SitesBLAST
Comparing Ac3H11_4615 FitnessBrowser__acidovorax_3H11:Ac3H11_4615 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)
91% identity, 100% coverage: 1:561/561 of query aligns to 1:561/561 of P00392
- M1 (= M1) modified: Initiator methionine, Removed
- A110 (= A110) binding
- G130 (= G130) binding
- T135 (= T135) binding
- C136 (= C136) modified: Disulfide link with 141, Redox-active
- C141 (= C141) modified: Disulfide link with 136, Redox-active
- K145 (= K145) binding
- A211 (= A211) binding
- D403 (= D403) binding
- V411 (= V411) binding
- C558 (= C558) binding
- C559 (= C559) binding
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
92% identity, 83% coverage: 96:561/561 of query aligns to 2:467/467 of 4k7zA
- active site: G14 (= G108), I38 (= I132), A42 (≠ C136), A47 (≠ C141), S50 (= S144), V76 (= V170), P77 (= P171), V186 (= V280), E190 (= E284), A321 (= A415), F439 (= F533), Y441 (= Y535), E446 (= E540), C464 (= C558), C465 (= C559)
- binding flavin-adenine dinucleotide: I10 (= I104), G11 (= G105), G13 (= G107), A15 (= A109), E34 (= E128), R35 (= R129), G40 (= G134), T41 (= T135), A42 (≠ C136), G46 (= G140), A47 (≠ C141), K51 (= K145), E116 (= E210), A117 (= A211), T146 (= T240), G147 (= G241), R269 (= R363), G308 (= G402), D309 (= D403), Q315 (= Q409), F316 (= F410), V317 (= V411), Y318 (= Y412)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (= S278), S185 (= S279), V186 (= V280), V187 (= V281), E190 (= E284), R207 (= R301), N208 (≠ R302), R213 (= R307), T267 (= T361), G268 (= G362), R269 (= R363), Q315 (= Q409), F316 (= F410), V346 (= V440)
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
92% identity, 83% coverage: 96:561/561 of query aligns to 1:466/466 of 4k8dA
- active site: G13 (= G108), I37 (= I132), C41 (= C136), C46 (= C141), S49 (= S144), V75 (= V170), P76 (= P171), V185 (= V280), E189 (= E284), A320 (= A415), F438 (= F533), Y440 (= Y535), E445 (= E540), A463 (≠ C558), A464 (≠ C559)
- binding flavin-adenine dinucleotide: I9 (= I104), G10 (= G105), G12 (= G107), A14 (= A109), E33 (= E128), R34 (= R129), G39 (= G134), T40 (= T135), C41 (= C136), G45 (= G140), C46 (= C141), K50 (= K145), E115 (= E210), A116 (= A211), T145 (= T240), G146 (= G241), R268 (= R363), G307 (= G402), D308 (= D403), F315 (= F410), V316 (= V411), Y317 (= Y412)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (= S278), S184 (= S279), V185 (= V280), V186 (= V281), E189 (= E284), R206 (= R301), N207 (≠ R302), R212 (= R307), T266 (= T361), G267 (= G362), Q314 (= Q409), F315 (= F410), V345 (= V440)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
42% identity, 100% coverage: 3:561/561 of query aligns to 5:546/546 of D9J041
- C122 (= C136) modified: Disulfide link with 127, Redox-active
- C127 (= C141) modified: Disulfide link with 122, Redox-active
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
40% identity, 100% coverage: 3:561/561 of query aligns to 84:631/631 of P16171
- Y264 (= Y194) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y535) 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, 81% coverage: 96:549/561 of query aligns to 1:453/454 of 5x1yB
- active site: A13 (≠ G108), V37 (≠ I132), C41 (= C136), C46 (= C141), S49 (= S144), A74 (≠ V170), G75 (≠ P171), Y178 (≠ V280), E182 (= E284), A318 (= A415), A437 (≠ F533), Y439 (= Y535), E444 (= E540)
- binding flavin-adenine dinucleotide: I9 (= I104), G12 (= G107), I32 (= I127), E33 (= E128), R34 (= R129), G39 (= G134), T40 (= T135), C41 (= C136), G45 (= G140), C46 (= C141), K50 (= K145), A114 (= A211), T138 (= T240), G139 (= G241), Y178 (≠ V280), R266 (= R363), G305 (= G402), D306 (= D403), F313 (= F410), V314 (= V411), A317 (= A414)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
37% identity, 81% coverage: 100:552/561 of query aligns to 7:444/444 of 4ywoA
- active site: A15 (≠ G108), I39 (= I132), C43 (= C136), C48 (= C141), S51 (= S144), A174 (≠ V280), E178 (= E284), G308 (≠ A415), H425 (≠ F533), F427 (≠ Y535), E432 (= E540)
- binding flavin-adenine dinucleotide: G12 (= G105), G14 (= G107), K36 (≠ R129), G41 (= G134), T42 (= T135), C43 (= C136), G47 (= G140), C48 (= C141), K52 (= K145), A110 (= A211), A133 (= A239), T134 (= T240), G135 (= G241), N154 (≠ S260), L175 (≠ V281), L263 (= L370), G295 (= G402), D296 (= D403), M302 (≠ Q409), L303 (≠ F410), E304 (≠ V411), A307 (= A414)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
35% identity, 78% coverage: 103:540/561 of query aligns to 8:445/455 of 1ebdA
- active site: P13 (≠ G108), L37 (≠ I132), C41 (= C136), C46 (= C141), S49 (= S144), N74 (≠ V170), V75 (≠ P171), Y180 (≠ V280), E184 (= E284), S320 (≠ A415), H438 (≠ F533), H440 (≠ Y535), E445 (= E540)
- binding flavin-adenine dinucleotide: G10 (= G105), G12 (= G107), P13 (≠ G108), V32 (≠ I127), E33 (= E128), K34 (≠ R129), G39 (= G134), V40 (≠ T135), C41 (= C136), G45 (= G140), C46 (= C141), K50 (= K145), E112 (= E210), A113 (= A211), T141 (= T240), G142 (= G241), Y180 (≠ V280), I181 (≠ V281), R268 (= R363), D308 (= D403), A314 (≠ Q409), L315 (≠ F410), A316 (≠ V411)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
35% identity, 78% coverage: 103:540/561 of query aligns to 14:451/470 of P11959
- 39:47 (vs. 128:136, 56% identical) binding
- K56 (= K145) binding
- D314 (= D403) binding
- A322 (≠ V411) binding
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
36% identity, 81% coverage: 101:552/561 of query aligns to 6:454/460 of 2eq6A
- active site: V37 (≠ I132), C41 (= C136), C46 (= C141), T49 (≠ S144), A176 (≠ V280), E180 (= E284), H435 (≠ F533), H437 (≠ Y535), E442 (= E540)
- binding flavin-adenine dinucleotide: I9 (= I104), G10 (= G105), G12 (= G107), P13 (≠ G108), G14 (≠ A109), E33 (= E128), A34 (≠ R129), G39 (= G134), V40 (≠ T135), C41 (= C136), G45 (= G140), C46 (= C141), K50 (= K145), F111 (≠ E210), A112 (= A211), A135 (= A239), T136 (= T240), G137 (= G241), S155 (= S260), R269 (≠ N366), D306 (= D403), L312 (≠ Q409), L313 (≠ F410), A314 (≠ V411), H315 (≠ Y412), Y344 (≠ F442)
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, 82% coverage: 96:556/561 of query aligns to 4:466/474 of P0A9P0
- K220 (≠ D318) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
30% identity, 82% coverage: 96:556/561 of query aligns to 3:465/471 of 4jdrA
- active site: P15 (≠ G108), L40 (≠ I132), C44 (= C136), C49 (= C141), S52 (= S144), E77 (≠ V170), P78 (= P171), I184 (≠ V280), E188 (= E284), V324 (≠ A415), H442 (≠ F533), H444 (≠ Y535), E449 (= E540)
- binding flavin-adenine dinucleotide: G12 (= G105), G14 (= G107), P15 (≠ G108), A16 (= A109), E35 (= E128), R36 (= R129), Y37 (vs. gap), V43 (≠ T135), C44 (= C136), G48 (= G140), C49 (= C141), K53 (= K145), L115 (≠ E210), G116 (≠ A211), A144 (≠ T240), G145 (= G241), I185 (≠ V281), G311 (= G402), D312 (= D403), M318 (≠ Q409), L319 (≠ F410), A320 (≠ V411), H321 (≠ Y412)
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, 80% coverage: 97:546/561 of query aligns to 3:462/475 of 6awaA
- active site: L45 (≠ I132), C49 (= C136), C54 (= C141), S57 (= S144), V191 (= V280), E195 (= E284), F449 (= F533), H451 (≠ Y535), E456 (= E540)
- binding adenosine monophosphate: I187 (= I276), E211 (vs. gap), A212 (= A300), L213 (≠ R301), V245 (≠ T331), V277 (≠ T361)
- binding flavin-adenine dinucleotide: I10 (= I104), G13 (= G107), P14 (≠ G108), G15 (≠ A109), E34 (= E128), K35 (≠ R129), T48 (= T135), C49 (= C136), G53 (= G140), C54 (= C141), K58 (= K145), H121 (≠ E210), G122 (≠ A211), S151 (≠ T240), G152 (= G241), I192 (≠ V281), R279 (= R363), G318 (= G402), D319 (= D403), M325 (≠ Q409), L326 (≠ F410), A327 (≠ V411), Y358 (≠ F442)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
29% identity, 80% coverage: 97:546/561 of query aligns to 5:459/470 of 6uziC
- active site: C45 (= C136), C50 (= C141), S53 (= S144), V187 (= V280), E191 (= E284), H448 (≠ Y535), E453 (= E540)
- binding flavin-adenine dinucleotide: I12 (= I104), G13 (= G105), G15 (= G107), P16 (≠ G108), G17 (≠ A109), E36 (= E128), K37 (≠ R129), G43 (= G134), T44 (= T135), C45 (= C136), G49 (= G140), C50 (= C141), S53 (= S144), K54 (= K145), V117 (≠ E210), G118 (≠ A211), T147 (= T240), G148 (= G241), I188 (≠ V281), R276 (= R363), D316 (= D403), M322 (≠ Q409), L323 (≠ F410), A324 (≠ V411)
- binding zinc ion: H448 (≠ Y535), E453 (= E540)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
30% identity, 79% coverage: 100:543/561 of query aligns to 1:425/432 of 6kyyA
- active site: C39 (= C136), C44 (= C141), T47 (≠ S144), Y159 (≠ V280), E163 (= E284), H417 (≠ Y535), E422 (= E540)
- binding copper (ii) ion: C39 (= C136), C44 (= C141), H226 (≠ T346), H229 (= H349), T291 (≠ V411)
- binding flavin-adenine dinucleotide: F7 (≠ S106), G8 (= G107), E29 (= E128), Q30 (≠ R129), M34 (vs. gap), T38 (= T135), C39 (= C136), C44 (= C141), K48 (= K145), A95 (= A211), N117 (≠ A239), T118 (= T240), G119 (= G241), I160 (≠ V281), R243 (= R363), D283 (= D403), F290 (= F410), T291 (≠ V411), S294 (≠ A414)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
31% identity, 80% coverage: 101:546/561 of query aligns to 4:445/452 of 2eq7A
- active site: P11 (≠ G108), L36 (≠ I132), C40 (= C136), C45 (= C141), S48 (= S144), G72 (≠ A168), V73 (≠ T169), V177 (= V280), E181 (= E284), S314 (≠ A415), H432 (≠ F533), H434 (≠ Y535), E439 (= E540)
- binding flavin-adenine dinucleotide: G10 (= G107), P11 (≠ G108), G12 (≠ A109), E31 (= E128), K32 (≠ R129), G38 (= G134), T39 (= T135), C40 (= C136), R42 (≠ N138), G44 (= G140), C45 (= C141), K49 (= K145), T110 (≠ E210), A111 (= A211), T137 (= T240), G138 (= G241), S157 (= S260), I178 (≠ V281), R262 (= R363), Y265 (≠ N366), D302 (= D403), M308 (≠ Q409), L309 (≠ F410), A310 (≠ V411), H311 (≠ Y412), Y341 (≠ F442)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I249), G174 (= G277), G176 (≠ S279), V177 (= V280), I178 (≠ V281), E197 (≠ A300), Y198 (≠ R301), V231 (≠ A333), V260 (≠ T361), G261 (= G362), R262 (= R363), M308 (≠ Q409), L309 (≠ F410), V339 (= V440)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
31% identity, 80% coverage: 101:546/561 of query aligns to 4:445/455 of 2yquB
- active site: P11 (≠ G108), L36 (≠ I132), C40 (= C136), C45 (= C141), S48 (= S144), G72 (≠ A168), V73 (≠ T169), V177 (= V280), E181 (= E284), S314 (≠ A415), H432 (≠ F533), H434 (≠ Y535), E439 (= E540)
- binding carbonate ion: A310 (≠ V411), S314 (≠ A415), S423 (≠ T524), D426 (≠ E527)
- binding flavin-adenine dinucleotide: G8 (= G105), G10 (= G107), P11 (≠ G108), G12 (≠ A109), E31 (= E128), K32 (≠ R129), G38 (= G134), T39 (= T135), C40 (= C136), R42 (≠ N138), G44 (= G140), C45 (= C141), K49 (= K145), T110 (≠ E210), A111 (= A211), T137 (= T240), G138 (= G241), I178 (≠ V281), Y265 (≠ N366), G301 (= G402), D302 (= D403), M308 (≠ Q409), L309 (≠ F410), A310 (≠ V411), H311 (≠ Y412)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
31% identity, 80% coverage: 101:546/561 of query aligns to 4:445/455 of 2yquA
- active site: P11 (≠ G108), L36 (≠ I132), C40 (= C136), C45 (= C141), S48 (= S144), G72 (≠ A168), V73 (≠ T169), V177 (= V280), E181 (= E284), S314 (≠ A415), H432 (≠ F533), H434 (≠ Y535), E439 (= E540)
- binding flavin-adenine dinucleotide: G8 (= G105), G10 (= G107), P11 (≠ G108), G12 (≠ A109), E31 (= E128), K32 (≠ R129), G38 (= G134), T39 (= T135), C40 (= C136), R42 (≠ N138), G44 (= G140), C45 (= C141), K49 (= K145), T110 (≠ E210), A111 (= A211), T137 (= T240), G138 (= G241), S157 (= S260), I178 (≠ V281), Y265 (≠ N366), G301 (= G402), D302 (= D403), M308 (≠ Q409), L309 (≠ F410), A310 (≠ V411)
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
30% identity, 80% coverage: 97:543/561 of query aligns to 2:434/441 of 6kgyB
- active site: C43 (= C136), C48 (= C141), T51 (≠ S144), Y168 (≠ V280), E172 (= E284), H426 (≠ Y535), E431 (= E540)
- binding flavin-adenine dinucleotide: I9 (= I104), G12 (= G107), E33 (= E128), Q34 (≠ R129), M38 (vs. gap), G41 (= G134), T42 (= T135), G47 (= G140), C48 (= C141), A99 (= A211), N126 (≠ A239), T127 (= T240), G128 (= G241), G291 (= G402), D292 (= D403), F299 (= F410), T300 (≠ V411), Y301 (= Y412), S303 (≠ A414), F333 (= F442)
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, 81% coverage: 97:550/561 of query aligns to 2:465/472 of 3ladA
- active site: L44 (≠ I132), C48 (= C136), C53 (= C141), S56 (= S144), V190 (= V280), E194 (= E284), F448 (= F533), H450 (≠ Y535), E455 (= E540)
- binding flavin-adenine dinucleotide: I9 (= I104), G10 (= G105), G12 (= G107), P13 (≠ G108), E33 (= E128), K34 (≠ R129), G46 (= G134), T47 (= T135), C48 (= C136), G52 (= G140), C53 (= C141), H120 (≠ E210), G121 (≠ A211), A149 (= A239), S150 (≠ T240), G151 (= G241), I191 (≠ V281), R278 (= R363), D318 (= D403), L325 (≠ F410), A326 (≠ V411)
Query Sequence
>Ac3H11_4615 FitnessBrowser__acidovorax_3H11:Ac3H11_4615
MTHLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLATEAGTSPDALTAAVVGL
GYKATLADAPPTDNCTGLLDKVSGWMGAADERSDGEHQLQIAVIGSGGAAMAAALKAVEQ
GAHVTLIERGTIGGTCVNIGCVPSKIMIRAAHIAHLRRESPFDGGITATVPAIDRSKLLA
QQQALVDELRHAKYEGILDSNSAITVLHGEARFKDDQSVVVRLNEGGERVVMFDRCLVAT
GASPAVPPIPGLKESPYWTSTEALVSETVPERLAVIGSSVVALELAQAFARLGSQVTILA
RRTLFFREDPAIGEAVTDAFRAEGITVLEHTQASQVAHVNREFVLTTGHGEIRADKLLVA
TGRTPNTRSLALDAAGVTVNAQGAIVIDKGMRTSTPHIYAAGDCADQPQFVYVAAAAGTR
AAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALAN
FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVE
GLKLAAQTFSKDVKQLSCCAG
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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