SitesBLAST
Comparing WP_012852398.1 NCBI__GCF_000024385.1:WP_012852398.1 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
35% identity, 97% coverage: 4:458/467 of query aligns to 1:462/465 of 3urhB
- active site: Y35 (≠ I38), C39 (= C42), C44 (≠ T47), S47 (= S50), V183 (= V184), E187 (= E188), H443 (≠ F439), H445 (≠ Y441), E450 (= E446)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (= P13), G11 (= G14), E30 (≠ D33), K31 (≠ R34), G37 (= G40), T38 (≠ V41), C39 (= C42), G43 (= G46), C44 (≠ T47), K48 (= K51), T111 (= T114), G112 (≠ A115), A140 (= A143), T141 (= T144), G142 (= G145), I184 (= I185), R273 (= R269), G312 (= G308), D313 (= D309), M319 (≠ S315), L320 (= L316), A321 (= A317), H322 (≠ A318)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 4:458/467 of query aligns to 2:451/455 of 2yquB
- active site: P11 (= P13), L36 (≠ I38), C40 (= C42), C45 (≠ T47), S48 (= S50), G72 (≠ R74), V73 (= V75), V177 (= V184), E181 (= E188), S314 (≠ M321), H432 (≠ F439), H434 (≠ Y441), E439 (= E446)
- binding carbonate ion: A310 (= A317), S314 (≠ M321), S423 (≠ T430), D426 (≠ Y433)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (≠ D33), K32 (≠ R34), G38 (= G40), T39 (≠ V41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (≠ T47), K49 (= K51), T110 (= T114), A111 (= A115), T137 (= T144), G138 (= G145), I178 (= I185), Y265 (≠ M272), G301 (= G308), D302 (= D309), M308 (≠ S315), L309 (= L316), A310 (= A317), H311 (≠ A318)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 4:458/467 of query aligns to 2:451/455 of 2yquA
- active site: P11 (= P13), L36 (≠ I38), C40 (= C42), C45 (≠ T47), S48 (= S50), G72 (≠ R74), V73 (= V75), V177 (= V184), E181 (= E188), S314 (≠ M321), H432 (≠ F439), H434 (≠ Y441), E439 (= E446)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (≠ D33), K32 (≠ R34), G38 (= G40), T39 (≠ V41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (≠ T47), K49 (= K51), T110 (= T114), A111 (= A115), T137 (= T144), G138 (= G145), S157 (= S164), I178 (= I185), Y265 (≠ M272), G301 (= G308), D302 (= D309), M308 (≠ S315), L309 (= L316), A310 (= A317)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
36% identity, 97% coverage: 4:458/467 of query aligns to 2:451/452 of 2eq7A
- active site: P11 (= P13), L36 (≠ I38), C40 (= C42), C45 (≠ T47), S48 (= S50), G72 (≠ R74), V73 (= V75), V177 (= V184), E181 (= E188), S314 (≠ M321), H432 (≠ F439), H434 (≠ Y441), E439 (= E446)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (= P13), G12 (= G14), E31 (≠ D33), K32 (≠ R34), G38 (= G40), T39 (≠ V41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (≠ T47), K49 (= K51), T110 (= T114), A111 (= A115), T137 (= T144), G138 (= G145), S157 (= S164), I178 (= I185), R262 (= R269), Y265 (≠ M272), D302 (= D309), M308 (≠ S315), L309 (= L316), A310 (= A317), H311 (≠ A318), Y341 (= Y348)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ S153), G174 (= G181), G176 (= G183), V177 (= V184), I178 (= I185), E197 (= E204), Y198 (≠ R205), V231 (= V238), V260 (≠ A267), G261 (= G268), R262 (= R269), M308 (≠ S315), L309 (= L316), V339 (≠ G346)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
33% identity, 98% coverage: 1:458/467 of query aligns to 4:465/470 of 6uziC
- active site: C45 (= C42), C50 (≠ T47), S53 (= S50), V187 (= V184), E191 (= E188), H448 (≠ Y441), E453 (= E446)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (= P13), G17 (= G14), E36 (≠ D33), K37 (≠ R34), G43 (= G40), T44 (≠ V41), C45 (= C42), G49 (= G46), C50 (≠ T47), S53 (= S50), K54 (= K51), V117 (≠ T114), G118 (≠ A115), T147 (= T144), G148 (= G145), I188 (= I185), R276 (= R269), D316 (= D309), M322 (≠ S315), L323 (= L316), A324 (= A317)
- binding zinc ion: H448 (≠ Y441), E453 (= E446)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
35% identity, 97% coverage: 2:453/467 of query aligns to 3:463/478 of P14218
- 34:49 (vs. 33:42, 19% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (≠ T47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- G122 (≠ A115) binding FAD
- D319 (= D309) binding FAD
- A327 (= A317) 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)
35% identity, 97% coverage: 2:453/467 of query aligns to 1:461/472 of 5u8vA
- active site: P12 (= P13), L43 (≠ I38), C47 (= C42), C52 (≠ T47), S55 (= S50), G81 (≠ K76), V82 (≠ E77), V189 (= V184), E193 (= E188), S329 (≠ M321), F447 (= F439), H449 (≠ Y441), E454 (= E446)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), E32 (≠ D33), G45 (= G40), T46 (≠ V41), C47 (= C42), G51 (= G46), C52 (≠ T47), K56 (= K51), H119 (≠ T114), G120 (≠ A115), A148 (= A143), S149 (≠ T144), G150 (= G145), S169 (= S164), I190 (= I185), R277 (= R269), G316 (= G308), D317 (= D309), M323 (≠ S315), L324 (= L316), A325 (= A317), H326 (≠ A318), H449 (≠ Y441), P450 (= P442)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V180), G186 (= G181), G188 (= G183), V189 (= V184), I190 (= I185), L208 (≠ V203), E209 (= E204), A210 (≠ R205), V243 (= V238), V275 (≠ A267), G276 (= G268)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
35% identity, 97% coverage: 2:453/467 of query aligns to 2:462/473 of 5u8wA
- active site: P13 (= P13), L44 (≠ I38), C48 (= C42), C53 (≠ T47), S56 (= S50), G82 (≠ K76), V83 (≠ E77), V190 (= V184), E194 (= E188), S330 (≠ M321), F448 (= F439), H450 (≠ Y441), E455 (= E446)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), P13 (= P13), G14 (= G14), E33 (≠ D33), K34 (≠ R34), G46 (= G40), T47 (≠ V41), C48 (= C42), G52 (= G46), C53 (≠ T47), K57 (= K51), H120 (≠ T114), G121 (≠ A115), A149 (= A143), S150 (≠ T144), G151 (= G145), S170 (= S164), G317 (= G308), D318 (= D309), M324 (≠ S315), L325 (= L316), A326 (= A317), H327 (≠ A318), Y357 (= Y348), H450 (≠ Y441), P451 (= P442)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V180), G189 (= G183), V190 (= V184), I191 (= I185), E194 (= E188), E210 (= E204), A211 (≠ R205), L212 (≠ R206), A275 (≠ S266), V276 (≠ A267), G277 (= G268), R278 (= R269), M324 (≠ S315), L325 (= L316), V355 (≠ G346), Y357 (= Y348)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
35% identity, 97% coverage: 2:453/467 of query aligns to 5:465/477 of 5u8uD
- active site: P16 (= P13), L47 (≠ I38), C51 (= C42), C56 (≠ T47), S59 (= S50), G85 (≠ K76), V86 (≠ E77), V193 (= V184), E197 (= E188), S333 (≠ M321), F451 (= F439), H453 (≠ Y441), E458 (= E446)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (= P13), G17 (= G14), E36 (≠ D33), K37 (≠ R34), G49 (= G40), T50 (≠ V41), C51 (= C42), G55 (= G46), C56 (≠ T47), K60 (= K51), H123 (≠ T114), G124 (≠ A115), A152 (= A143), S153 (≠ T144), G154 (= G145), I194 (= I185), R281 (= R269), G320 (= G308), D321 (= D309), M327 (≠ S315), L328 (= L316), A329 (= A317), H330 (≠ A318), H453 (≠ Y441), P454 (= P442)
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.
33% identity, 97% coverage: 2:453/467 of query aligns to 3:463/475 of 6awaA
- active site: L45 (≠ I38), C49 (= C42), C54 (≠ T47), S57 (= S50), V191 (= V184), E195 (= E188), F449 (= F439), H451 (≠ Y441), E456 (= E446)
- binding adenosine monophosphate: I187 (≠ V180), E211 (= E204), A212 (≠ R205), L213 (≠ R206), V245 (= V238), V277 (≠ A267)
- binding flavin-adenine dinucleotide: I10 (= I9), G13 (= G12), P14 (= P13), G15 (= G14), E34 (≠ D33), K35 (≠ R34), T48 (≠ V41), C49 (= C42), G53 (= G46), C54 (≠ T47), K58 (= K51), H121 (≠ T114), G122 (≠ A115), S151 (≠ T144), G152 (= G145), I192 (= I185), R279 (= R269), G318 (= G308), D319 (= D309), M325 (≠ S315), L326 (= L316), A327 (= A317), Y358 (= Y348)
Sites not aligning to the query:
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
33% identity, 97% coverage: 2:453/467 of query aligns to 3:463/477 of P18925
- 34:49 (vs. 33:42, 19% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (≠ T47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- D319 (= D309) binding FAD
- A327 (= A317) binding FAD
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, 97% coverage: 3:455/467 of query aligns to 41:501/509 of P09622
- 71:80 (vs. 33:42, 30% identical) binding FAD
- K72 (≠ R34) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K51) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ R66) to T: in dbSNP:rs1130477
- G154 (≠ A115) binding FAD
- TGS 183:185 (≠ TGT 144:146) binding FAD
- 220:227 (vs. 181:188, 88% identical) binding NAD(+)
- E243 (= E204) binding NAD(+)
- V278 (= V238) binding NAD(+)
- G314 (= G268) binding NAD(+)
- D355 (= D309) binding FAD
- MLAH 361:364 (≠ SLAA 315:318) binding FAD
- E375 (≠ H329) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H340) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ R402) 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 (≠ I420) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ C427) 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 (≠ Y433) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ D436) 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 (≠ F439) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P442) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ A445) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E446) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K449) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
Sites not aligning to the query:
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
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)
33% identity, 97% coverage: 2:453/467 of query aligns to 2:462/472 of 3ladA
- active site: L44 (≠ I38), C48 (= C42), C53 (≠ T47), S56 (= S50), V190 (= V184), E194 (= E188), F448 (= F439), H450 (≠ Y441), E455 (= E446)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (= P13), E33 (≠ D33), K34 (≠ R34), G46 (= G40), T47 (≠ V41), C48 (= C42), G52 (= G46), C53 (≠ T47), H120 (≠ T114), G121 (≠ A115), A149 (= A143), S150 (≠ T144), G151 (= G145), I191 (= I185), R278 (= R269), D318 (= D309), L325 (= L316), A326 (= A317)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
32% identity, 97% coverage: 3:455/467 of query aligns to 14:474/482 of 6hg8B
- active site: C53 (= C42), C58 (≠ T47), S61 (= S50), V196 (= V184), E200 (= E188), H460 (≠ Y441), E465 (= E446)
- binding flavin-adenine dinucleotide: I20 (= I9), G23 (= G12), P24 (= P13), G25 (= G14), E44 (≠ D33), K45 (≠ R34), N46 (≠ R35), G51 (= G40), T52 (≠ V41), C53 (= C42), G57 (= G46), C58 (≠ T47), K62 (= K51), Y126 (≠ T114), G127 (≠ A115), T156 (= T144), G157 (= G145), I197 (= I185), R288 (= R269), F291 (≠ M272), G327 (= G308), D328 (= D309), M334 (≠ S315), L335 (= L316), A336 (= A317), H337 (≠ A318)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
32% identity, 97% coverage: 3:455/467 of query aligns to 4:464/472 of 1zmdA
- active site: L39 (≠ I38), C43 (= C42), C48 (≠ T47), S51 (= S50), V186 (= V184), E190 (= E188), H448 (≠ F439), H450 (≠ Y441), E455 (= E446)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (≠ D33), K35 (≠ R34), N36 (≠ R35), G41 (= G40), T42 (≠ V41), C43 (= C42), G47 (= G46), C48 (≠ T47), K52 (= K51), Y116 (≠ T114), G117 (≠ A115), T146 (= T144), G147 (= G145), S166 (= S164), R278 (= R269), F281 (≠ M272), G317 (= G308), D318 (= D309), M324 (≠ S315), L325 (= L316), A326 (= A317), H327 (≠ A318)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V180), G183 (= G181), G185 (= G183), V186 (= V184), I187 (= I185), E190 (= E188), E206 (= E204), F207 (≠ R205), L208 (≠ R206), I276 (≠ A267), G277 (= G268), R278 (= R269), M324 (≠ S315), L325 (= L316), V355 (≠ G346), Y357 (= Y348)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
32% identity, 97% coverage: 3:455/467 of query aligns to 4:464/472 of 1zmcA
- active site: L39 (≠ I38), C43 (= C42), C48 (≠ T47), S51 (= S50), V186 (= V184), E190 (= E188), H448 (≠ F439), H450 (≠ Y441), E455 (= E446)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (≠ D33), K35 (≠ R34), N36 (≠ R35), G41 (= G40), T42 (≠ V41), C43 (= C42), G47 (= G46), C48 (≠ T47), K52 (= K51), Y116 (≠ T114), G117 (≠ A115), T146 (= T144), G147 (= G145), S166 (= S164), I187 (= I185), F281 (≠ M272), G317 (= G308), D318 (= D309), M324 (≠ S315), L325 (= L316), A326 (= A317), H327 (≠ A318)
- binding nicotinamide-adenine-dinucleotide: G183 (= G181), G185 (= G183), V205 (= V203), E206 (= E204), F207 (≠ R205), L208 (≠ R206), K240 (≠ N237), V241 (= V238), I276 (≠ A267), G277 (= G268), R278 (= R269), R297 (= R288), M324 (≠ S315)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
34% identity, 95% coverage: 5:446/467 of query aligns to 5:445/455 of 1ebdA
- active site: P13 (= P13), L37 (≠ M37), C41 (= C42), C46 (≠ T47), S49 (= S50), N74 (≠ R74), V75 (= V75), Y180 (≠ V184), E184 (= E188), S320 (≠ M321), H438 (≠ F439), H440 (≠ Y441), E445 (= E446)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), P13 (= P13), V32 (= V32), E33 (≠ D33), K34 (≠ R34), G39 (= G40), V40 (= V41), C41 (= C42), G45 (= G46), C46 (≠ T47), K50 (= K51), E112 (≠ T114), A113 (= A115), T141 (= T144), G142 (= G145), Y180 (≠ V184), I181 (= I185), R268 (= R269), D308 (= D309), A314 (≠ S315), L315 (= L316), A316 (= A317)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
34% identity, 95% coverage: 3:446/467 of query aligns to 5:451/470 of P11959
- 39:47 (vs. 33:42, 40% identical) binding FAD
- K56 (= K51) binding FAD
- D314 (= D309) binding FAD
- A322 (= A317) binding FAD
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
32% identity, 97% coverage: 2:453/467 of query aligns to 1:464/473 of 6aonA
- active site: P43 (≠ I38), C47 (= C42), C52 (≠ T47), S55 (= S50), V191 (= V184), E195 (= E188), H450 (≠ F439), H452 (≠ Y441), E457 (= E446)
- binding calcium ion: A218 (≠ E211), A220 (≠ C213), Q222 (≠ L215)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), D32 (= D33), A33 (≠ R34), W34 (≠ R35), G45 (= G40), T46 (≠ V41), C47 (= C42), G51 (= G46), C52 (≠ T47), K56 (= K51), K119 (≠ T114), G120 (≠ A115), T151 (= T144), G152 (= G145), N171 (≠ S164), I192 (= I185), R280 (= R269), Y283 (≠ M272), G319 (= G308), D320 (= D309), M326 (≠ S315), L327 (= L316), A328 (= A317), H329 (≠ A318)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
32% identity, 93% coverage: 18:453/467 of query aligns to 17:456/465 of 2qaeA
- active site: L37 (≠ I38), C41 (= C42), C46 (≠ T47), S49 (= S50), V184 (= V184), E188 (= E188), H442 (≠ F439), H444 (≠ Y441), E449 (= E446)
- binding flavin-adenine dinucleotide: E32 (≠ D33), K33 (≠ R34), R34 (= R35), G39 (= G40), T40 (≠ V41), C41 (= C42), G45 (= G46), C46 (≠ T47), K50 (= K51), E114 (≠ T114), G115 (≠ A115), T144 (= T144), G145 (= G145), S164 (= S164), I185 (= I185), F274 (≠ M272), G310 (= G308), D311 (= D309), M318 (≠ S315), L319 (= L316), A320 (= A317), H321 (≠ A318)
Sites not aligning to the query:
Query Sequence
>WP_012852398.1 NCBI__GCF_000024385.1:WP_012852398.1
MRDFDILVIGSGPGGQRAAIAAAKLGRRVAIVDRRDMIGGVCINTGTIPSKTLREAVLYL
TGLNQRELYGQSYRVKEEITVADLGMRTRHVVGREVDVIRSQLARNRVTVVTGTARFLDP
HTVEVTDGGGQRRELTADKIVIATGTRPARPASVEFDDETIIDSDGILRLKRIPDSMVVV
GAGVIGIEYASMFAALGTKVTVVERRERMLEFCDLEIVEALKYHLRDLAVTFRFGENVKA
VEKRPGGAITILESGKRIPADTVMYSAGRHGMTDDLGLEAAGLTADERGRIAVDDCYRTA
VPHIYAVGDVIGFPSLAATSMEQGRLAAHHACGEPAGGIHELQPIGIYTIPEISFVGHTE
DELTAAKIPFEVGVARYRELARGQIIGDSYGMLKLLVSPLDRSLLGVHVFGTGATELVHI
GQTVMGCGGTVDYLVDAVFNYPTLAESYKVAALDAMNKMRQIALLDE
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