SitesBLAST
Comparing Dsui_2497 FitnessBrowser__PS:Dsui_2497 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)
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
85% identity, 100% coverage: 1:548/548 of query aligns to 1:561/561 of P00392
- M1 (= M1) modified: Initiator methionine, Removed
- A110 (= A97) binding
- G130 (= G117) binding
- T135 (= T122) binding
- C136 (= C123) modified: Disulfide link with 141, Redox-active
- C141 (= C128) modified: Disulfide link with 136, Redox-active
- K145 (= K132) binding
- A211 (= A198) binding
- D403 (= D390) binding
- V411 (= V398) binding
- C558 (= C545) binding
- C559 (= C546) binding
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
94% identity, 84% coverage: 86:548/548 of query aligns to 4:466/466 of 4k8dA
- active site: G13 (= G95), I37 (= I119), C41 (= C123), C46 (= C128), S49 (= S131), V75 (= V157), P76 (= P158), V185 (= V267), E189 (= E271), A320 (= A402), F438 (= F520), Y440 (= Y522), E445 (= E527), A463 (≠ C545), A464 (≠ C546)
- binding flavin-adenine dinucleotide: I9 (= I91), G10 (= G92), G12 (= G94), A14 (= A96), E33 (= E115), R34 (= R116), G39 (= G121), T40 (= T122), C41 (= C123), G45 (= G127), C46 (= C128), K50 (= K132), E115 (= E197), A116 (= A198), T145 (= T227), G146 (= G228), R268 (= R350), G307 (= G389), D308 (= D390), F315 (= F397), V316 (= V398), Y317 (= Y399)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (= S265), S184 (= S266), V185 (= V267), V186 (= V268), E189 (= E271), R206 (= R288), N207 (≠ S289), R212 (= R294), T266 (= T348), G267 (= G349), Q314 (= Q396), F315 (= F397), V345 (= V427)
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
94% identity, 84% coverage: 86:548/548 of query aligns to 5:467/467 of 4k7zA
- active site: G14 (= G95), I38 (= I119), A42 (≠ C123), A47 (≠ C128), S50 (= S131), V76 (= V157), P77 (= P158), V186 (= V267), E190 (= E271), A321 (= A402), F439 (= F520), Y441 (= Y522), E446 (= E527), C464 (= C545), C465 (= C546)
- binding flavin-adenine dinucleotide: I10 (= I91), G11 (= G92), G13 (= G94), A15 (= A96), E34 (= E115), R35 (= R116), G40 (= G121), T41 (= T122), A42 (≠ C123), G46 (= G127), A47 (≠ C128), K51 (= K132), E116 (= E197), A117 (= A198), T146 (= T227), G147 (= G228), R269 (= R350), G308 (= G389), D309 (= D390), Q315 (= Q396), F316 (= F397), V317 (= V398), Y318 (= Y399)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (= S265), S185 (= S266), V186 (= V267), V187 (= V268), E190 (= E271), R207 (= R288), N208 (≠ S289), R213 (= R294), T267 (= T348), G268 (= G349), R269 (= R350), Q315 (= Q396), F316 (= F397), V346 (= V427)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
42% identity, 100% coverage: 3:548/548 of query aligns to 5:546/546 of D9J041
- C122 (= C123) modified: Disulfide link with 127, Redox-active
- C127 (= C128) modified: Disulfide link with 122, Redox-active
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
42% identity, 99% coverage: 4:548/548 of query aligns to 85:631/631 of P16171
- Y264 (= Y181) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y522) 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)
44% identity, 82% coverage: 88:537/548 of query aligns to 6:454/454 of 5x1yB
- active site: A13 (≠ G95), V37 (≠ I119), C41 (= C123), C46 (= C128), S49 (= S131), A74 (≠ V157), G75 (≠ P158), Y178 (≠ V267), E182 (= E271), A318 (= A402), A437 (≠ F520), Y439 (= Y522), E444 (= E527)
- binding flavin-adenine dinucleotide: I9 (= I91), G12 (= G94), I32 (= I114), E33 (= E115), R34 (= R116), G39 (= G121), T40 (= T122), C41 (= C123), G45 (= G127), C46 (= C128), K50 (= K132), A114 (= A198), T138 (= T227), G139 (= G228), Y178 (≠ V267), R266 (= R350), G305 (= G389), D306 (= D390), F313 (= F397), V314 (= V398), A317 (= A401)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
37% identity, 82% coverage: 88:539/548 of query aligns to 8:444/444 of 4ywoA
- active site: A15 (≠ G95), I39 (= I119), C43 (= C123), C48 (= C128), S51 (= S131), A174 (≠ V267), E178 (= E271), G308 (≠ A402), H425 (≠ F520), F427 (≠ Y522), E432 (= E527)
- binding flavin-adenine dinucleotide: G12 (= G92), G14 (= G94), K36 (≠ R116), G41 (= G121), T42 (= T122), C43 (= C123), G47 (= G127), C48 (= C128), K52 (= K132), A110 (= A198), A133 (= A226), T134 (= T227), G135 (= G228), N154 (≠ S247), L175 (≠ V268), L263 (= L357), G295 (= G389), D296 (= D390), M302 (≠ Q396), L303 (≠ F397), E304 (≠ V398), A307 (= A401)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
35% identity, 80% coverage: 90:527/548 of query aligns to 8:445/455 of 1ebdA
- active site: P13 (≠ G95), L37 (≠ I119), C41 (= C123), C46 (= C128), S49 (= S131), N74 (≠ V157), V75 (≠ P158), Y180 (≠ V267), E184 (= E271), S320 (≠ A402), H438 (≠ F520), H440 (≠ Y522), E445 (= E527)
- binding flavin-adenine dinucleotide: G10 (= G92), G12 (= G94), P13 (≠ G95), V32 (≠ I114), E33 (= E115), K34 (≠ R116), G39 (= G121), V40 (≠ T122), C41 (= C123), G45 (= G127), C46 (= C128), K50 (= K132), E112 (= E197), A113 (= A198), T141 (= T227), G142 (= G228), Y180 (≠ V267), I181 (≠ V268), R268 (= R350), D308 (= D390), A314 (≠ Q396), L315 (≠ F397), A316 (≠ V398)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
35% identity, 80% coverage: 90:527/548 of query aligns to 14:451/470 of P11959
- 39:47 (vs. 115:123, 56% identical) binding
- K56 (= K132) binding
- D314 (= D390) binding
- A322 (≠ V398) binding
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
31% identity, 80% coverage: 90:530/548 of query aligns to 8:434/441 of 6kgyB
- active site: C43 (= C123), C48 (= C128), T51 (≠ S131), Y168 (≠ V267), E172 (= E271), H426 (≠ Y522), E431 (= E527)
- binding flavin-adenine dinucleotide: I9 (= I91), G12 (= G94), E33 (= E115), Q34 (≠ R116), M38 (vs. gap), G41 (= G121), T42 (= T122), G47 (= G127), C48 (= C128), A99 (= A198), N126 (≠ A226), T127 (= T227), G128 (= G228), G291 (= G389), D292 (= D390), F299 (= F397), T300 (≠ V398), Y301 (= Y399), S303 (≠ A401), F333 (= F429)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
31% identity, 80% coverage: 90:530/548 of query aligns to 4:425/432 of 6kyyA
- active site: C39 (= C123), C44 (= C128), T47 (≠ S131), Y159 (≠ V267), E163 (= E271), H417 (≠ Y522), E422 (= E527)
- binding copper (ii) ion: C39 (= C123), C44 (= C128), H226 (≠ T333), H229 (= H336), T291 (≠ V398)
- binding flavin-adenine dinucleotide: F7 (≠ S93), G8 (= G94), E29 (= E115), Q30 (≠ R116), M34 (vs. gap), T38 (= T122), C39 (= C123), C44 (= C128), K48 (= K132), A95 (= A198), N117 (≠ A226), T118 (= T227), G119 (= G228), I160 (≠ V268), R243 (= R350), D283 (= D390), F290 (= F397), T291 (≠ V398), S294 (≠ A401)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
35% identity, 82% coverage: 88:538/548 of query aligns to 6:453/460 of 2eq6A
- active site: V37 (≠ I119), C41 (= C123), C46 (= C128), T49 (≠ S131), A176 (≠ V267), E180 (= E271), H435 (≠ F520), H437 (≠ Y522), E442 (= E527)
- binding flavin-adenine dinucleotide: I9 (= I91), G10 (= G92), G12 (= G94), P13 (≠ G95), G14 (≠ A96), E33 (= E115), A34 (≠ R116), G39 (= G121), V40 (≠ T122), C41 (= C123), G45 (= G127), C46 (= C128), K50 (= K132), F111 (≠ E197), A112 (= A198), A135 (= A226), T136 (= T227), G137 (= G228), S155 (= S247), R269 (≠ N353), D306 (= D390), L312 (≠ Q396), L313 (≠ F397), A314 (≠ V398), H315 (≠ Y399), Y344 (≠ F429)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
30% identity, 81% coverage: 88:533/548 of query aligns to 9:459/470 of 6uziC
- active site: C45 (= C123), C50 (= C128), S53 (= S131), V187 (= V267), E191 (= E271), H448 (≠ Y522), E453 (= E527)
- binding flavin-adenine dinucleotide: I12 (= I91), G13 (= G92), G15 (= G94), P16 (≠ G95), G17 (≠ A96), E36 (= E115), K37 (≠ R116), G43 (= G121), T44 (= T122), C45 (= C123), G49 (= G127), C50 (= C128), S53 (= S131), K54 (= K132), V117 (≠ E197), G118 (≠ A198), T147 (= T227), G148 (= G228), I188 (≠ V268), R276 (= R350), D316 (= D390), M322 (≠ Q396), L323 (≠ F397), A324 (≠ V398)
- binding zinc ion: H448 (≠ Y522), E453 (= E527)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
29% identity, 82% coverage: 86:537/548 of query aligns to 5:466/475 of 6awaA
- active site: L45 (≠ I119), C49 (= C123), C54 (= C128), S57 (= S131), V191 (= V267), E195 (= E271), F449 (= F520), H451 (≠ Y522), E456 (= E527)
- binding adenosine monophosphate: I187 (= I263), E211 (vs. gap), A212 (= A287), L213 (≠ R288), V245 (≠ A320), V277 (≠ T348)
- binding flavin-adenine dinucleotide: I10 (= I91), G13 (= G94), P14 (≠ G95), G15 (≠ A96), E34 (= E115), K35 (≠ R116), T48 (= T122), C49 (= C123), G53 (= G127), C54 (= C128), K58 (= K132), H121 (≠ E197), G122 (≠ A198), S151 (≠ T227), G152 (= G228), I192 (≠ V268), R279 (= R350), G318 (= G389), D319 (= D390), M325 (≠ Q396), L326 (≠ F397), A327 (≠ V398), Y358 (≠ F429)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
31% identity, 81% coverage: 88:533/548 of query aligns to 4:445/455 of 2yquB
- active site: P11 (≠ G95), L36 (≠ I119), C40 (= C123), C45 (= C128), S48 (= S131), G72 (≠ A159), V73 (≠ I160), V177 (= V267), E181 (= E271), S314 (≠ A402), H432 (≠ F520), H434 (≠ Y522), E439 (= E527)
- binding carbonate ion: A310 (≠ V398), S314 (≠ A402), S423 (≠ T511), D426 (≠ E514)
- binding flavin-adenine dinucleotide: G8 (= G92), G10 (= G94), P11 (≠ G95), G12 (≠ A96), E31 (= E115), K32 (≠ R116), G38 (= G121), T39 (= T122), C40 (= C123), R42 (≠ N125), G44 (= G127), C45 (= C128), K49 (= K132), T110 (≠ E197), A111 (= A198), T137 (= T227), G138 (= G228), I178 (≠ V268), Y265 (≠ N353), G301 (= G389), D302 (= D390), M308 (≠ Q396), L309 (≠ F397), A310 (≠ V398), H311 (≠ Y399)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
31% identity, 81% coverage: 88:533/548 of query aligns to 4:445/455 of 2yquA
- active site: P11 (≠ G95), L36 (≠ I119), C40 (= C123), C45 (= C128), S48 (= S131), G72 (≠ A159), V73 (≠ I160), V177 (= V267), E181 (= E271), S314 (≠ A402), H432 (≠ F520), H434 (≠ Y522), E439 (= E527)
- binding flavin-adenine dinucleotide: G8 (= G92), G10 (= G94), P11 (≠ G95), G12 (≠ A96), E31 (= E115), K32 (≠ R116), G38 (= G121), T39 (= T122), C40 (= C123), R42 (≠ N125), G44 (= G127), C45 (= C128), K49 (= K132), T110 (≠ E197), A111 (= A198), T137 (= T227), G138 (= G228), S157 (= S247), I178 (≠ V268), Y265 (≠ N353), G301 (= G389), D302 (= D390), M308 (≠ Q396), L309 (≠ F397), A310 (≠ V398)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
31% identity, 81% coverage: 88:533/548 of query aligns to 4:445/452 of 2eq7A
- active site: P11 (≠ G95), L36 (≠ I119), C40 (= C123), C45 (= C128), S48 (= S131), G72 (≠ A159), V73 (≠ I160), V177 (= V267), E181 (= E271), S314 (≠ A402), H432 (≠ F520), H434 (≠ Y522), E439 (= E527)
- binding flavin-adenine dinucleotide: G10 (= G94), P11 (≠ G95), G12 (≠ A96), E31 (= E115), K32 (≠ R116), G38 (= G121), T39 (= T122), C40 (= C123), R42 (≠ N125), G44 (= G127), C45 (= C128), K49 (= K132), T110 (≠ E197), A111 (= A198), T137 (= T227), G138 (= G228), S157 (= S247), I178 (≠ V268), R262 (= R350), Y265 (≠ N353), D302 (= D390), M308 (≠ Q396), L309 (≠ F397), A310 (≠ V398), H311 (≠ Y399), Y341 (≠ F429)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I236), G174 (= G264), G176 (≠ S266), V177 (= V267), I178 (≠ V268), E197 (≠ A287), Y198 (≠ R288), V231 (≠ A320), V260 (≠ T348), G261 (= G349), R262 (= R350), M308 (≠ Q396), L309 (≠ F397), V339 (= V427)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
30% identity, 83% coverage: 87:543/548 of query aligns to 7:465/471 of 4jdrA
- active site: P15 (≠ G95), L40 (≠ I119), C44 (= C123), C49 (= C128), S52 (= S131), E77 (≠ V157), P78 (= P158), I184 (≠ V267), E188 (= E271), V324 (≠ A402), H442 (≠ F520), H444 (≠ Y522), E449 (= E527)
- binding flavin-adenine dinucleotide: G12 (= G92), G14 (= G94), P15 (≠ G95), A16 (= A96), E35 (= E115), R36 (= R116), Y37 (vs. gap), V43 (≠ T122), C44 (= C123), G48 (= G127), C49 (= C128), K53 (= K132), L115 (≠ E197), G116 (≠ A198), A144 (≠ T227), G145 (= G228), I185 (≠ V268), G311 (= G389), D312 (= D390), M318 (≠ Q396), L319 (≠ F397), A320 (≠ V398), H321 (≠ Y399)
Sites not aligning to the query:
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)
30% identity, 83% coverage: 87:543/548 of query aligns to 8:466/474 of P0A9P0
- K220 (≠ A305) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
29% identity, 91% coverage: 43:540/548 of query aligns to 3:499/501 of P31023
- 67:76 (vs. 115:123, 70% identical) binding
- C76 (= C123) modified: Disulfide link with 81, Redox-active
- C81 (= C128) modified: Disulfide link with 76, Redox-active
- G149 (≠ A198) binding
- D348 (= D390) binding
- MLAH 354:357 (≠ QFVY 396:399) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
Query Sequence
>Dsui_2497 FitnessBrowser__PS:Dsui_2497
MTEITVNGMTCTSCATHVKDALEKIPGVNAAVVSYPESRAQVMADTAVSHNQLLAAIAAL
GYQGSIRVGDFKDEPKIRDALEGAGLHIAIIGSGGAAMAAALKAVEQGATVTLIERGTIG
GTCVNIGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPAIDRSKLLAQQQARVDELRHAK
YEGILDGNPAITVLHGEARFKDDQSLVVRLNEGGEREVTFDRCLVATGASPAVPPIPGLK
ESPYWTSTEALVSDTIPARLAVIGSSVVALELAQAFARLGSQVTILARSTLFFREDPAIG
EAVTAAFRAEGIEVLEHTQASQVAHVNGEFVLTTGHGELRADKLLVATGRAPNTRSLALD
AAGVTVNAQGAIVIDQGMRTSNPNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALN
LTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLVIEE
GSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDV
KQLSCCAG
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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