SitesBLAST
Comparing Synpcc7942_1118 FitnessBrowser__SynE:Synpcc7942_1118 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)
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
38% identity, 89% coverage: 36:492/516 of query aligns to 2:450/454 of 5x1yB
- active site: A13 (≠ T47), V37 (≠ M73), C41 (= C77), C46 (= C82), S49 (= S85), A74 (= A112), G75 (≠ I113), Y178 (≠ P216), E182 (= E220), A318 (≠ D356), A437 (≠ H479), Y439 (= Y481), E444 (= E486)
- binding flavin-adenine dinucleotide: I9 (= I43), G12 (= G46), I32 (= I68), E33 (= E69), R34 (≠ K70), G39 (= G75), T40 (≠ D76), C41 (= C77), G45 (= G81), C46 (= C82), K50 (= K86), A114 (= A152), T138 (= T176), G139 (= G177), Y178 (≠ P216), R266 (= R304), G305 (= G343), D306 (= D344), F313 (= F351), V314 (≠ T352), A317 (= A355)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
37% identity, 90% coverage: 36:499/516 of query aligns to 83:538/546 of D9J041
- C122 (= C77) modified: Disulfide link with 127, Redox-active
- C127 (= C82) modified: Disulfide link with 122, Redox-active
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
35% identity, 90% coverage: 30:491/516 of query aligns to 162:615/631 of P16171
- Y264 (≠ S136) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y481) 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.
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
34% identity, 89% coverage: 40:497/516 of query aligns to 6:456/466 of 4k8dA
- active site: G13 (= G49), I37 (≠ M73), C41 (= C77), C46 (= C82), S49 (= S85), V75 (≠ A112), P76 (≠ I113), V185 (≠ P216), E189 (= E220), A320 (≠ D356), F438 (≠ H479), Y440 (= Y481), E445 (= E486)
- binding flavin-adenine dinucleotide: I9 (= I43), G10 (= G44), G12 (= G46), A14 (≠ L50), E33 (= E69), R34 (≠ K70), G39 (= G75), T40 (≠ D76), C41 (= C77), G45 (= G81), C46 (= C82), K50 (= K86), E115 (≠ Q151), A116 (= A152), T145 (= T176), G146 (= G177), R268 (= R304), G307 (= G343), D308 (= D344), F315 (= F351), V316 (≠ T352), Y317 (≠ H353)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ G214), S184 (≠ G215), V185 (≠ P216), V186 (≠ I217), E189 (= E220), R206 (= R237), N207 (≠ R238), R212 (≠ K244), T266 (= T302), G267 (= G303), Q314 (≠ K350), F315 (= F351), V345 (= V386)
Sites not aligning to the query:
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
34% identity, 89% coverage: 40:497/516 of query aligns to 101:551/561 of P00392
- A110 (≠ V51) binding
- G130 (≠ Q71) binding
- T135 (≠ D76) binding
- C136 (= C77) modified: Disulfide link with 141, Redox-active
- C141 (= C82) modified: Disulfide link with 136, Redox-active
- K145 (= K86) binding
- A211 (= A152) binding
- D403 (= D344) binding
- V411 (≠ T352) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 558 binding
- 559 binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
32% identity, 88% coverage: 39:493/516 of query aligns to 5:452/455 of 1ebdA
- active site: P13 (≠ T47), L37 (≠ M73), C41 (= C77), C46 (= C82), S49 (= S85), N74 (≠ A112), V75 (≠ I113), Y180 (≠ P216), E184 (= E220), S320 (≠ D356), H438 (= H479), H440 (≠ Y481), E445 (= E486)
- binding flavin-adenine dinucleotide: G10 (= G44), G12 (= G46), P13 (≠ T47), V32 (≠ I68), E33 (= E69), K34 (= K70), G39 (= G75), V40 (≠ D76), C41 (= C77), G45 (= G81), C46 (= C82), K50 (= K86), E112 (≠ Q151), A113 (= A152), T141 (= T176), G142 (= G177), Y180 (≠ P216), I181 (= I217), R268 (= R304), D308 (= D344), A314 (≠ K350), L315 (≠ F351), A316 (≠ T352)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
31% identity, 91% coverage: 39:505/516 of query aligns to 11:470/470 of P11959
- 39:47 (vs. 69:77, 56% identical) binding
- K56 (= K86) binding
- D314 (= D344) binding
- A322 (≠ T352) binding
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
34% identity, 89% coverage: 40:497/516 of query aligns to 7:457/467 of 4k7zA
- active site: G14 (= G49), I38 (≠ M73), A42 (≠ C77), A47 (≠ C82), S50 (= S85), V76 (≠ A112), P77 (≠ I113), V186 (≠ P216), E190 (= E220), A321 (≠ D356), F439 (≠ H479), Y441 (= Y481), E446 (= E486)
- binding flavin-adenine dinucleotide: I10 (= I43), G11 (= G44), G13 (= G46), A15 (≠ L50), E34 (= E69), R35 (≠ K70), G40 (= G75), T41 (≠ D76), A42 (≠ C77), G46 (= G81), A47 (≠ C82), K51 (= K86), E116 (≠ Q151), A117 (= A152), T146 (= T176), G147 (= G177), R269 (= R304), G308 (= G343), D309 (= D344), Q315 (≠ K350), F316 (= F351), V317 (≠ T352), Y318 (≠ H353)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ G214), S185 (≠ G215), V186 (≠ P216), V187 (≠ I217), E190 (= E220), R207 (= R237), N208 (≠ R238), R213 (≠ K244), T267 (= T302), G268 (= G303), R269 (= R304), Q315 (≠ K350), F316 (= F351), V346 (= V386)
Sites not aligning to the query:
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
31% identity, 89% coverage: 37:497/516 of query aligns to 3:453/460 of 2eq6A
- active site: V37 (≠ M73), C41 (= C77), C46 (= C82), T49 (≠ S85), A176 (≠ P216), E180 (= E220), H435 (= H479), H437 (≠ Y481), E442 (= E486)
- binding flavin-adenine dinucleotide: I9 (= I43), G10 (= G44), G12 (= G46), P13 (≠ T47), G14 (≠ T48), E33 (= E69), A34 (≠ K70), G39 (= G75), V40 (≠ D76), C41 (= C77), G45 (= G81), C46 (= C82), K50 (= K86), F111 (≠ Q151), A112 (= A152), A135 (= A175), T136 (= T176), G137 (= G177), S155 (≠ L202), R269 (≠ N307), D306 (= D344), L312 (≠ K350), L313 (≠ F351), A314 (≠ T352), H315 (= H353), Y344 (≠ F388)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
32% identity, 88% coverage: 38:492/516 of query aligns to 7:459/470 of 6uziC
- active site: C45 (= C77), C50 (= C82), S53 (= S85), V187 (≠ P216), E191 (= E220), H448 (≠ Y481), E453 (= E486)
- binding flavin-adenine dinucleotide: I12 (= I43), G13 (= G44), G15 (= G46), P16 (≠ T47), G17 (≠ T48), E36 (= E69), K37 (= K70), G43 (= G75), T44 (≠ D76), C45 (= C77), G49 (= G81), C50 (= C82), S53 (= S85), K54 (= K86), V117 (≠ Q151), G118 (≠ A152), T147 (= T176), G148 (= G177), I188 (= I217), R276 (= R304), D316 (= D344), M322 (≠ K350), L323 (≠ F351), A324 (≠ T352)
- binding zinc ion: H448 (≠ Y481), E453 (= E486)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
32% identity, 88% coverage: 37:492/516 of query aligns to 1:445/452 of 2eq7A
- active site: P11 (≠ T47), L36 (≠ M73), C40 (= C77), C45 (= C82), S48 (= S85), G72 (≠ A112), V73 (≠ I113), V177 (≠ P216), E181 (= E220), S314 (≠ D356), H432 (= H479), H434 (≠ Y481), E439 (= E486)
- binding flavin-adenine dinucleotide: G10 (= G46), P11 (≠ T47), G12 (≠ T48), E31 (= E69), K32 (= K70), G38 (= G75), T39 (≠ D76), C40 (= C77), R42 (≠ N79), G44 (= G81), C45 (= C82), K49 (= K86), T110 (≠ Q151), A111 (= A152), T137 (= T176), G138 (= G177), S157 (≠ N196), I178 (= I217), R262 (= R304), Y265 (≠ N307), D302 (= D344), M308 (≠ K350), L309 (≠ F351), A310 (≠ T352), H311 (= H353), Y341 (≠ F388)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I185), G174 (= G213), G176 (= G215), V177 (≠ P216), I178 (= I217), E197 (≠ Q236), Y198 (≠ R237), V231 (≠ I270), V260 (≠ T302), G261 (= G303), R262 (= R304), M308 (≠ K350), L309 (≠ F351), V339 (= V386)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 88% coverage: 37:492/516 of query aligns to 1:445/455 of 2yquB
- active site: P11 (≠ T47), L36 (≠ M73), C40 (= C77), C45 (= C82), S48 (= S85), G72 (≠ A112), V73 (≠ I113), V177 (≠ P216), E181 (= E220), S314 (≠ D356), H432 (= H479), H434 (≠ Y481), E439 (= E486)
- binding carbonate ion: A310 (≠ T352), S314 (≠ D356), S423 (≠ G470), D426 (≠ A473)
- binding flavin-adenine dinucleotide: G8 (= G44), G10 (= G46), P11 (≠ T47), G12 (≠ T48), E31 (= E69), K32 (= K70), G38 (= G75), T39 (≠ D76), C40 (= C77), R42 (≠ N79), G44 (= G81), C45 (= C82), K49 (= K86), T110 (≠ Q151), A111 (= A152), T137 (= T176), G138 (= G177), I178 (= I217), Y265 (≠ N307), G301 (= G343), D302 (= D344), M308 (≠ K350), L309 (≠ F351), A310 (≠ T352), H311 (= H353)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 88% coverage: 37:492/516 of query aligns to 1:445/455 of 2yquA
- active site: P11 (≠ T47), L36 (≠ M73), C40 (= C77), C45 (= C82), S48 (= S85), G72 (≠ A112), V73 (≠ I113), V177 (≠ P216), E181 (= E220), S314 (≠ D356), H432 (= H479), H434 (≠ Y481), E439 (= E486)
- binding flavin-adenine dinucleotide: G8 (= G44), G10 (= G46), P11 (≠ T47), G12 (≠ T48), E31 (= E69), K32 (= K70), G38 (= G75), T39 (≠ D76), C40 (= C77), R42 (≠ N79), G44 (= G81), C45 (= C82), K49 (= K86), T110 (≠ Q151), A111 (= A152), T137 (= T176), G138 (= G177), S157 (≠ N196), I178 (= I217), Y265 (≠ N307), G301 (= G343), D302 (= D344), M308 (≠ K350), L309 (≠ F351), A310 (≠ T352)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
32% identity, 88% coverage: 38:492/516 of query aligns to 1:456/465 of 3urhB
- active site: Y35 (≠ M73), C39 (= C77), C44 (= C82), S47 (= S85), V183 (≠ P216), E187 (= E220), H443 (= H479), H445 (≠ Y481), E450 (= E486)
- binding flavin-adenine dinucleotide: I6 (= I43), G7 (= G44), G9 (= G46), P10 (≠ T47), G11 (≠ T48), E30 (= E69), K31 (= K70), G37 (= G75), T38 (≠ D76), C39 (= C77), G43 (= G81), C44 (= C82), K48 (= K86), T111 (≠ Q151), G112 (≠ A152), A140 (= A175), T141 (= T176), G142 (= G177), I184 (= I217), R273 (= R304), G312 (= G343), D313 (= D344), M319 (≠ K350), L320 (≠ F351), A321 (≠ T352), H322 (= H353)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
32% identity, 89% coverage: 37:496/516 of query aligns to 5:442/444 of 4ywoA
- active site: A15 (≠ T47), I39 (≠ M73), C43 (= C77), C48 (= C82), S51 (= S85), A174 (≠ P216), E178 (= E220), G308 (≠ D356), H425 (= H479), F427 (≠ Y481), E432 (= E486)
- binding flavin-adenine dinucleotide: G12 (= G44), G14 (= G46), K36 (= K70), G41 (= G75), T42 (≠ D76), C43 (= C77), G47 (= G81), C48 (= C82), K52 (= K86), A110 (= A152), A133 (= A175), T134 (= T176), G135 (= G177), N154 (= N196), L175 (≠ I217), L263 (= L311), G295 (= G343), D296 (= D344), M302 (≠ K350), L303 (≠ F351), E304 (≠ T352), A307 (= A355)
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)
31% identity, 89% coverage: 35:492/516 of query aligns to 35:491/501 of P31023
- 67:76 (vs. 69:77, 50% identical) binding
- C76 (= C77) modified: Disulfide link with 81, Redox-active
- C81 (= C82) modified: Disulfide link with 76, Redox-active
- G149 (≠ A152) binding
- D348 (= D344) binding
- MLAH 354:357 (≠ KFTH 350:353) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
31% identity, 89% coverage: 35:492/516 of query aligns to 1:457/467 of 1dxlA
- active site: L38 (≠ M73), C42 (= C77), C47 (= C82), S50 (= S85), Y184 (≠ P216), E188 (= E220), H444 (= H479), H446 (≠ Y481), E451 (= E486)
- binding flavin-adenine dinucleotide: I9 (= I43), P13 (≠ T47), G14 (≠ T48), E33 (= E69), K34 (= K70), R35 (≠ Q71), G40 (= G75), T41 (≠ D76), C42 (= C77), G46 (= G81), C47 (= C82), K51 (= K86), Y114 (≠ Q151), G115 (≠ A152), T144 (= T176), G145 (= G177), Y184 (≠ P216), I185 (= I217), R274 (= R304), D314 (= D344), M320 (≠ K350), L321 (≠ F351), A322 (≠ T352), H323 (= H353)
3ladA Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 angstroms resolution. A comparison with the structure of glutathione reductase (see paper)
30% identity, 88% coverage: 38:492/516 of query aligns to 4:461/472 of 3ladA
- active site: L44 (≠ M73), C48 (= C77), C53 (= C82), S56 (= S85), V190 (≠ P216), E194 (= E220), F448 (≠ H479), H450 (≠ Y481), E455 (= E486)
- binding flavin-adenine dinucleotide: I9 (= I43), G10 (= G44), G12 (= G46), P13 (≠ T47), E33 (= E69), K34 (= K70), G46 (= G75), T47 (≠ D76), C48 (= C77), G52 (= G81), C53 (= C82), H120 (≠ Q151), G121 (≠ A152), A149 (= A175), S150 (≠ T176), G151 (= G177), I191 (= I217), R278 (= R304), D318 (= D344), L325 (≠ F351), A326 (≠ T352)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
30% identity, 88% coverage: 38:492/516 of query aligns to 5:462/477 of P18925
- 34:49 (vs. 69:77, 31% identical) binding
- C49 (= C77) modified: Disulfide link with 54, Redox-active
- C54 (= C82) modified: Disulfide link with 49, Redox-active
- K58 (= K86) binding
- D319 (= D344) binding
- A327 (≠ T352) binding
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
29% identity, 88% coverage: 38:492/516 of query aligns to 5:462/475 of 6awaA
- active site: L45 (≠ M73), C49 (= C77), C54 (= C82), S57 (= S85), V191 (≠ P216), E195 (= E220), F449 (≠ H479), H451 (≠ Y481), E456 (= E486)
- binding adenosine monophosphate: I187 (= I212), E211 (≠ Q236), A212 (≠ R237), L213 (≠ R238), V245 (≠ I270), V277 (≠ T302)
- binding flavin-adenine dinucleotide: I10 (= I43), G13 (= G46), P14 (≠ T47), G15 (≠ T48), E34 (= E69), K35 (= K70), T48 (≠ D76), C49 (= C77), G53 (= G81), C54 (= C82), K58 (= K86), H121 (≠ Q151), G122 (≠ A152), S151 (≠ T176), G152 (= G177), I192 (= I217), R279 (= R304), G318 (= G343), D319 (= D344), M325 (≠ K350), L326 (≠ F351), A327 (≠ T352), Y358 (≠ F388)
Sites not aligning to the query:
Query Sequence
>Synpcc7942_1118 FitnessBrowser__SynE:Synpcc7942_1118
LSSQSFIAFVSPADSHNQLLIDRVHPQDWINPEPADCYDLVVIGAGTTGLVVAAGATGLG
LGLKVALIEKQLMGGDCLNFGCVPSKALIRSSRVIGELQRANTLGIQVAPEAIAVDFAAV
MERLRKVRAGMSVHDSAQRFQALGVDVFLGQACFCDRNTIQVGEATLKFRKAVIATGARA
TYPNIEGLEASGFLTNETVFSLSNCPRRLAVIGGGPIGCELAQAFQRLGSQVTLFQRRSQ
LLPKEDFEAAEVIQNQLRADGVQVCLSAEITRIERTASGKLITFRQEGRESVLEVDEILV
GTGRSPNVQDLNLEAVGVDYDSVHGVKVNDYLQTTNPKIYAAGDVCSPWKFTHAADAAAR
IVIKNALFSPFGLGKSKVSDLIIPRVTFTDPEVAHVGLSETAARHQGIAIATITIPLDQV
DRTVLDGETAGFIRIHHQPNSDKILGATIVAPHAGEMISEVTTAIANQLGMSALSSVIHP
YPTQAEGIKKAADNYRRTLLTPMTKQLLKLLMIFSK
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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