SitesBLAST
Comparing Echvi_4481 Echvi_4481 mercuric reductase 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)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
39% identity, 83% coverage: 109:646/647 of query aligns to 7:545/546 of D9J041
- C122 (= C226) modified: Disulfide link with 127, Redox-active
- C127 (= C231) modified: Disulfide link with 122, Redox-active
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
34% identity, 96% coverage: 27:646/647 of query aligns to 6:630/631 of P16171
- Y264 (= Y283) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y621) 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.
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
40% identity, 69% coverage: 188:636/647 of query aligns to 4:454/454 of 5x1yB
- active site: A13 (≠ S197), V37 (≠ I222), C41 (= C226), C46 (= C231), S49 (= S234), A74 (≠ N259), G75 (≠ P260), Y178 (= Y364), E182 (= E368), A318 (= A500), A437 (≠ H619), Y439 (= Y621), E444 (= E626)
- binding flavin-adenine dinucleotide: I9 (= I193), G12 (= G196), I32 (≠ V216), E33 (≠ N217), R34 (≠ A218), G39 (= G224), T40 (= T225), C41 (= C226), G45 (= G230), C46 (= C231), K50 (= K235), A114 (= A300), T138 (= T324), G139 (= G325), Y178 (= Y364), R266 (≠ T448), G305 (= G487), D306 (= D488), F313 (= F495), V314 (= V496), A317 (= A499)
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
41% identity, 83% coverage: 108:646/647 of query aligns to 4:560/561 of P00392
- A110 (= A199) binding
- G130 (= G219) binding
- T135 (= T225) binding
- C136 (= C226) modified: Disulfide link with 141, Redox-active
- C141 (= C231) modified: Disulfide link with 136, Redox-active
- K145 (= K235) binding
- A211 (= A300) binding
- D403 (= D488) binding
- V411 (= V496) binding
- C558 (= C644) binding
- C559 (= C645) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
45% identity, 70% coverage: 192:646/647 of query aligns to 9:466/467 of 4k7zA
- active site: G14 (≠ S197), I38 (= I222), A42 (≠ C226), A47 (≠ C231), S50 (= S234), V76 (≠ N259), P77 (= P260), V186 (≠ Y364), E190 (= E368), A321 (= A500), F439 (≠ H619), Y441 (= Y621), E446 (= E626), C464 (= C644), C465 (= C645)
- binding flavin-adenine dinucleotide: I10 (= I193), G11 (= G194), G13 (= G196), A15 (= A198), E34 (≠ N217), R35 (≠ A218), G40 (= G224), T41 (= T225), A42 (≠ C226), G46 (= G230), A47 (≠ C231), K51 (= K235), E116 (≠ W299), A117 (= A300), T146 (= T324), G147 (= G325), R269 (≠ T448), G308 (= G487), D309 (= D488), Q315 (≠ A494), F316 (= F495), V317 (= V496), Y318 (= Y497)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ A362), S185 (≠ G363), V186 (≠ Y364), V187 (≠ I365), E190 (= E368), R207 (= R385), N208 (≠ S386), R213 (= R391), T267 (= T446), G268 (= G447), R269 (≠ T448), Q315 (≠ A494), F316 (= F495), V346 (= V526)
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
45% identity, 70% coverage: 192:646/647 of query aligns to 8:465/466 of 4k8dA
- active site: G13 (≠ S197), I37 (= I222), C41 (= C226), C46 (= C231), S49 (= S234), V75 (≠ N259), P76 (= P260), V185 (≠ Y364), E189 (= E368), A320 (= A500), F438 (≠ H619), Y440 (= Y621), E445 (= E626), A463 (≠ C644), A464 (≠ C645)
- binding flavin-adenine dinucleotide: I9 (= I193), G10 (= G194), G12 (= G196), A14 (= A198), E33 (≠ N217), R34 (≠ A218), G39 (= G224), T40 (= T225), C41 (= C226), G45 (= G230), C46 (= C231), K50 (= K235), E115 (≠ W299), A116 (= A300), T145 (= T324), G146 (= G325), R268 (≠ T448), G307 (= G487), D308 (= D488), F315 (= F495), V316 (= V496), Y317 (= Y497)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ A362), S184 (≠ G363), V185 (≠ Y364), V186 (≠ I365), E189 (= E368), R206 (= R385), N207 (≠ S386), R212 (= R391), T266 (= T446), G267 (= G447), Q314 (≠ A494), F315 (= F495), V345 (= V526)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
34% identity, 70% coverage: 184:638/647 of query aligns to 3:444/444 of 4ywoA
- active site: A15 (≠ S197), I39 (= I222), C43 (= C226), C48 (= C231), S51 (= S234), A174 (≠ Y364), E178 (= E368), G308 (≠ A500), H425 (= H619), F427 (≠ Y621), E432 (= E626)
- binding flavin-adenine dinucleotide: G12 (= G194), G14 (= G196), K36 (≠ A218), G41 (= G224), T42 (= T225), C43 (= C226), G47 (= G230), C48 (= C231), K52 (= K235), A110 (= A300), A133 (= A323), T134 (= T324), G135 (= G325), N154 (= N344), L175 (≠ I365), L263 (= L455), G295 (= G487), D296 (= D488), M302 (≠ A494), L303 (≠ F495), E304 (≠ V496), A307 (= A499)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
36% identity, 70% coverage: 188:638/647 of query aligns to 4:454/460 of 2eq6A
- active site: V37 (≠ I222), C41 (= C226), C46 (= C231), T49 (≠ S234), A176 (≠ Y364), E180 (= E368), H435 (= H619), H437 (≠ Y621), E442 (= E626)
- binding flavin-adenine dinucleotide: I9 (= I193), G10 (= G194), G12 (= G196), P13 (≠ S197), G14 (≠ A198), E33 (≠ N217), A34 (= A218), G39 (= G224), V40 (≠ T225), C41 (= C226), G45 (= G230), C46 (= C231), K50 (= K235), F111 (≠ W299), A112 (= A300), A135 (= A323), T136 (= T324), G137 (= G325), S155 (≠ T343), R269 (≠ N451), D306 (= D488), L312 (≠ A494), L313 (≠ F495), A314 (≠ V496), H315 (≠ Y497), Y344 (≠ F528)
Sites not aligning to the query:
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
36% identity, 68% coverage: 187:626/647 of query aligns to 9:451/470 of P11959
- 39:47 (vs. 217:226, 40% identical) binding
- K56 (= K235) binding
- D314 (= D488) binding
- A322 (≠ V496) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
36% identity, 68% coverage: 187:626/647 of query aligns to 3:445/455 of 1ebdA
- active site: P13 (≠ S197), L37 (≠ I222), C41 (= C226), C46 (= C231), S49 (= S234), N74 (= N259), V75 (≠ P260), Y180 (= Y364), E184 (= E368), S320 (≠ A500), H438 (= H619), H440 (≠ Y621), E445 (= E626)
- binding flavin-adenine dinucleotide: G10 (= G194), G12 (= G196), P13 (≠ S197), V32 (= V216), E33 (≠ N217), K34 (≠ A218), G39 (= G224), V40 (≠ T225), C41 (= C226), G45 (= G230), C46 (= C231), K50 (= K235), E112 (≠ W299), A113 (= A300), T141 (= T327), G142 (≠ T328), Y180 (= Y364), I181 (= I365), R268 (≠ T448), D308 (= D488), A314 (= A494), L315 (≠ F495), A316 (≠ V496)
P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see 2 papers)
33% identity, 70% coverage: 187:639/647 of query aligns to 37:499/501 of P31023
- 67:76 (vs. 217:226, 40% identical) binding
- C76 (= C226) modified: Disulfide link with 81, Redox-active
- C81 (= C231) modified: Disulfide link with 76, Redox-active
- G149 (≠ A300) binding
- D348 (= D488) binding
- MLAH 354:357 (≠ AFVY 494:497) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
33% identity, 70% coverage: 187:639/647 of query aligns to 3:465/467 of 1dxlA
- active site: L38 (≠ I222), C42 (= C226), C47 (= C231), S50 (= S234), Y184 (= Y364), E188 (= E368), H444 (= H619), H446 (≠ Y621), E451 (= E626)
- binding flavin-adenine dinucleotide: I9 (= I193), P13 (≠ S197), G14 (≠ A198), E33 (≠ N217), K34 (≠ A218), R35 (≠ G219), G40 (= G224), T41 (= T225), C42 (= C226), G46 (= G230), C47 (= C231), K51 (= K235), Y114 (≠ W299), G115 (≠ A300), T144 (= T324), G145 (= G325), Y184 (= Y364), I185 (= I365), R274 (≠ T448), D314 (= D488), M320 (≠ A494), L321 (≠ F495), A322 (≠ V496), H323 (≠ Y497)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
31% identity, 69% coverage: 187:633/647 of query aligns to 6:460/470 of 6uziC
- active site: C45 (= C226), C50 (= C231), S53 (= S234), V187 (≠ Y364), E191 (= E368), H448 (≠ Y621), E453 (= E626)
- binding flavin-adenine dinucleotide: I12 (= I193), G13 (= G194), G15 (= G196), P16 (≠ S197), G17 (≠ A198), E36 (≠ N217), K37 (≠ A218), G43 (= G224), T44 (= T225), C45 (= C226), G49 (= G230), C50 (= C231), S53 (= S234), K54 (= K235), V117 (≠ W299), G118 (≠ A300), T147 (= T324), G148 (= G325), I188 (= I365), R276 (≠ T448), D316 (= D488), M322 (≠ A494), L323 (≠ F495), A324 (≠ V496)
- binding zinc ion: H448 (≠ Y621), E453 (= E626)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
33% identity, 69% coverage: 188:634/647 of query aligns to 2:447/452 of 2eq7A
- active site: P11 (≠ S197), L36 (≠ I222), C40 (= C226), C45 (= C231), S48 (= S234), G72 (vs. gap), V73 (vs. gap), V177 (≠ Y364), E181 (= E368), S314 (≠ A500), H432 (= H619), H434 (≠ Y621), E439 (= E626)
- binding flavin-adenine dinucleotide: G10 (= G196), P11 (≠ S197), G12 (≠ A198), E31 (≠ N217), K32 (≠ A218), G38 (= G224), T39 (= T225), C40 (= C226), R42 (≠ N228), G44 (= G230), C45 (= C231), K49 (= K235), T110 (≠ W299), A111 (= A300), T137 (= T324), G138 (= G325), S157 (≠ N344), I178 (= I365), R262 (≠ T448), Y265 (≠ N451), D302 (= D488), M308 (≠ A494), L309 (≠ F495), A310 (≠ V496), H311 (≠ Y497), Y341 (≠ F528)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ L333), G174 (= G361), G176 (= G363), V177 (≠ Y364), I178 (= I365), E197 (≠ H384), Y198 (≠ R385), V231 (≠ I418), V260 (≠ T446), G261 (= G447), R262 (≠ T448), M308 (≠ A494), L309 (≠ F495), V339 (= V526)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 69% coverage: 188:634/647 of query aligns to 2:447/455 of 2yquB
- active site: P11 (≠ S197), L36 (≠ I222), C40 (= C226), C45 (= C231), S48 (= S234), G72 (vs. gap), V73 (vs. gap), V177 (≠ Y364), E181 (= E368), S314 (≠ A500), H432 (= H619), H434 (≠ Y621), E439 (= E626)
- binding carbonate ion: A310 (≠ V496), S314 (≠ A500), S423 (≠ T610), D426 (≠ E613)
- binding flavin-adenine dinucleotide: G8 (= G194), G10 (= G196), P11 (≠ S197), G12 (≠ A198), E31 (≠ N217), K32 (≠ A218), G38 (= G224), T39 (= T225), C40 (= C226), R42 (≠ N228), G44 (= G230), C45 (= C231), K49 (= K235), T110 (≠ W299), A111 (= A300), T137 (= T324), G138 (= G325), I178 (= I365), Y265 (≠ N451), G301 (= G487), D302 (= D488), M308 (≠ A494), L309 (≠ F495), A310 (≠ V496), H311 (≠ Y497)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 69% coverage: 188:634/647 of query aligns to 2:447/455 of 2yquA
- active site: P11 (≠ S197), L36 (≠ I222), C40 (= C226), C45 (= C231), S48 (= S234), G72 (vs. gap), V73 (vs. gap), V177 (≠ Y364), E181 (= E368), S314 (≠ A500), H432 (= H619), H434 (≠ Y621), E439 (= E626)
- binding flavin-adenine dinucleotide: G8 (= G194), G10 (= G196), P11 (≠ S197), G12 (≠ A198), E31 (≠ N217), K32 (≠ A218), G38 (= G224), T39 (= T225), C40 (= C226), R42 (≠ N228), G44 (= G230), C45 (= C231), K49 (= K235), T110 (≠ W299), A111 (= A300), T137 (= T324), G138 (= G325), S157 (≠ N344), I178 (= I365), Y265 (≠ N451), G301 (= G487), D302 (= D488), M308 (≠ A494), L309 (≠ F495), A310 (≠ V496)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
31% identity, 70% coverage: 188:639/647 of query aligns to 1:464/465 of 3urhB
- active site: Y35 (≠ I222), C39 (= C226), C44 (= C231), S47 (= S234), V183 (≠ Y364), E187 (= E368), H443 (= H619), H445 (≠ Y621), E450 (= E626)
- binding flavin-adenine dinucleotide: I6 (= I193), G7 (= G194), G9 (= G196), P10 (≠ S197), G11 (≠ A198), E30 (≠ N217), K31 (≠ A218), G37 (= G224), T38 (= T225), C39 (= C226), G43 (= G230), C44 (= C231), K48 (= K235), T111 (≠ W299), G112 (≠ A300), A140 (= A323), T141 (= T324), G142 (= G325), I184 (= I365), R273 (≠ T448), G312 (= G487), D313 (= D488), M319 (≠ A494), L320 (≠ F495), A321 (≠ V496), H322 (≠ Y497)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
31% identity, 68% coverage: 188:626/647 of query aligns to 2:430/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G196), E31 (≠ N217), Q32 (≠ A218), M36 (≠ I222), G39 (= G224), T40 (= T225), C41 (= C226), C46 (= C231), K50 (= K235), A97 (= A300), N126 (≠ A323), T127 (= T324), G128 (= G325), I169 (= I365), N255 (= N451), G290 (= G487), D291 (= D488), Q297 (≠ A494), F298 (= F495), T299 (≠ V496), Y300 (= Y497), S302 (≠ A499)
- binding histidine: D353 (≠ P549), Y354 (= Y550)
Sites not aligning to the query:
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
31% identity, 68% coverage: 188:626/647 of query aligns to 5:433/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G194), G13 (= G196), E34 (≠ N217), Q35 (≠ A218), M39 (≠ I222), G42 (= G224), T43 (= T225), G48 (= G230), C49 (= C231), K53 (= K235), K99 (≠ W299), A100 (= A300), N129 (≠ A323), T130 (= T324), G131 (= G325), G293 (= G487), D294 (= D488), Q300 (≠ A494), F301 (= F495), T302 (≠ V496), Y303 (= Y497), S305 (≠ A499)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
30% identity, 70% coverage: 190:642/647 of query aligns to 8:465/471 of 4jdrA
- active site: P15 (≠ S197), L40 (≠ I222), C44 (= C226), C49 (= C231), S52 (= S234), E77 (≠ N259), P78 (= P260), I184 (≠ Y364), E188 (= E368), V324 (≠ A500), H442 (= H619), H444 (≠ Y621), E449 (= E626)
- binding flavin-adenine dinucleotide: G12 (= G194), G14 (= G196), P15 (≠ S197), A16 (= A198), E35 (≠ N217), R36 (≠ A218), Y37 (≠ G219), V43 (≠ T225), C44 (= C226), G48 (= G230), C49 (= C231), K53 (= K235), L115 (≠ W299), G116 (≠ A300), A144 (≠ T324), G145 (= G325), I185 (= I365), G311 (= G487), D312 (= D488), M318 (≠ A494), L319 (≠ F495), A320 (≠ V496), H321 (≠ Y497)
Sites not aligning to the query:
Query Sequence
>Echvi_4481 Echvi_4481 mercuric reductase
MVKIRNMFTPKSNKIGEGQKSLSEVVLEIEGMTCDHCATGIEKKVGHLVGTASQKVNYPE
GKGIFSYDPEKVSKKEIIDTINGMGNYSVKKELPASSNGQGTEEEVTFSISGMTCDHCAT
SIEKRFEGHEGLISKSVSYADEKGTFIFNPDKISRQEIIETINKEGNYKVQKEIGGNGNL
ERADPGQHDLIIIGGGSAAFSAATTANELGLTVLMVNAGLDIGGTCVNVGCVPSKHLIRA
AEQVHRAQHSPFNGVSGANPTFDFKATIQQKKELVAALQKKKYLGVVGDLDNITILEGWA
RFVDAHTIEVDGKPYKGMKYLLATGATTNVPDLPGLEDVGYLTNETLFDLEEQPEHLIVL
GAGYIALEIAQAYHRFGTKVTMLHRSERILRTQAADITDDLTSHFTEEGIEVHTNVSIQK
FEKNGDAIVAHTNEGTFEASHVLVATGTRPNTSGLAIENAGVNLNKTGHILVNTKQETNV
GHIYAAGDCTDTPAFVYTAAKEGKVAVLNAFQSTGDMVDYTGLPWVVFTDPQIAGAGLDE
KEAEEAGIPYETSVMPLTEVPRAQAALDTRGVIKLIRNSETDKLIGGRIIAPEGGELAMQ
VSLAIKAGMTIQELADAFHPYLTLSEGVKLAAITFNKDVSELSCCAS
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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