SitesBLAST
Comparing GFF194 FitnessBrowser__Marino:GFF194 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)
67% identity, 100% coverage: 3:468/468 of query aligns to 95:561/561 of P00392
- A110 (= A18) binding
- G130 (= G38) binding
- T135 (= T43) binding
- C136 (= C44) modified: Disulfide link with 141, Redox-active
- C141 (= C49) modified: Disulfide link with 136, Redox-active
- K145 (= K53) binding
- A211 (= A119) binding
- D403 (= D310) binding
- V411 (= V318) binding
- C558 (= C465) binding
- C559 (= C466) 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+
67% identity, 99% coverage: 7:468/468 of query aligns to 5:467/467 of 4k7zA
- active site: G14 (= G16), I38 (≠ V40), A42 (≠ C44), A47 (≠ C49), S50 (= S52), V76 (≠ A78), P77 (= P79), V186 (≠ F188), E190 (= E192), A321 (= A322), F439 (= F440), Y441 (= Y442), E446 (= E447), C464 (= C465), C465 (= C466)
- binding flavin-adenine dinucleotide: I10 (= I12), G11 (= G13), G13 (= G15), A15 (= A17), E34 (= E36), R35 (= R37), G40 (= G42), T41 (= T43), A42 (≠ C44), G46 (= G48), A47 (≠ C49), K51 (= K53), E116 (= E118), A117 (= A119), T146 (= T148), G147 (= G149), R269 (= R271), G308 (= G309), D309 (= D310), Q315 (= Q316), F316 (= F317), V317 (= V318), Y318 (= Y319)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ A186), S185 (≠ G187), V186 (≠ F188), V187 (= V189), E190 (= E192), R207 (= R209), N208 (≠ S210), R213 (≠ S215), T267 (= T269), G268 (= G270), R269 (= R271), Q315 (= Q316), F316 (= F317), V346 (= V347)
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
67% identity, 99% coverage: 7:468/468 of query aligns to 4:466/466 of 4k8dA
- active site: G13 (= G16), I37 (≠ V40), C41 (= C44), C46 (= C49), S49 (= S52), V75 (≠ A78), P76 (= P79), V185 (≠ F188), E189 (= E192), A320 (= A322), F438 (= F440), Y440 (= Y442), E445 (= E447), A463 (≠ C465), A464 (≠ C466)
- binding flavin-adenine dinucleotide: I9 (= I12), G10 (= G13), G12 (= G15), A14 (= A17), E33 (= E36), R34 (= R37), G39 (= G42), T40 (= T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E115 (= E118), A116 (= A119), T145 (= T148), G146 (= G149), R268 (= R271), G307 (= G309), D308 (= D310), F315 (= F317), V316 (= V318), Y317 (= Y319)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ A186), S184 (≠ G187), V185 (≠ F188), V186 (= V189), E189 (= E192), R206 (= R209), N207 (≠ S210), R212 (≠ S215), T266 (= T269), G267 (= G270), Q314 (= Q316), F315 (= F317), V345 (= V347)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
46% identity, 100% coverage: 3:468/468 of query aligns to 81:546/546 of D9J041
- C122 (= C44) modified: Disulfide link with 127, Redox-active
- C127 (= C49) modified: Disulfide link with 122, Redox-active
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
45% identity, 97% coverage: 4:456/468 of query aligns to 1:453/454 of 5x1yB
- active site: A13 (≠ G16), V37 (= V40), C41 (= C44), C46 (= C49), S49 (= S52), A74 (= A78), G75 (≠ P79), Y178 (≠ F188), E182 (= E192), A318 (= A322), A437 (≠ F440), Y439 (= Y442), E444 (= E447)
- binding flavin-adenine dinucleotide: I9 (= I12), G12 (= G15), I32 (= I35), E33 (= E36), R34 (= R37), G39 (= G42), T40 (= T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), A114 (= A119), T138 (= T148), G139 (= G149), Y178 (≠ F188), R266 (= R271), G305 (= G309), D306 (= D310), F313 (= F317), V314 (= V318), A317 (= A321)
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
45% identity, 98% coverage: 11:468/468 of query aligns to 174:631/631 of P16171
- Y264 (= Y102) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y442) 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.
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
34% identity, 93% coverage: 11:447/468 of query aligns to 8:445/455 of 1ebdA
- active site: P13 (≠ G16), L37 (≠ V40), C41 (= C44), C46 (= C49), S49 (= S52), N74 (≠ A78), V75 (≠ P79), Y180 (≠ F188), E184 (= E192), S320 (≠ A322), H438 (≠ F440), H440 (≠ Y442), E445 (= E447)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (≠ G16), V32 (≠ I35), E33 (= E36), K34 (≠ R37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E112 (= E118), A113 (= A119), T141 (= T148), G142 (= G149), Y180 (≠ F188), I181 (≠ V189), R268 (= R271), D308 (= D310), A314 (≠ Q316), L315 (≠ F317), A316 (≠ V318)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
34% identity, 93% coverage: 11:447/468 of query aligns to 14:451/470 of P11959
- 39:47 (vs. 36:44, 56% identical) binding
- K56 (= K53) binding
- D314 (= D310) binding
- A322 (≠ V318) binding
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
35% identity, 98% coverage: 3:459/468 of query aligns to 2:444/444 of 4ywoA
- active site: A15 (≠ G16), I39 (≠ V40), C43 (= C44), C48 (= C49), S51 (= S52), A174 (≠ F188), E178 (= E192), G308 (≠ A322), H425 (≠ F440), F427 (≠ Y442), E432 (= E447)
- binding flavin-adenine dinucleotide: G12 (= G13), G14 (= G15), K36 (≠ R37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), A110 (= A119), A133 (≠ G147), T134 (= T148), G135 (= G149), N154 (≠ S168), L175 (≠ V189), L263 (= L278), G295 (= G309), D296 (= D310), M302 (≠ Q316), L303 (≠ F317), E304 (≠ V318), A307 (= A321)
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
32% identity, 97% coverage: 9:460/468 of query aligns to 6:465/467 of 1dxlA
- active site: L38 (≠ V40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (≠ F188), E188 (= E192), H444 (≠ F440), H446 (≠ Y442), E451 (= E447)
- binding flavin-adenine dinucleotide: I9 (= I12), P13 (≠ G16), G14 (≠ A17), E33 (= E36), K34 (vs. gap), R35 (= R37), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (≠ E118), G115 (≠ A119), T144 (= T148), G145 (= G149), Y184 (≠ F188), I185 (≠ V189), R274 (= R271), D314 (= D310), M320 (≠ Q316), L321 (≠ F317), A322 (≠ V318), H323 (≠ Y319)
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)
32% identity, 97% coverage: 9:460/468 of query aligns to 40:499/501 of P31023
- 67:76 (vs. 36:44, 70% identical) binding
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (≠ A119) binding
- D348 (= D310) binding
- MLAH 354:357 (≠ QFVY 316:319) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
30% identity, 96% coverage: 5:453/468 of query aligns to 5:459/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (≠ F188), E191 (= E192), H448 (≠ Y442), E453 (= E447)
- binding flavin-adenine dinucleotide: I12 (= I12), G13 (= G13), G15 (= G15), P16 (≠ G16), G17 (≠ A17), E36 (= E36), K37 (≠ R37), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ E118), G118 (≠ A119), T147 (= T148), G148 (= G149), I188 (≠ V189), R276 (= R271), D316 (= D310), M322 (≠ Q316), L323 (≠ F317), A324 (≠ V318)
- binding zinc ion: H448 (≠ Y442), E453 (= E447)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
31% identity, 96% coverage: 11:460/468 of query aligns to 5:464/465 of 3urhB
- active site: Y35 (≠ V40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (≠ F188), E187 (= E192), H443 (≠ F440), H445 (≠ Y442), E450 (= E447)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), P10 (≠ G16), G11 (≠ A17), E30 (= E36), K31 (vs. gap), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ E118), G112 (≠ A119), A140 (≠ G147), T141 (= T148), G142 (= G149), I184 (≠ V189), R273 (= R271), G312 (= G309), D313 (= D310), M319 (≠ Q316), L320 (≠ F317), A321 (≠ V318), H322 (≠ Y319)
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, 99% coverage: 1:463/468 of query aligns to 1:466/474 of P0A9P0
- M1 (= M1) modified: Initiator methionine, Removed
- K220 (≠ G226) modified: N6-acetyllysine
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 95% coverage: 11:453/468 of query aligns to 6:445/455 of 2yquB
- active site: P11 (≠ G16), L36 (≠ V40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ A76), V73 (≠ A77), V177 (≠ F188), E181 (= E192), S314 (≠ A322), H432 (≠ F440), H434 (≠ Y442), E439 (= E447)
- binding carbonate ion: A310 (≠ V318), S314 (≠ A322), S423 (≠ T431), D426 (≠ E434)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (≠ G16), G12 (≠ A17), E31 (= E36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E118), A111 (= A119), T137 (= T148), G138 (= G149), I178 (≠ V189), Y265 (≠ N274), G301 (= G309), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ V318), H311 (≠ Y319)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 95% coverage: 11:453/468 of query aligns to 6:445/455 of 2yquA
- active site: P11 (≠ G16), L36 (≠ V40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ A76), V73 (≠ A77), V177 (≠ F188), E181 (= E192), S314 (≠ A322), H432 (≠ F440), H434 (≠ Y442), E439 (= E447)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (≠ G16), G12 (≠ A17), E31 (= E36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E118), A111 (= A119), T137 (= T148), G138 (= G149), S157 (= S168), I178 (≠ V189), Y265 (≠ N274), G301 (= G309), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ V318)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
33% identity, 95% coverage: 11:453/468 of query aligns to 6:445/452 of 2eq7A
- active site: P11 (≠ G16), L36 (≠ V40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ A76), V73 (≠ A77), V177 (≠ F188), E181 (= E192), S314 (≠ A322), H432 (≠ F440), H434 (≠ Y442), E439 (= E447)
- binding flavin-adenine dinucleotide: G10 (= G15), P11 (≠ G16), G12 (≠ A17), E31 (= E36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E118), A111 (= A119), T137 (= T148), G138 (= G149), S157 (= S168), I178 (≠ V189), R262 (= R271), Y265 (≠ N274), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ V318), H311 (≠ Y319), Y341 (≠ F349)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I157), G174 (= G185), G176 (= G187), V177 (≠ F188), I178 (≠ V189), E197 (≠ A208), Y198 (≠ R209), V231 (≠ P241), V260 (≠ T269), G261 (= G270), R262 (= R271), M308 (≠ Q316), L309 (≠ F317), V339 (= V347)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
30% identity, 98% coverage: 6:463/468 of query aligns to 5:465/471 of 4jdrA
- active site: P15 (≠ G16), L40 (≠ V40), C44 (= C44), C49 (= C49), S52 (= S52), E77 (≠ A78), P78 (= P79), I184 (≠ F188), E188 (= E192), V324 (≠ A322), H442 (≠ F440), H444 (≠ Y442), E449 (= E447)
- binding flavin-adenine dinucleotide: G12 (= G13), G14 (= G15), P15 (≠ G16), A16 (= A17), E35 (= E36), R36 (= R37), Y37 (vs. gap), V43 (≠ T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), L115 (≠ E118), G116 (≠ A119), A144 (≠ T148), G145 (= G149), I185 (≠ V189), G311 (= G309), D312 (= D310), M318 (≠ Q316), L319 (≠ F317), A320 (≠ V318), H321 (≠ Y319)
Sites not aligning to the query:
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
30% identity, 96% coverage: 5:453/468 of query aligns to 3:462/475 of 6awaA
- active site: L45 (≠ V40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (≠ F188), E195 (= E192), F449 (= F440), H451 (≠ Y442), E456 (= E447)
- binding adenosine monophosphate: I187 (= I184), E211 (vs. gap), A212 (= A208), L213 (≠ R209), V245 (≠ T239), V277 (≠ T269)
- binding flavin-adenine dinucleotide: I10 (= I12), G13 (= G15), P14 (≠ G16), G15 (≠ A17), E34 (= E36), K35 (≠ R37), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ E118), G122 (≠ A119), S151 (≠ T148), G152 (= G149), I192 (≠ V189), R279 (= R271), G318 (= G309), D319 (= D310), M325 (≠ Q316), L326 (≠ F317), A327 (≠ V318), Y358 (≠ F349)
Sites not aligning to the query:
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
30% identity, 96% coverage: 5:453/468 of query aligns to 3:462/478 of P14218
- 34:49 (vs. 36:44, 44% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (≠ A119) binding
- D319 (= D310) binding
- A327 (≠ V318) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>GFF194 FitnessBrowser__Marino:GFF194
MKNDQKLHIAVIGSGGAAMAAALKATERGARVTLIERGTVGGTCVNVGCVPSKIMIRAAH
IAHLRKESPFDAGISAAAPEVDRAKLLQQQLARVEELRDTKYEKILREHKDITVLNGEAR
FLDTNSLLVTLAEGGEKPVHFDRAFIGTGARPAEPPITGLADTPYLTSTSALTLDTGPKR
LIVIGAGFVALELAQAFARLGSKVTVLARSRVLSSEDPAIGEAIAGAFNREGIEVLSQTL
PSNVDYSDNEFIVETPAGTLRADQLLVATGRTPNTEALNLASIGVETSRDAIQVDEHLQT
TVPGIYAAGDCTNQPQFVYVAAAGGSRAAINMTEGEAKLDFSAMPGVMFTDPQVATVGLS
EAEAVARGYSVDTRLLDLENVPRALVNFDTQGFIKMVAERNSGRLLGVQIVAAEGGEIIQ
TAVMALRAGLTVQEIGDDLFPYLTMVEGFKLCAQTFTKDVKQLSCCAG
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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