 (= D544), F315 (= F551), V316 (≠ T552), Y317 (≠ H553)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ G414), S184 (≠ G415), V185 (≠ A416), V186 (≠ I417), E189 (= E420), R206 (= R440), N207 (vs. gap), R212 (= R444), T266 (≠ L502), G267 (= G503), Q314 (= Q550), F315 (= F551), V345 (≠ A584)
Sites not aligning to the query:
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
35% identity, 66% coverage: 239:707/715 of query aligns to 6:466/467 of 4k7zA
- active site: G14 (≠ A247), I38 (≠ M271), A42 (≠ C275), A47 (≠ C280), S50 (= S283), V76 (≠ P308), P77 (= P309), V186 (≠ A416), E190 (= E420), A321 (= A556), F439 (≠ H677), Y441 (= Y679), E446 (= E684), C464 (= C705), C465 (≠ L706)
- binding flavin-adenine dinucleotide: I10 (= I243), G11 (= G244), G13 (= G246), A15 (≠ G248), E34 (= E267), R35 (≠ K268), G40 (= G273), T41 (≠ D274), A42 (≠ C275), G46 (= G279), A47 (≠ C280), K51 (= K284), E116 (≠ T347), A117 (= A348), T146 (= T376), G147 (= G377), R269 (= R504), G308 (= G543), D309 (= D544), Q315 (= Q550), F316 (= F551), V317 (≠ T552), Y318 (≠ H553)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ G414), S185 (≠ G415), V186 (≠ A416), V187 (≠ I417), E190 (= E420), R207 (= R440), N208 (vs. gap), R213 (= R444), T267 (≠ L502), G268 (= G503), R269 (= R504), Q315 (= Q550), F316 (= F551), V346 (≠ A584)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
33% identity, 63% coverage: 238:690/715 of query aligns to 6:438/444 of 4ywoA
- active site: A15 (= A247), I39 (≠ M271), C43 (= C275), C48 (= C280), S51 (= S283), A174 (= A416), E178 (= E420), G308 (≠ A556), H425 (= H677), F427 (≠ Y679), E432 (= E684)
- binding flavin-adenine dinucleotide: G12 (= G244), G14 (= G246), K36 (= K268), G41 (= G273), T42 (≠ D274), C43 (= C275), G47 (= G279), C48 (= C280), K52 (= K284), A110 (= A348), A133 (= A375), T134 (= T376), G135 (= G377), N154 (≠ S396), L175 (≠ I417), L263 (≠ F511), G295 (= G543), D296 (= D544), M302 (≠ Q550), L303 (≠ F551), E304 (≠ T552), A307 (= A555)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
32% identity, 63% coverage: 239:690/715 of query aligns to 8:459/470 of 6uziC
- active site: C45 (= C275), C50 (= C280), S53 (= S283), V187 (≠ A416), E191 (= E420), H448 (≠ Y679), E453 (= E684)
- binding flavin-adenine dinucleotide: I12 (= I243), G13 (= G244), G15 (= G246), P16 (≠ A247), G17 (= G248), E36 (= E267), K37 (= K268), G43 (= G273), T44 (≠ D274), C45 (= C275), G49 (= G279), C50 (= C280), S53 (= S283), K54 (= K284), V117 (≠ T347), G118 (≠ A348), T147 (= T376), G148 (= G377), I188 (= I417), R276 (= R504), D316 (= D544), M322 (≠ Q550), L323 (≠ F551), A324 (≠ T552)
- binding zinc ion: H448 (≠ Y679), E453 (= E684)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
33% identity, 64% coverage: 236:692/715 of query aligns to 8:459/470 of P11959
- 39:47 (vs. 267:275, 56% identical) binding FAD
- K56 (= K284) binding FAD
- D314 (= D544) binding FAD
- A322 (≠ T552) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
33% identity, 64% coverage: 236:692/715 of query aligns to 2:453/455 of 1ebdA
- active site: P13 (≠ A247), L37 (≠ M271), C41 (= C275), C46 (= C280), S49 (= S283), N74 (≠ P308), V75 (≠ P309), Y180 (≠ A416), E184 (= E420), S320 (≠ A556), H438 (= H677), H440 (≠ Y679), E445 (= E684)
- binding flavin-adenine dinucleotide: G10 (= G244), G12 (= G246), P13 (≠ A247), V32 (≠ I266), E33 (= E267), K34 (= K268), G39 (= G273), V40 (≠ D274), C41 (= C275), G45 (= G279), C46 (= C280), K50 (= K284), E112 (≠ T347), A113 (= A348), T141 (= T376), G142 (= G377), Y180 (≠ A416), I181 (= I417), R268 (= R504), D308 (= D544), A314 (≠ Q550), L315 (≠ F551), A316 (≠ T552)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
33% identity, 65% coverage: 234:698/715 of query aligns to 2:456/460 of 2eq6A
- active site: V37 (≠ M271), C41 (= C275), C46 (= C280), T49 (≠ S283), A176 (= A416), E180 (= E420), H435 (= H677), H437 (≠ Y679), E442 (= E684)
- binding flavin-adenine dinucleotide: I9 (= I243), G10 (= G244), G12 (= G246), P13 (≠ A247), G14 (= G248), E33 (= E267), A34 (≠ K268), G39 (= G273), V40 (≠ D274), C41 (= C275), G45 (= G279), C46 (= C280), K50 (= K284), F111 (≠ T347), A112 (= A348), A135 (= A375), T136 (= T376), G137 (= G377), S155 (vs. gap), R269 (≠ N507), D306 (= D544), L312 (≠ Q550), L313 (≠ F551), A314 (≠ T552), H315 (= H553), Y344 (≠ F586)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 64% coverage: 239:695/715 of query aligns to 3:451/455 of 2yquB
- active site: P11 (≠ A247), L36 (≠ M271), C40 (= C275), C45 (= C280), S48 (= S283), G72 (≠ P308), V73 (≠ P309), V177 (≠ A416), E181 (= E420), S314 (≠ W560), H432 (= H677), H434 (≠ Y679), E439 (= E684)
- binding carbonate ion: A310 (= A556), S314 (≠ W560), S423 (≠ G668), D426 (≠ Q671)
- binding flavin-adenine dinucleotide: G8 (= G244), G10 (= G246), P11 (≠ A247), G12 (= G248), E31 (= E267), K32 (= K268), G38 (= G273), T39 (≠ D274), C40 (= C275), R42 (≠ Y277), G44 (= G279), C45 (= C280), K49 (= K284), T110 (= T347), A111 (= A348), T137 (= T376), G138 (= G377), I178 (= I417), Y265 (≠ N507), G301 (= G543), D302 (= D544), M308 (≠ T554), L309 (≠ A555), A310 (= A556), H311 (= H557)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 64% coverage: 239:695/715 of query aligns to 3:451/455 of 2yquA
- active site: P11 (≠ A247), L36 (≠ M271), C40 (= C275), C45 (= C280), S48 (= S283), G72 (≠ P308), V73 (≠ P309), V177 (≠ A416), E181 (= E420), S314 (≠ W560), H432 (= H677), H434 (≠ Y679), E439 (= E684)
- binding flavin-adenine dinucleotide: G8 (= G244), G10 (= G246), P11 (≠ A247), G12 (= G248), E31 (= E267), K32 (= K268), G38 (= G273), T39 (≠ D274), C40 (= C275), R42 (≠ Y277), G44 (= G279), C45 (= C280), K49 (= K284), T110 (= T347), A111 (= A348), T137 (= T376), G138 (= G377), S157 (= S396), I178 (= I417), Y265 (≠ N507), G301 (= G543), D302 (= D544), M308 (≠ T554), L309 (≠ A555), A310 (= A556)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
33% identity, 64% coverage: 239:695/715 of query aligns to 3:451/452 of 2eq7A
- active site: P11 (≠ A247), L36 (≠ M271), C40 (= C275), C45 (= C280), S48 (= S283), G72 (≠ P308), V73 (≠ P309), V177 (≠ A416), E181 (= E420), S314 (≠ W560), H432 (= H677), H434 (≠ Y679), E439 (= E684)
- binding flavin-adenine dinucleotide: G10 (= G246), P11 (≠ A247), G12 (= G248), E31 (= E267), K32 (= K268), G38 (= G273), T39 (≠ D274), C40 (= C275), R42 (≠ Y277), G44 (= G279), C45 (= C280), K49 (= K284), T110 (= T347), A111 (= A348), T137 (= T376), G138 (= G377), S157 (= S396), I178 (= I417), R262 (= R504), Y265 (≠ N507), D302 (= D544), M308 (≠ T554), L309 (≠ A555), A310 (= A556), H311 (= H557), Y341 (≠ F586)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I385), G174 (= G413), G176 (= G415), V177 (≠ A416), I178 (= I417), E197 (= E436), Y198 (≠ I437), V231 (≠ A470), V260 (≠ L502), G261 (= G503), R262 (= R504), M308 (≠ T554), L309 (≠ A555), V339 (≠ A584)
2rabA Structure of glutathione amide reductase from chromatium gracile in complex with NAD (see paper)
33% identity, 63% coverage: 234:684/715 of query aligns to 2:438/451 of 2rabA
- active site: S13 (≠ A247), L37 (≠ M271), C41 (= C275), C46 (= C280), K49 (≠ S283), Y173 (≠ A416), E177 (= E420), I310 (≠ A556), A431 (≠ H677), H433 (≠ Y679), E438 (= E684)
- binding flavin-adenine dinucleotide: G10 (= G244), G12 (= G246), S13 (≠ A247), G14 (= G248), I32 (= I266), E33 (= E267), S34 (≠ K268), T40 (≠ D274), G45 (= G279), C46 (= C280), K49 (≠ S283), H110 (≠ T347), A111 (= A348), T135 (= T376), G136 (= G377), R258 (= R504), G297 (= G543), D298 (= D544), Q304 (= Q550), L305 (≠ F551), T306 (= T552)
- binding nicotinamide-adenine-dinucleotide: K49 (≠ S283), I169 (≠ L412), G172 (= G415), Y173 (≠ A416), I174 (= I417), E177 (= E420), A193 (≠ E436), L194 (≠ I437), E195 (≠ L438), V227 (≠ K471), V256 (≠ L502), G257 (= G503), Q304 (= Q550), V337 (≠ A584)
D0VWY5 Glutathione amide reductase; GAR; EC 1.8.1.16 from Marichromatium gracile (Chromatium gracile) (see 2 papers)
33% identity, 63% coverage: 234:684/715 of query aligns to 3:442/463 of D0VWY5
- Q3 (= Q234) binding Ni(2+)
- H4 (≠ T235) binding Ni(2+)
- SG 14:15 (≠ AG 247:248) binding FAD
- E34 (= E267) binding FAD
- T41 (≠ D274) binding FAD
- C42 (= C275) modified: Disulfide link with 47, Redox-active
- C47 (= C280) modified: Disulfide link with 42, Redox-active
- K50 (≠ S283) binding FAD; binding NAD(+)
- HA 113:114 (≠ TA 347:348) binding FAD
- 174:180 (vs. 414:420, 57% identical) binding NAD(+)
- LE 197:198 (≠ IL 437:438) binding NAD(+)
- V230 (≠ K471) binding NAD(+)
- G261 (= G503) binding NAD(+)
- D302 (= D544) binding FAD
- Q308 (= Q550) binding NAD(+)
- QLT 308:310 (≠ QFT 550:552) binding FAD
- V341 (≠ A584) binding NAD(+)
- H437 (≠ Y679) active site, Proton acceptor; binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 binding Ni(2+)
- 2:463 modified: mature protein, Glutathione amide reductase
P0A9P0 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein; EC 1.8.1.4 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 64% coverage: 240:694/715 of query aligns to 9:460/474 of P0A9P0
- K220 (vs. gap) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
32% identity, 64% coverage: 240:694/715 of query aligns to 8:459/471 of 4jdrA
- active site: P15 (≠ A247), L40 (≠ M271), C44 (= C275), C49 (= C280), S52 (= S283), E77 (≠ P308), P78 (= P309), I184 (≠ A416), E188 (= E420), V324 (≠ A556), H442 (= H677), H444 (≠ Y679), E449 (= E684)
- binding flavin-adenine dinucleotide: G12 (= G244), G14 (= G246), P15 (≠ A247), A16 (≠ G248), E35 (= E267), R36 (≠ K268), Y37 (≠ H269), V43 (≠ D274), C44 (= C275), G48 (= G279), C49 (= C280), K53 (= K284), L115 (≠ T347), G116 (≠ A348), A144 (≠ T376), G145 (= G377), I185 (= I417), G311 (= G543), D312 (= D544), M318 (≠ Q550), L319 (≠ F551), A320 (≠ T552), H321 (= H553)
Sites not aligning to the query:
2r9zB Glutathione amide reductase from chromatium gracile (see paper)
33% identity, 63% coverage: 234:684/715 of query aligns to 2:440/453 of 2r9zB
- active site: S13 (≠ A247), L37 (≠ M271), C41 (= C275), C46 (= C280), K49 (≠ S283), G74 (≠ P309), Y174 (≠ A416), E178 (= E420), I312 (≠ A556), A433 (≠ H677), H435 (≠ Y679), E440 (= E684)
- binding flavin-adenine dinucleotide: G12 (= G246), S13 (≠ A247), G14 (= G248), I32 (= I266), E33 (= E267), S34 (≠ K268), G39 (= G273), T40 (≠ D274), C41 (= C275), G45 (= G279), C46 (= C280), K49 (≠ S283), H111 (≠ T347), A112 (= A348), T136 (= T376), G137 (= G377), I175 (= I417), R260 (= R504), G299 (= G543), D300 (= D544), Q306 (= Q550), L307 (≠ F551), T308 (= T552)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
32% identity, 63% coverage: 239:690/715 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (vs. gap), C39 (= C275), C44 (= C280), S47 (= S283), V183 (≠ A416), E187 (= E420), H443 (= H677), H445 (≠ Y679), E450 (= E684)
- binding flavin-adenine dinucleotide: I6 (= I243), G7 (= G244), G9 (= G246), P10 (≠ A247), G11 (= G248), E30 (= E267), K31 (= K268), G37 (= G273), T38 (≠ D274), C39 (= C275), G43 (= G279), C44 (= C280), K48 (= K284), T111 (= T347), G112 (≠ A348), A140 (= A375), T141 (= T376), G142 (= G377), I184 (= I417), R273 (= R504), G312 (= G543), D313 (= D544), M319 (≠ Q550), L320 (≠ F551), A321 (≠ T552), H322 (= H553)
Query Sequence
>WP_019865045.1 NCBI__GCF_000384075.1:WP_019865045.1
MNPSRILLLAIAAVAISVFFASGGQHYLTLDMLKAQQDNLSAYRDGHRSLTIALYSLLYI
LVTGLSLPGATVMTLAGGALFGLLWGTVIVSFASTIGATLAFLAARFLFREQIQDRFGDR
LKTINEGMAQDGALYLFTLRLVPLFPFFIINLVMGLTAISTRTFYAVSQVGMLAGTLVYV
NAGTQLAQLDSLAGILSPTLVGSFALLGLFPLITQKILALLQARKVYSAWVKPQTFDNNL
VVIGAGAGGLVASYIAAAVKAKVTLIEKHRMGGDCLYTGCVPSKTLIRSAKAAAQIRRSA
EFGIYTSPPDVDFAAVMARVQAVIKAIEPHDSPGRYTELGVDVINGTAKIISPWEVEVNG
DNGSHVITTRAIVIATGAQPFVPEIPGLAETGYLTSDTIWSLQEKPERLLVLGGGAIGCE
LAQAFARLGCRVTQVEILPRLLAREDSEVSEWVESKFRQEGIQVLLGHEAKTFLIENGEK
TLITGQQGQTTRIAFDQVLLALGRSANVSGFGLEALGIRLSPKKTIAIDGFQTTNFPNIY
ACGDAAGPYQFTHTAAHQAWYASVNALFGQVKKFRTDGSAIPQAMFIDPEVARVGLNEQE
AREQGIAYETSTYALEDLDRAIADGATQGFVKVLTKPGKDKILGVTIVGEQASELVAEFV
LAMKHNLGLNQVLGTIHIYPTLAEANKYAAGVWKKQHIPQTALKCLAVYHRWLRH
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