SitesBLAST
Comparing 7022666 FitnessBrowser__ANA3:7022666 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)
57% identity, 100% coverage: 1:551/551 of query aligns to 1:561/561 of P00392
- M1 (= M1) modified: Initiator methionine, Removed
- A110 (= A100) binding
- G130 (≠ A120) binding
- T135 (≠ C126) binding
- C136 (= C127) modified: Disulfide link with 141, Redox-active
- C141 (= C132) modified: Disulfide link with 136, Redox-active
- K145 (= K136) binding
- A211 (= A201) binding
- D403 (= D393) binding
- V411 (= V401) binding
- C558 (= C548) binding
- C559 (= C549) binding
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
62% identity, 84% coverage: 90:551/551 of query aligns to 6:467/467 of 4k7zA
- active site: G14 (≠ S98), I38 (= I123), A42 (≠ C127), A47 (≠ C132), S50 (= S135), V76 (≠ A160), P77 (= P161), V186 (= V270), E190 (= E274), A321 (= A405), F439 (= F523), Y441 (= Y525), E446 (= E530), C464 (= C548), C465 (= C549)
- binding flavin-adenine dinucleotide: I10 (= I94), G11 (= G95), G13 (= G97), A15 (≠ G99), E34 (= E118), R35 (≠ G119), G40 (= G125), T41 (≠ C126), A42 (≠ C127), G46 (= G131), A47 (≠ C132), K51 (= K136), E116 (≠ W200), A117 (= A201), T146 (= T230), G147 (= G231), R269 (= R353), G308 (= G392), D309 (= D393), Q315 (= Q399), F316 (= F400), V317 (= V401), Y318 (= Y402)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (= S268), S185 (= S269), V186 (= V270), V187 (= V271), E190 (= E274), R207 (= R291), N208 (≠ H292), R213 (≠ S297), T267 (= T351), G268 (= G352), R269 (= R353), Q315 (= Q399), F316 (= F400), V346 (= V430)
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
62% identity, 84% coverage: 90:551/551 of query aligns to 5:466/466 of 4k8dA
- active site: G13 (≠ S98), I37 (= I123), C41 (= C127), C46 (= C132), S49 (= S135), V75 (≠ A160), P76 (= P161), V185 (= V270), E189 (= E274), A320 (= A405), F438 (= F523), Y440 (= Y525), E445 (= E530), A463 (≠ C548), A464 (≠ C549)
- binding flavin-adenine dinucleotide: I9 (= I94), G10 (= G95), G12 (= G97), A14 (≠ G99), E33 (= E118), R34 (≠ G119), G39 (= G125), T40 (≠ C126), C41 (= C127), G45 (= G131), C46 (= C132), K50 (= K136), E115 (≠ W200), A116 (= A201), T145 (= T230), G146 (= G231), R268 (= R353), G307 (= G392), D308 (= D393), F315 (= F400), V316 (= V401), Y317 (= Y402)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (= S268), S184 (= S269), V185 (= V270), V186 (= V271), E189 (= E274), R206 (= R291), N207 (≠ H292), R212 (≠ S297), T266 (= T351), G267 (= G352), Q314 (= Q399), F315 (= F400), V345 (= V430)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
41% identity, 99% coverage: 4:551/551 of query aligns to 6:546/546 of D9J041
- C122 (= C127) modified: Disulfide link with 127, Redox-active
- C127 (= C132) 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, 99% coverage: 4:551/551 of query aligns to 85:631/631 of P16171
- Y264 (= Y184) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y525) 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)
43% identity, 81% coverage: 93:540/551 of query aligns to 8:454/454 of 5x1yB
- active site: A13 (≠ S98), V37 (= V122), C41 (= C127), C46 (= C132), S49 (= S135), A74 (= A160), G75 (≠ P161), Y178 (≠ V270), E182 (= E274), A318 (= A405), A437 (≠ F523), Y439 (= Y525), E444 (= E530)
- binding flavin-adenine dinucleotide: I9 (= I94), G12 (= G97), I32 (= I117), E33 (= E118), R34 (≠ G119), G39 (= G125), T40 (≠ C126), C41 (= C127), G45 (= G131), C46 (= C132), K50 (= K136), A114 (= A201), T138 (= T230), G139 (= G231), Y178 (≠ V270), R266 (= R353), G305 (= G392), D306 (= D393), F313 (= F400), V314 (= V401), A317 (= A404)
4ywoA Mercuric reductase from metallosphaera sedula (see paper)
37% identity, 82% coverage: 89:542/551 of query aligns to 6:444/444 of 4ywoA
- active site: A15 (≠ S98), I39 (= I123), C43 (= C127), C48 (= C132), S51 (= S135), A174 (≠ V270), E178 (= E274), G308 (≠ A405), H425 (≠ F523), F427 (≠ Y525), E432 (= E530)
- binding flavin-adenine dinucleotide: G12 (= G95), G14 (= G97), K36 (≠ A120), G41 (= G125), T42 (≠ C126), C43 (= C127), G47 (= G131), C48 (= C132), K52 (= K136), A110 (= A201), A133 (= A229), T134 (= T230), G135 (= G231), N154 (≠ S250), L175 (≠ V271), L263 (= L360), G295 (= G392), D296 (= D393), M302 (≠ Q399), L303 (≠ F400), E304 (≠ V401), A307 (= A404)
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)
33% identity, 88% coverage: 61:543/551 of query aligns to 11:499/501 of P31023
- 67:76 (vs. 118:127, 40% identical) binding
- C76 (= C127) modified: Disulfide link with 81, Redox-active
- C81 (= C132) modified: Disulfide link with 76, Redox-active
- G149 (≠ A201) binding
- D348 (= D393) binding
- MLAH 354:357 (≠ QFVY 399:402) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
34% identity, 82% coverage: 91:543/551 of query aligns to 6:465/467 of 1dxlA
- active site: L38 (≠ I123), C42 (= C127), C47 (= C132), S50 (= S135), Y184 (≠ V270), E188 (= E274), H444 (≠ F523), H446 (≠ Y525), E451 (= E530)
- binding flavin-adenine dinucleotide: I9 (= I94), P13 (≠ S98), G14 (= G99), E33 (= E118), K34 (≠ G119), R35 (≠ A120), G40 (= G125), T41 (≠ C126), C42 (= C127), G46 (= G131), C47 (= C132), K51 (= K136), Y114 (≠ W200), G115 (≠ A201), T144 (= T230), G145 (= G231), Y184 (≠ V270), I185 (≠ V271), R274 (= R353), D314 (= D393), M320 (≠ Q399), L321 (≠ F400), A322 (≠ V401), H323 (≠ Y402)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
31% identity, 81% coverage: 91:536/551 of query aligns to 9:459/470 of 6uziC
- active site: C45 (= C127), C50 (= C132), S53 (= S135), V187 (= V270), E191 (= E274), H448 (≠ Y525), E453 (= E530)
- binding flavin-adenine dinucleotide: I12 (= I94), G13 (= G95), G15 (= G97), P16 (≠ S98), G17 (= G99), E36 (= E118), K37 (≠ G119), G43 (= G125), T44 (≠ C126), C45 (= C127), G49 (= G131), C50 (= C132), S53 (= S135), K54 (= K136), V117 (≠ W200), G118 (≠ A201), T147 (= T230), G148 (= G231), I188 (≠ V271), R276 (= R353), D316 (= D393), M322 (≠ Q399), L323 (≠ F400), A324 (≠ V401)
- binding zinc ion: H448 (≠ Y525), E453 (= E530)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
36% identity, 83% coverage: 87:541/551 of query aligns to 2:453/460 of 2eq6A
- active site: V37 (= V122), C41 (= C127), C46 (= C132), T49 (≠ S135), A176 (≠ V270), E180 (= E274), H435 (≠ F523), H437 (≠ Y525), E442 (= E530)
- binding flavin-adenine dinucleotide: I9 (= I94), G10 (= G95), G12 (= G97), P13 (≠ S98), G14 (= G99), E33 (= E118), A34 (≠ G119), G39 (= G125), V40 (≠ C126), C41 (= C127), G45 (= G131), C46 (= C132), K50 (= K136), F111 (≠ W200), A112 (= A201), A135 (= A229), T136 (= T230), G137 (= G231), S155 (= S250), R269 (≠ N356), D306 (= D393), L312 (≠ Q399), L313 (≠ F400), A314 (≠ V401), H315 (≠ Y402), Y344 (≠ F432)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
32% identity, 82% coverage: 91:543/551 of query aligns to 7:470/472 of 1zmdA
- active site: L39 (≠ I123), C43 (= C127), C48 (= C132), S51 (= S135), V186 (= V270), E190 (= E274), H448 (≠ F523), H450 (≠ Y525), E455 (= E530)
- binding flavin-adenine dinucleotide: I10 (= I94), G11 (= G95), G13 (= G97), P14 (≠ S98), G15 (= G99), E34 (= E118), K35 (≠ G119), N36 (≠ A120), G41 (= G125), T42 (≠ C126), C43 (= C127), G47 (= G131), C48 (= C132), K52 (= K136), Y116 (≠ W200), G117 (≠ A201), T146 (= T230), G147 (= G231), S166 (= S250), R278 (= R353), F281 (≠ N356), G317 (= G392), D318 (= D393), M324 (≠ Q399), L325 (≠ F400), A326 (≠ V401), H327 (≠ Y402)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I266), G183 (= G267), G185 (≠ S269), V186 (= V270), I187 (≠ V271), E190 (= E274), E206 (≠ A290), F207 (≠ R291), L208 (vs. gap), I276 (≠ T351), G277 (= G352), R278 (= R353), M324 (≠ Q399), L325 (≠ F400), V355 (= V430), Y357 (≠ F432)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
32% identity, 82% coverage: 91:543/551 of query aligns to 7:470/472 of 1zmcA
- active site: L39 (≠ I123), C43 (= C127), C48 (= C132), S51 (= S135), V186 (= V270), E190 (= E274), H448 (≠ F523), H450 (≠ Y525), E455 (= E530)
- binding flavin-adenine dinucleotide: I10 (= I94), G11 (= G95), G13 (= G97), P14 (≠ S98), G15 (= G99), E34 (= E118), K35 (≠ G119), N36 (≠ A120), G41 (= G125), T42 (≠ C126), C43 (= C127), G47 (= G131), C48 (= C132), K52 (= K136), Y116 (≠ W200), G117 (≠ A201), T146 (= T230), G147 (= G231), S166 (= S250), I187 (≠ V271), F281 (≠ N356), G317 (= G392), D318 (= D393), M324 (≠ Q399), L325 (≠ F400), A326 (≠ V401), H327 (≠ Y402)
- binding nicotinamide-adenine-dinucleotide: G183 (= G267), G185 (≠ S269), V205 (≠ L289), E206 (≠ A290), F207 (≠ R291), L208 (vs. gap), K240 (≠ Q322), V241 (≠ A323), I276 (≠ T351), G277 (= G352), R278 (= R353), R297 (≠ K372), M324 (≠ Q399)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
32% identity, 82% coverage: 91:543/551 of query aligns to 44:507/509 of P09622
- 71:80 (vs. 118:127, 40% identical) binding
- K72 (≠ G119) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K136) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ N151) to T: in dbSNP:rs1130477
- G154 (≠ A201) binding
- TGS 183:185 (= TGS 230:232) binding
- 220:227 (vs. 267:274, 38% identical) binding
- E243 (≠ A290) binding
- V278 (≠ A323) binding
- G314 (= G352) binding
- D355 (= D393) binding
- MLAH 361:364 (≠ QFVY 399:402) binding
- E375 (≠ I413) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ K421) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G486) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
- E466 (≠ S504) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ N511) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
- D479 (≠ E517) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ D520) to G: in DLDD; reduced enzyme activity; dbSNP:rs397514650; mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
- H485 (≠ F523) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (≠ L526) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ V529) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E530) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K533) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (= K541) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
32% identity, 82% coverage: 91:543/551 of query aligns to 17:480/482 of 6hg8B
- active site: C53 (= C127), C58 (= C132), S61 (= S135), V196 (= V270), E200 (= E274), H460 (≠ F523), E465 (≠ M528)
- binding flavin-adenine dinucleotide: I20 (= I94), G23 (= G97), P24 (≠ S98), G25 (= G99), E44 (= E118), K45 (≠ G119), N46 (≠ A120), G51 (= G125), T52 (≠ C126), C53 (= C127), G57 (= G131), C58 (= C132), K62 (= K136), Y126 (≠ W200), G127 (≠ A201), T156 (= T230), G157 (= G231), I197 (≠ V271), R288 (= R353), F291 (≠ N356), G327 (= G392), D328 (= D393), M334 (≠ Q399), L335 (≠ F400), A336 (≠ V401), H337 (≠ Y402)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
32% identity, 79% coverage: 93:530/551 of query aligns to 8:445/455 of 1ebdA
- active site: P13 (≠ S98), L37 (≠ I123), C41 (= C127), C46 (= C132), S49 (= S135), N74 (≠ A160), V75 (≠ P161), Y180 (≠ V270), E184 (= E274), S320 (≠ A405), H438 (≠ F523), H440 (≠ Y525), E445 (= E530)
- binding flavin-adenine dinucleotide: G10 (= G95), G12 (= G97), P13 (≠ S98), V32 (≠ I117), E33 (= E118), K34 (≠ G119), G39 (= G125), V40 (≠ C126), C41 (= C127), G45 (= G131), C46 (= C132), K50 (= K136), E112 (≠ W200), A113 (= A201), T141 (= T230), G142 (= G231), Y180 (≠ V270), I181 (≠ V271), R268 (= R353), D308 (= D393), A314 (≠ Q399), L315 (≠ F400), A316 (≠ V401)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
32% identity, 79% coverage: 93:530/551 of query aligns to 14:451/470 of P11959
- 39:47 (vs. 118:127, 40% identical) binding
- K56 (= K136) binding
- D314 (= D393) binding
- A322 (≠ V401) binding
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 81% coverage: 93:536/551 of query aligns to 6:445/455 of 2yquB
- active site: P11 (≠ S98), L36 (≠ I123), C40 (= C127), C45 (= C132), S48 (= S135), G72 (= G155), V73 (≠ L156), V177 (= V270), E181 (= E274), S314 (≠ A405), H432 (≠ F523), H434 (≠ Y525), E439 (= E530)
- binding carbonate ion: A310 (≠ V401), S314 (≠ A405), S423 (≠ T514), D426 (≠ E517)
- binding flavin-adenine dinucleotide: G8 (= G95), G10 (= G97), P11 (≠ S98), G12 (= G99), E31 (= E118), K32 (≠ G119), G38 (= G125), T39 (≠ C126), C40 (= C127), R42 (≠ N129), G44 (= G131), C45 (= C132), K49 (= K136), T110 (≠ W200), A111 (= A201), T137 (= T230), G138 (= G231), I178 (≠ V271), Y265 (≠ N356), G301 (= G392), D302 (= D393), M308 (≠ Q399), L309 (≠ F400), A310 (≠ V401), H311 (≠ Y402)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 81% coverage: 93:536/551 of query aligns to 6:445/455 of 2yquA
- active site: P11 (≠ S98), L36 (≠ I123), C40 (= C127), C45 (= C132), S48 (= S135), G72 (= G155), V73 (≠ L156), V177 (= V270), E181 (= E274), S314 (≠ A405), H432 (≠ F523), H434 (≠ Y525), E439 (= E530)
- binding flavin-adenine dinucleotide: G8 (= G95), G10 (= G97), P11 (≠ S98), G12 (= G99), E31 (= E118), K32 (≠ G119), G38 (= G125), T39 (≠ C126), C40 (= C127), R42 (≠ N129), G44 (= G131), C45 (= C132), K49 (= K136), T110 (≠ W200), A111 (= A201), T137 (= T230), G138 (= G231), S157 (= S250), I178 (≠ V271), Y265 (≠ N356), G301 (= G392), D302 (= D393), M308 (≠ Q399), L309 (≠ F400), A310 (≠ V401)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
32% identity, 81% coverage: 93:536/551 of query aligns to 6:445/452 of 2eq7A
- active site: P11 (≠ S98), L36 (≠ I123), C40 (= C127), C45 (= C132), S48 (= S135), G72 (= G155), V73 (≠ L156), V177 (= V270), E181 (= E274), S314 (≠ A405), H432 (≠ F523), H434 (≠ Y525), E439 (= E530)
- binding flavin-adenine dinucleotide: G10 (= G97), P11 (≠ S98), G12 (= G99), E31 (= E118), K32 (≠ G119), G38 (= G125), T39 (≠ C126), C40 (= C127), R42 (≠ N129), G44 (= G131), C45 (= C132), K49 (= K136), T110 (≠ W200), A111 (= A201), T137 (= T230), G138 (= G231), S157 (= S250), I178 (≠ V271), R262 (= R353), Y265 (≠ N356), D302 (= D393), M308 (≠ Q399), L309 (≠ F400), A310 (≠ V401), H311 (≠ Y402), Y341 (≠ F432)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I239), G174 (= G267), G176 (≠ S269), V177 (= V270), I178 (≠ V271), E197 (≠ A290), Y198 (≠ R291), V231 (≠ A323), V260 (≠ T351), G261 (= G352), R262 (= R353), M308 (≠ Q399), L309 (≠ F400), V339 (= V430)
Query Sequence
>7022666 FitnessBrowser__ANA3:7022666
MILLSIEGMTCPSCVAHVKEALDAIEGVNKVEISYENASATITTNGGVSVTDLIGAIEAL
GYNPLAENTAPNAYCDNENTSNTESNRTQHVAIIGTGSGAFACAIKAAEGGAKVTLIEGA
DVIGGCCVNVGCVPSKILIRAAQLAQQQRNNPFAGLENHAPQLSRALLAQQQTARVEELR
AAKYQNILETNPALSLLKGWAQFKNANTLIVRKNDGTEQEIFADKILIATGSTPTIPPIE
GLAETPYWTSTEALFAEELPQHLVVIGSSVVALEIAQAYRRLGSEVTVLARHSLLYSEDP
IIGEKLAGCFEKEGIRVLNNTQATQVTHDGNQFTLNTNAGELSCDRLLVSTGRHANTSQL
NLDAVGVTTNKKGEIVVNERMETNVAGIYAAGDCSNMPQFVYVAAAAGSRAGINMTGGDA
KLDLSTMPAVIFTDPQVATVGLTEEQARAQDIETDSRVLGMENVPRALANFETDGFIKLV
TEKETGLLLGAQILAHEGGELIQSAALAIRNRMTVTELADQLFPYLTMVEGLKLCAQTFN
KDVKELSCCAG
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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