SitesBLAST
Comparing 351070 FitnessBrowser__Btheta:351070 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)
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
47% identity, 100% coverage: 1:457/457 of query aligns to 1:439/441 of 6kgyB
- active site: C43 (= C43), C48 (= C48), T51 (= T51), Y168 (= Y180), E172 (= E184), H426 (= H444), E431 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), E33 (= E33), Q34 (= Q34), M38 (= M38), G41 (= G41), T42 (≠ A42), G47 (≠ A47), C48 (= C48), A99 (≠ G111), N126 (= N138), T127 (= T139), G128 (= G140), G291 (= G309), D292 (= D310), F299 (= F317), T300 (= T318), Y301 (= Y319), S303 (= S321), F333 (= F351)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
46% identity, 99% coverage: 6:457/457 of query aligns to 2:430/432 of 6kyyA
- active site: C39 (= C43), C44 (= C48), T47 (= T51), Y159 (= Y180), E163 (= E184), H417 (= H444), E422 (= E449)
- binding copper (ii) ion: C39 (= C43), C44 (= C48), H226 (≠ Y248), H229 (≠ T251), T291 (= T318)
- binding flavin-adenine dinucleotide: F7 (= F11), G8 (= G12), E29 (= E33), Q30 (= Q34), M34 (= M38), T38 (≠ A42), C39 (= C43), C44 (= C48), K48 (= K52), A95 (≠ G111), N117 (= N138), T118 (= T139), G119 (= G140), I160 (= I181), R243 (= R270), D283 (= D310), F290 (= F317), T291 (= T318), S294 (= S321)
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
41% identity, 100% coverage: 1:456/457 of query aligns to 2:440/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), E34 (= E33), Q35 (= Q34), M39 (= M38), G42 (= G41), T43 (≠ A42), G48 (≠ A47), C49 (= C48), K53 (= K52), K99 (= K110), A100 (≠ G111), N129 (= N138), T130 (= T139), G131 (= G140), G293 (= G309), D294 (= D310), Q300 (= Q316), F301 (= F317), T302 (= T318), Y303 (= Y319), S305 (= S321)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
41% identity, 99% coverage: 4:456/457 of query aligns to 2:437/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G12), E31 (= E33), Q32 (= Q34), M36 (= M38), G39 (= G41), T40 (≠ A42), C41 (= C43), C46 (= C48), K50 (= K52), A97 (≠ G111), N126 (= N138), T127 (= T139), G128 (= G140), I169 (= I181), N255 (≠ M273), G290 (= G309), D291 (= D310), Q297 (= Q316), F298 (= F317), T299 (= T318), Y300 (= Y319), S302 (= S321)
- binding histidine: D353 (≠ S372), Y354 (≠ F373)
Sites not aligning to the query:
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
33% identity, 98% coverage: 4:451/457 of query aligns to 4:446/454 of 5x1yB
- active site: A13 (≠ K13), V37 (≠ Y39), C41 (= C43), C46 (= C48), S49 (≠ T51), A74 (≠ Y76), G75 (≠ R77), Y178 (= Y180), E182 (= E184), A318 (≠ L322), A437 (≠ F442), Y439 (≠ H444), E444 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), I32 (≠ V32), E33 (= E33), R34 (≠ Q34), G39 (= G41), T40 (≠ A42), C41 (= C43), G45 (≠ A47), C46 (= C48), K50 (= K52), A114 (≠ G111), T138 (= T139), G139 (= G140), Y178 (= Y180), R266 (= R270), G305 (= G309), D306 (= D310), F313 (= F317), V314 (≠ T318), A317 (≠ S321)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
33% identity, 98% coverage: 4:451/457 of query aligns to 85:527/546 of D9J041
- C122 (= C43) modified: Disulfide link with 127, Redox-active
- C127 (= C48) modified: Disulfide link with 122, Redox-active
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
32% identity, 98% coverage: 4:451/457 of query aligns to 170:612/631 of P16171
- Y264 (= Y95) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (≠ H444) 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.
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
31% identity, 98% coverage: 4:453/457 of query aligns to 1:454/465 of 3urhB
- active site: Y35 (= Y39), C39 (= C43), C44 (= C48), S47 (≠ T51), V183 (≠ Y180), E187 (= E184), H443 (≠ F442), H445 (= H444), E450 (= E449)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (≠ K13), G11 (≠ A14), E30 (= E33), K31 (≠ Q34), G37 (= G41), T38 (≠ A42), C39 (= C43), G43 (≠ A47), C44 (= C48), K48 (= K52), T111 (≠ K110), G112 (= G111), A140 (≠ N138), T141 (= T139), G142 (= G140), I184 (= I181), R273 (= R270), G312 (= G309), D313 (= D310), M319 (≠ Q316), L320 (≠ F317), A321 (≠ T318), H322 (≠ Y319)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
31% identity, 99% coverage: 1:453/457 of query aligns to 4:457/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (≠ Y180), E191 (= E184), H448 (= H444), E453 (= E449)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (≠ K13), G17 (≠ A14), E36 (= E33), K37 (≠ Q34), G43 (= G41), T44 (≠ A42), C45 (= C43), G49 (≠ A47), C50 (= C48), S53 (≠ T51), K54 (= K52), V117 (≠ K110), G118 (= G111), T147 (= T139), G148 (= G140), I188 (= I181), R276 (= R270), D316 (= D310), M322 (≠ Q316), L323 (≠ F317), A324 (≠ T318)
- binding zinc ion: H448 (= H444), E453 (= E449)
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
32% identity, 99% coverage: 3:453/457 of query aligns to 3:455/467 of 1dxlA
- active site: L38 (≠ M38), C42 (= C43), C47 (= C48), S50 (≠ T51), Y184 (= Y180), E188 (= E184), H444 (≠ F442), H446 (= H444), E451 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I9), P13 (≠ K13), G14 (≠ A14), E33 (= E33), K34 (≠ Q34), R35 (≠ S35), G40 (= G41), T41 (≠ A42), C42 (= C43), G46 (≠ A47), C47 (= C48), K51 (= K52), Y114 (≠ K110), G115 (= G111), T144 (= T139), G145 (= G140), Y184 (= Y180), I185 (= I181), R274 (= R270), D314 (= D310), M320 (≠ Q316), L321 (≠ F317), A322 (≠ T318), 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, 99% coverage: 3:453/457 of query aligns to 37:489/501 of P31023
- 67:76 (vs. 33:43, 36% identical) binding
- C76 (= C43) modified: Disulfide link with 81, Redox-active
- C81 (= C48) modified: Disulfide link with 76, Redox-active
- G149 (= G111) binding
- D348 (= D310) binding
- MLAH 354:357 (≠ QFTY 316:319) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
29% identity, 98% coverage: 3:449/457 of query aligns to 3:445/455 of 1ebdA
- active site: P13 (≠ K13), L37 (≠ Y39), C41 (= C43), C46 (= C48), S49 (≠ T51), N74 (= N84), V75 (≠ K85), Y180 (= Y180), E184 (= E184), S320 (≠ L322), H438 (≠ F442), H440 (= H444), E445 (= E449)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), P13 (≠ K13), V32 (= V32), E33 (= E33), K34 (≠ Q34), G39 (= G41), V40 (≠ A42), C41 (= C43), G45 (≠ A47), C46 (= C48), K50 (= K52), E112 (≠ K110), A113 (≠ G111), T141 (= T139), G142 (= G140), Y180 (= Y180), I181 (= I181), R268 (= R270), D308 (= D310), A314 (≠ Q316), L315 (≠ F317), A316 (≠ T318)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
29% identity, 98% coverage: 3:449/457 of query aligns to 9:451/470 of P11959
- 39:47 (vs. 33:43, 36% identical) binding
- K56 (= K52) binding
- D314 (= D310) binding
- A322 (≠ T318) binding
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
31% identity, 99% coverage: 1:453/457 of query aligns to 1:446/460 of 2eq6A
- active site: V37 (≠ Y39), C41 (= C43), C46 (= C48), T49 (= T51), A176 (≠ Y180), E180 (= E184), H435 (≠ F442), H437 (= H444), E442 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (≠ K13), G14 (≠ A14), E33 (= E33), A34 (≠ Q34), G39 (= G41), V40 (≠ A42), C41 (= C43), G45 (≠ A47), C46 (= C48), K50 (= K52), F111 (vs. gap), A112 (vs. gap), A135 (≠ N138), T136 (= T139), G137 (= G140), S155 (= S160), R269 (≠ M273), D306 (= D310), L312 (≠ Q316), L313 (≠ F317), A314 (≠ T318), H315 (≠ Y319), Y344 (≠ F351)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
29% identity, 98% coverage: 4:453/457 of query aligns to 2:443/455 of 2yquB
- active site: P11 (≠ K13), L36 (≠ Y39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ H66), V73 (≠ N67), V177 (≠ Y180), E181 (= E184), S314 (≠ L322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding carbonate ion: A310 (≠ T318), S314 (≠ L322), S423 (≠ T433), D426 (≠ F436)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (≠ K13), G12 (≠ A14), E31 (= E33), K32 (≠ Q34), G38 (= G41), T39 (≠ A42), C40 (= C43), R42 (≠ N45), G44 (≠ A47), C45 (= C48), K49 (= K52), T110 (≠ K110), A111 (≠ G111), T137 (= T139), G138 (= G140), I178 (= I181), Y265 (≠ M273), G301 (= G309), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ T318), H311 (≠ Y319)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
29% identity, 98% coverage: 4:453/457 of query aligns to 2:443/455 of 2yquA
- active site: P11 (≠ K13), L36 (≠ Y39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ H66), V73 (≠ N67), V177 (≠ Y180), E181 (= E184), S314 (≠ L322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (≠ K13), G12 (≠ A14), E31 (= E33), K32 (≠ Q34), G38 (= G41), T39 (≠ A42), C40 (= C43), R42 (≠ N45), G44 (≠ A47), C45 (= C48), K49 (= K52), T110 (≠ K110), A111 (≠ G111), T137 (= T139), G138 (= G140), S157 (= S160), I178 (= I181), Y265 (≠ M273), G301 (= G309), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ T318)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
29% identity, 98% coverage: 4:453/457 of query aligns to 2:443/452 of 2eq7A
- active site: P11 (≠ K13), L36 (≠ Y39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ H66), V73 (≠ N67), V177 (≠ Y180), E181 (= E184), S314 (≠ L322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (≠ K13), G12 (≠ A14), E31 (= E33), K32 (≠ Q34), G38 (= G41), T39 (≠ A42), C40 (= C43), R42 (≠ N45), G44 (≠ A47), C45 (= C48), K49 (= K52), T110 (≠ K110), A111 (≠ G111), T137 (= T139), G138 (= G140), S157 (= S160), I178 (= I181), R262 (= R270), Y265 (≠ M273), D302 (= D310), M308 (≠ Q316), L309 (≠ F317), A310 (≠ T318), H311 (≠ Y319), Y341 (≠ F351)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I148), G174 (= G177), G176 (= G179), V177 (≠ Y180), I178 (= I181), E197 (= E200), Y198 (≠ A201), V231 (≠ T234), V260 (≠ T268), G261 (= G269), R262 (= R270), M308 (≠ Q316), L309 (≠ F317), V339 (≠ A349)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
29% identity, 99% coverage: 2:453/457 of query aligns to 3:460/478 of P14218
- 34:49 (vs. 33:43, 25% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- G122 (= G111) binding
- D319 (= D310) binding
- A327 (≠ T318) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
28% identity, 99% coverage: 2:453/457 of query aligns to 5:462/477 of 5u8uD
- active site: P16 (≠ K13), L47 (≠ Y39), C51 (= C43), C56 (= C48), S59 (≠ T51), G85 (≠ K71), V86 (≠ Q72), V193 (≠ Y180), E197 (= E184), S333 (≠ L322), F451 (= F442), H453 (= H444), E458 (= E449)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (≠ K13), G17 (≠ A14), E36 (= E33), K37 (vs. gap), G49 (= G41), T50 (≠ A42), C51 (= C43), G55 (≠ A47), C56 (= C48), K60 (= K52), H123 (≠ K110), G124 (= G111), A152 (≠ N138), S153 (≠ T139), G154 (= G140), I194 (= I181), R281 (= R270), G320 (= G309), D321 (= D310), M327 (≠ Q316), L328 (≠ F317), A329 (≠ T318), H330 (≠ Y319), H453 (= H444), P454 (= P445)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
29% identity, 99% coverage: 2:453/457 of query aligns to 1:458/472 of 5u8vA
- active site: P12 (≠ K13), L43 (≠ Y39), C47 (= C43), C52 (= C48), S55 (≠ T51), G81 (≠ K71), V82 (≠ Q72), V189 (≠ Y180), E193 (= E184), S329 (≠ L322), F447 (= F442), H449 (= H444), E454 (= E449)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (≠ K13), G13 (≠ A14), E32 (= E33), G45 (= G41), T46 (≠ A42), C47 (= C43), G51 (≠ A47), C52 (= C48), K56 (= K52), H119 (≠ K110), G120 (= G111), A148 (≠ N138), S149 (≠ T139), G150 (= G140), S169 (= S160), I190 (= I181), R277 (= R270), G316 (= G309), D317 (= D310), M323 (≠ Q316), L324 (≠ F317), A325 (≠ T318), H326 (≠ Y319), H449 (= H444), P450 (= P445)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V176), G186 (= G177), G188 (= G179), V189 (≠ Y180), I190 (= I181), L208 (= L199), E209 (= E200), A210 (= A201), V243 (≠ T234), V275 (≠ T268), G276 (= G269)
Sites not aligning to the query:
Query Sequence
>351070 FitnessBrowser__Btheta:351070
MKQYDAIIIGFGKAGKTLAAELSNRGWQVAVVEQSDEMYGGACPNVACIPTKTLIHESEI
STLLYHNDFDKQSNMYRQAIARKNKLTSFLRENNYEKLSKRPNVTIYTGKGSLVSANTVK
VALPEEEIELQGKEIFINTGSTPIIPSIEGIQQSRNVYTSTTLLELDILPKHLIIVGGGY
IGLEFASMYAGFGSKVTLLEAGNRFMPRNDSDIAKSVREVMEKKGVEIRLNVRTQSIHDT
HDGVTLTYSDTSDGTPYFVDGDAILIATGRKPMIEGLNLQAAGVEVDAHGAIVVNDQLHT
NAPHIWAMGDVKGGAQFTYVSLDDFRIIRDQLFGDKKRDINDRDPLPYAVFIDPPLAHIG
ITEEEALRKGYSFKVSRLPATSVVRSRTLQQTDGMLKAIINSHSGKIMGCTMFCTDAPEL
INMVAMAMKTGQTSTFLRDFIFTHPSMSEGLNQLFDV
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