SitesBLAST
Comparing WP_013835779.1 NCBI__GCF_000214825.1:WP_013835779.1 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)
3ic9C The structure of dihydrolipoamide dehydrogenase from colwellia psychrerythraea 34h.
37% identity, 95% coverage: 6:446/462 of query aligns to 4:462/483 of 3ic9C
- active site: C45 (= C47), C50 (= C52), S53 (= S55), V183 (= V187), E187 (= E191), H451 (= H435), E456 (= E440)
- binding flavin-adenine dinucleotide: I13 (= I15), G14 (= G16), G16 (= G18), T17 (≠ S19), E37 (≠ D39), G38 (≠ S40), T44 (= T46), G49 (= G51), C50 (= C52), K54 (= K56), F117 (≠ R121), A118 (= A122), T143 (≠ V146), G144 (= G147), N163 (≠ S167), I184 (= I188), R271 (= R269), G311 (= G301), D312 (= D302), T318 (≠ G308), L319 (≠ I309), L320 (= L310)
Sites not aligning to the query:
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
28% identity, 92% coverage: 14:440/462 of query aligns to 14:451/470 of P11959
- 39:47 (vs. 39:47, 44% identical) binding FAD
- K56 (= K56) binding FAD
- D314 (= D302) binding FAD
- A322 (≠ L310) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
28% identity, 92% coverage: 14:440/462 of query aligns to 8:445/455 of 1ebdA
- active site: P13 (≠ S19), L37 (= L43), C41 (= C47), C46 (= C52), S49 (= S55), N74 (≠ C80), V75 (≠ L81), Y180 (≠ V187), E184 (= E191), S320 (≠ N314), H438 (≠ Y433), H440 (= H435), E445 (= E440)
- binding flavin-adenine dinucleotide: G10 (= G16), G12 (= G18), P13 (≠ S19), V32 (= V38), E33 (≠ D39), K34 (≠ S40), G39 (≠ T45), V40 (≠ T46), C41 (= C47), G45 (= G51), C46 (= C52), K50 (= K56), E112 (≠ R121), A113 (= A122), T141 (≠ V146), G142 (= G147), Y180 (≠ V187), I181 (= I188), R268 (= R269), D308 (= D302), A314 (≠ G308), L315 (≠ I309), A316 (≠ L310)
8qcjA Crystal structure of mycothiol disulfide reductase mtr from rhodococcus erythropolis (see paper)
26% identity, 94% coverage: 13:446/462 of query aligns to 7:453/458 of 8qcjA
- binding flavin-adenine dinucleotide: G10 (= G16), G12 (= G18), L30 (≠ V38), E31 (≠ D39), E32 (≠ S40), G37 (≠ T45), T38 (= T46), G43 (= G51), A113 (≠ K129), A138 (≠ V146), G139 (= G147), N158 (≠ S167), F178 (≠ V187), I179 (= I188), D302 (= D302), Q308 (≠ G308), L309 (≠ I309), K310 (≠ L310), H311 (= H311)
P09063 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of branched-chain alpha-keto acid dehydrogenase complex; LPD-Val; EC 1.8.1.4 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
29% identity, 89% coverage: 36:444/462 of query aligns to 33:447/459 of P09063
- 36:44 (vs. 39:47, 44% identical) binding FAD
- C44 (= C47) modified: Disulfide link with 49, Redox-active
- C49 (= C52) modified: Disulfide link with 44, Redox-active
- K53 (= K56) binding FAD
- A119 (= A122) binding FAD
- A142 (= A145) binding FAD
- GGGYI 179:183 (≠ GLGVI 184:188) binding NAD(+)
- Y182 (≠ V187) binding FAD
- E202 (≠ D207) binding NAD(+)
- V236 (= V240) binding NAD(+)
- AVGR 264:267 (≠ TLGR 266:269) binding NAD(+)
- D306 (= D302) binding FAD
- M312 (≠ G308) binding NAD(+)
- A314 (≠ L310) binding FAD
1lvlA The refined structure of pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 angstroms resolution (see paper)
29% identity, 89% coverage: 36:444/462 of query aligns to 32:446/458 of 1lvlA
- active site: L39 (= L43), C43 (= C47), C48 (= C52), S51 (= S55), S79 (≠ C80), P80 (= P82), Y181 (≠ V187), E185 (= E191), M317 (≠ N314), H435 (≠ Y433), H437 (= H435), E442 (= E440)
- binding flavin-adenine dinucleotide: E35 (≠ D39), G36 (≠ S40), G41 (≠ T45), T42 (= T46), C43 (= C47), G47 (= G51), C48 (= C52), K52 (= K56), W117 (≠ R121), A118 (= A122), A141 (= A145), T142 (≠ V146), G143 (= G147), Y181 (≠ V187), R266 (= R269), R269 (≠ N272), D305 (= D302), L312 (≠ I309), A313 (≠ L310), H314 (= H311)
- binding nicotinamide-adenine-dinucleotide: V177 (≠ I183), G178 (= G184), Y181 (≠ V187), I182 (= I188), E201 (≠ D207), A263 (≠ T266), V264 (≠ L267), G265 (= G268), R266 (= R269), E309 (≠ F306), M311 (≠ G308)
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.
27% identity, 94% coverage: 8:443/462 of query aligns to 3:459/475 of 6awaA
- active site: L45 (= L43), C49 (= C47), C54 (= C52), S57 (= S55), V191 (= V187), E195 (= E191), F449 (≠ Y433), H451 (= H435), E456 (= E440)
- binding adenosine monophosphate: I187 (= I183), E211 (≠ D207), A212 (= A208), L213 (≠ Q209), V245 (= V240), V277 (≠ L267)
- binding flavin-adenine dinucleotide: I10 (= I15), G13 (= G18), P14 (≠ S19), G15 (≠ A20), E34 (≠ K29), K35 (= K30), T48 (= T46), C49 (= C47), G53 (= G51), C54 (= C52), K58 (= K56), H121 (≠ D127), G122 (= G128), S151 (≠ V146), G152 (= G147), I192 (= I188), R279 (= R269), G318 (= G301), D319 (= D302), M325 (≠ G308), L326 (≠ I309), A327 (≠ L310), Y358 (≠ F343)
Sites not aligning to the query:
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
28% identity, 94% coverage: 14:449/462 of query aligns to 8:451/460 of 2eq6A
- active site: V37 (≠ L43), C41 (= C47), C46 (= C52), T49 (≠ S55), A176 (≠ V187), E180 (= E191), H435 (≠ Y433), H437 (= H435), E442 (= E440)
- binding flavin-adenine dinucleotide: I9 (= I15), G10 (= G16), G12 (= G18), P13 (≠ S19), G14 (≠ A20), E33 (≠ D39), A34 (≠ S40), G39 (≠ T45), V40 (≠ T46), C41 (= C47), G45 (= G51), C46 (= C52), K50 (= K56), F111 (≠ R121), A112 (= A122), A135 (= A145), T136 (≠ V146), G137 (= G147), S155 (= S167), R269 (≠ N272), D306 (= D302), L312 (≠ G308), L313 (≠ I309), A314 (≠ L310), H315 (= H311), Y344 (≠ F343)
Sites not aligning to the query:
6cmzA 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
29% identity, 93% coverage: 14:444/462 of query aligns to 9:450/462 of 6cmzA
- active site: C42 (= C47), C47 (= C52), S50 (= S55), Y184 (≠ V187), E188 (= E191), H441 (= H435), E446 (= E440)
- binding flavin-adenine dinucleotide: G11 (= G16), G13 (= G18), P14 (≠ S19), E34 (≠ D39), R35 (≠ S40), G40 (≠ T45), T41 (= T46), C42 (= C47), G46 (= G51), C47 (= C52), K51 (= K56), E116 (≠ R121), A117 (= A122), T145 (≠ V146), G146 (= G147), V180 (≠ I183), G181 (= G184), Y184 (≠ V187), I185 (= I188), E204 (≠ D207), V268 (≠ L267), R270 (= R269), R273 (≠ N272), F277 (≠ R276), R289 (≠ V288), G308 (= G301), D309 (= D302), M315 (≠ G308), L316 (≠ I309), A317 (≠ L310), H318 (= H311)
- binding flavin mononucleotide: L152 (≠ V152), P153 (= P153)
6cmzB 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
29% identity, 93% coverage: 14:444/462 of query aligns to 9:450/459 of 6cmzB
- active site: C42 (= C47), C47 (= C52), S50 (= S55), Y184 (≠ V187), E188 (= E191), H441 (= H435), E446 (= E440)
- binding adenosine-5'-diphosphate: V150 (≠ I151), L152 (≠ V152), G181 (= G184), G183 (= G186), A205 (= A208), V268 (≠ L267), G269 (= G268)
- binding flavin-adenine dinucleotide: G11 (= G16), G13 (= G18), P14 (≠ S19), E34 (≠ D39), R35 (≠ S40), T41 (= T46), C42 (= C47), G46 (= G51), C47 (= C52), K51 (= K56), E116 (≠ R121), A117 (= A122), T145 (≠ V146), G146 (= G147), S164 (= S167), Y184 (≠ V187), I185 (= I188), R270 (= R269), F277 (≠ R276), G308 (= G301), D309 (= D302), M315 (≠ G308), L316 (≠ I309), A317 (≠ L310), H318 (= H311)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
27% identity, 94% coverage: 8:443/462 of query aligns to 3:459/478 of P14218
- 34:49 (vs. 33:47, 44% identical) binding FAD
- C49 (= C47) modified: Disulfide link with 54, Redox-active
- C54 (= C52) modified: Disulfide link with 49, Redox-active
- K58 (= K56) binding FAD
- G122 (= G128) binding FAD
- D319 (= D302) binding FAD
- A327 (≠ L310) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
27% identity, 94% coverage: 8:443/462 of query aligns to 1:457/472 of 5u8vA
- active site: P12 (≠ S19), L43 (= L43), C47 (= C47), C52 (= C52), S55 (= S55), G81 (≠ C80), V82 (≠ L81), V189 (= V187), E193 (= E191), S329 (≠ N314), F447 (≠ Y433), H449 (= H435), E454 (= E440)
- binding flavin-adenine dinucleotide: I8 (= I15), G11 (= G18), P12 (≠ S19), G13 (≠ A20), E32 (= E33), G45 (≠ T45), T46 (= T46), C47 (= C47), G51 (= G51), C52 (= C52), K56 (= K56), H119 (≠ D127), G120 (= G128), A148 (= A145), S149 (≠ V146), G150 (= G147), S169 (= S167), I190 (= I188), R277 (= R269), G316 (= G301), D317 (= D302), M323 (≠ G308), L324 (≠ I309), A325 (≠ L310), H326 (= H311), H449 (= H435), P450 (= P436)
- binding nicotinamide-adenine-dinucleotide: I185 (= I183), G186 (= G184), G188 (= G186), V189 (= V187), I190 (= I188), L208 (≠ F206), E209 (≠ D207), A210 (= A208), V243 (= V240), V275 (≠ L267), G276 (= G268)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
28% identity, 94% coverage: 8:443/462 of query aligns to 5:461/477 of 5u8uD
- active site: P16 (≠ S19), L47 (= L43), C51 (= C47), C56 (= C52), S59 (= S55), G85 (≠ C80), V86 (≠ L81), V193 (= V187), E197 (= E191), S333 (≠ N314), F451 (≠ Y433), H453 (= H435), E458 (= E440)
- binding flavin-adenine dinucleotide: I12 (= I15), G15 (= G18), P16 (≠ S19), G17 (≠ A20), E36 (= E33), K37 (≠ D34), G49 (≠ T45), T50 (= T46), C51 (= C47), G55 (= G51), C56 (= C52), K60 (= K56), H123 (≠ R121), G124 (≠ A122), A152 (= A145), S153 (≠ V146), G154 (= G147), I194 (= I188), R281 (= R269), G320 (= G301), D321 (= D302), M327 (≠ G308), L328 (≠ I309), A329 (≠ L310), H330 (= H311), H453 (= H435), P454 (= P436)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
28% identity, 94% coverage: 8:443/462 of query aligns to 2:458/473 of 5u8wA
- active site: P13 (≠ S19), L44 (= L43), C48 (= C47), C53 (= C52), S56 (= S55), G82 (≠ C80), V83 (≠ L81), V190 (= V187), E194 (= E191), S330 (≠ N314), F448 (≠ Y433), H450 (= H435), E455 (= E440)
- binding flavin-adenine dinucleotide: I9 (= I15), G12 (= G18), P13 (≠ S19), G14 (≠ A20), E33 (= E33), K34 (≠ D34), G46 (≠ T45), T47 (= T46), C48 (= C47), G52 (= G51), C53 (= C52), K57 (= K56), H120 (≠ R121), G121 (≠ A122), A149 (= A145), S150 (≠ V146), G151 (= G147), S170 (= S167), G317 (= G301), D318 (= D302), M324 (≠ G308), L325 (≠ I309), A326 (≠ L310), H327 (= H311), Y357 (≠ F343), H450 (= H435), P451 (= P436)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I183), G189 (= G186), V190 (= V187), I191 (= I188), E194 (= E191), E210 (≠ D207), A211 (= A208), L212 (≠ Q209), A275 (≠ T266), V276 (≠ L267), G277 (= G268), R278 (= R269), M324 (≠ G308), L325 (≠ I309), V355 (≠ I341), Y357 (≠ F343)
Sites not aligning to the query:
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
29% identity, 93% coverage: 14:444/462 of query aligns to 6:443/452 of 2eq7A
- active site: P11 (≠ S19), L36 (= L43), C40 (= C47), C45 (= C52), S48 (= S55), G72 (≠ S73), V73 (≠ L74), V177 (= V187), E181 (= E191), S314 (≠ N314), H432 (≠ Y433), H434 (= H435), E439 (= E440)
- binding flavin-adenine dinucleotide: G10 (= G18), P11 (≠ S19), G12 (≠ A20), E31 (≠ D39), K32 (≠ S40), G38 (≠ T45), T39 (= T46), C40 (= C47), R42 (= R49), G44 (= G51), C45 (= C52), K49 (= K56), T110 (≠ D114), A111 (≠ Q115), T137 (≠ V146), G138 (= G147), S157 (= S167), I178 (= I188), R262 (= R269), Y265 (≠ N272), D302 (= D302), M308 (≠ G308), L309 (≠ I309), A310 (≠ L310), H311 (= H311), Y341 (≠ F343)
- binding nicotinamide-adenine-dinucleotide: W146 (= W156), G174 (= G184), G176 (= G186), V177 (= V187), I178 (= I188), E197 (≠ D207), Y198 (≠ A208), V231 (vs. gap), V260 (≠ L267), G261 (= G268), R262 (= R269), M308 (≠ G308), L309 (≠ I309), V339 (≠ I341)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
29% identity, 93% coverage: 14:444/462 of query aligns to 6:443/455 of 2yquB
- active site: P11 (≠ S19), L36 (= L43), C40 (= C47), C45 (= C52), S48 (= S55), G72 (≠ S73), V73 (≠ L74), V177 (= V187), E181 (= E191), S314 (≠ N314), H432 (≠ Y433), H434 (= H435), E439 (= E440)
- binding carbonate ion: A310 (≠ L310), S314 (≠ N314), S423 (≠ T424), D426 (= D427)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), P11 (≠ S19), G12 (≠ A20), E31 (≠ D39), K32 (≠ S40), G38 (≠ T45), T39 (= T46), C40 (= C47), R42 (= R49), G44 (= G51), C45 (= C52), K49 (= K56), T110 (≠ D114), A111 (≠ Q115), T137 (≠ V146), G138 (= G147), I178 (= I188), Y265 (≠ N272), G301 (= G301), D302 (= D302), M308 (≠ G308), L309 (≠ I309), A310 (≠ L310), H311 (= H311)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
29% identity, 93% coverage: 14:444/462 of query aligns to 6:443/455 of 2yquA
- active site: P11 (≠ S19), L36 (= L43), C40 (= C47), C45 (= C52), S48 (= S55), G72 (≠ S73), V73 (≠ L74), V177 (= V187), E181 (= E191), S314 (≠ N314), H432 (≠ Y433), H434 (= H435), E439 (= E440)
- binding flavin-adenine dinucleotide: G8 (= G16), G10 (= G18), P11 (≠ S19), G12 (≠ A20), E31 (≠ D39), K32 (≠ S40), G38 (≠ T45), T39 (= T46), C40 (= C47), R42 (= R49), G44 (= G51), C45 (= C52), K49 (= K56), T110 (≠ D114), A111 (≠ Q115), T137 (≠ V146), G138 (= G147), S157 (= S167), I178 (= I188), Y265 (≠ N272), G301 (= G301), D302 (= D302), M308 (≠ G308), L309 (≠ I309), A310 (≠ L310)
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
26% identity, 93% coverage: 14:443/462 of query aligns to 8:447/454 of 5x1yB
- active site: A13 (≠ S19), V37 (≠ L43), C41 (= C47), C46 (= C52), S49 (= S55), A74 (≠ C80), G75 (≠ P82), Y178 (≠ V187), E182 (= E191), A318 (≠ N314), A437 (≠ Y433), Y439 (≠ H435), E444 (= E440)
- binding flavin-adenine dinucleotide: I9 (= I15), G12 (= G18), I32 (≠ V38), E33 (≠ D39), R34 (≠ S40), G39 (≠ T45), T40 (= T46), C41 (= C47), G45 (= G51), C46 (= C52), K50 (= K56), A114 (= A122), T138 (≠ V146), G139 (= G147), Y178 (≠ V187), R266 (= R269), G305 (= G301), D306 (= D302), F313 (≠ I309), V314 (≠ L310), A317 (= A313)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
26% identity, 93% coverage: 14:443/462 of query aligns to 89:528/546 of D9J041
- C122 (= C47) modified: Disulfide link with 127, Redox-active
- C127 (= C52) modified: Disulfide link with 122, Redox-active
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)
26% identity, 90% coverage: 41:454/462 of query aligns to 70:496/501 of P31023
- C76 (= C47) modified: Disulfide link with 81, Redox-active
- C81 (= C52) modified: Disulfide link with 76, Redox-active
- G149 (≠ A122) binding FAD
- D348 (vs. gap) binding FAD
- MLAH 354:357 (≠ --LH 310:311) binding FAD
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
- 67:76 binding FAD
Query Sequence
>WP_013835779.1 NCBI__GCF_000214825.1:WP_013835779.1
MQAHPKIRKVKYAIIGAGSAGLTAWSEIKKHTEDYILVDSGPLGTTCARVGCMPSKALIH
IAEHYQAWQNAESLGINLPCLPELDEAKVMQRVRRFRDRFTSGLIASTTGGLTDQHFISG
RAKVYPDGKLVVADKMFEAERIIVAVGSTPIVPADWQKELGELALTSDDVFELETLPKRL
AVIGLGVIGLELGQALSKLGVEVIGFDAQAQIGGLQDSYCNEFMLEQIQKHFPIHINQQV
VPFRDRNQVKITYQDSDWVGDKVLLTLGRRPNDDWRTPELQGLAIDPVTLQLGDLPIFVA
GDASGFHGILHEANREGKTAAQNAIHYTHLRGSDYLCPLAIVFSDPQIARIGCEYNELDK
NTTLIGSFDLNCNNGRAIVMDQDYGRMRLYADRATGRLLGGELAMPNAEHLGHLLAWSVQ
MGLTLQDLSTMPYYHPVLEEALQNVIDAMLAEYNALKGLTKN
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