SitesBLAST
Comparing Dsui_1576 FitnessBrowser__PS:Dsui_1576 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)
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)
63% identity, 80% coverage: 115:581/581 of query aligns to 4:472/474 of P0A9P0
- K220 (= K332) 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)
63% identity, 80% coverage: 115:581/581 of query aligns to 3:471/471 of 4jdrA
- active site: P15 (= P127), L40 (= L152), C44 (= C156), C49 (= C161), S52 (= S164), E77 (≠ A189), P78 (= P190), I184 (= I297), E188 (= E301), V324 (= V434), H442 (= H552), H444 (= H554), E449 (= E559), N467 (≠ P577), P468 (≠ M578)
- binding flavin-adenine dinucleotide: G12 (= G124), G14 (= G126), P15 (= P127), A16 (≠ G128), E35 (= E147), R36 (= R148), Y37 (= Y149), V43 (= V155), C44 (= C156), G48 (= G160), C49 (= C161), K53 (= K165), L115 (≠ V227), G116 (= G228), A144 (= A257), G145 (= G258), I185 (= I298), G311 (= G421), D312 (= D422), M318 (= M428), L319 (= L429), A320 (= A430), H321 (= H431)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
67% identity, 81% coverage: 112:580/581 of query aligns to 1:482/482 of 1bhyA
- active site: L41 (= L152), C45 (= C156), C50 (= C161), S53 (= S164), I195 (= I297), E199 (= E301), H454 (= H552), H456 (= H554), E461 (= E559), P479 (= P577), Q480 (≠ M578)
- binding flavin-adenine dinucleotide: L12 (= L123), P16 (= P127), G17 (= G128), E36 (= E147), R37 (= R148), Y38 (= Y149), G43 (= G154), V44 (= V155), C45 (= C156), G49 (= G160), C50 (= C161), K54 (= K165), D116 (≠ V227), G117 (= G228), Y135 (vs. gap), A156 (= A257), G157 (= G258), D324 (= D422), L331 (= L429), A332 (= A430)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 78% coverage: 116:571/581 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 147:156, 60% identical) binding
- K56 (= K165) binding
- D314 (= D422) binding
- A322 (= A430) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 78% coverage: 116:568/581 of query aligns to 2:454/455 of 1ebdA
- active site: P13 (= P127), L37 (= L152), C41 (= C156), C46 (= C161), S49 (= S164), N74 (≠ A189), V75 (≠ P190), Y180 (≠ I297), E184 (= E301), S320 (≠ V434), H438 (= H552), H440 (= H554), E445 (= E559)
- binding flavin-adenine dinucleotide: G10 (= G124), G12 (= G126), P13 (= P127), V32 (= V146), E33 (= E147), K34 (≠ R148), G39 (= G154), V40 (= V155), C41 (= C156), G45 (= G160), C46 (= C161), K50 (= K165), E112 (≠ V227), A113 (≠ G228), T141 (≠ A257), G142 (= G258), Y180 (≠ I297), I181 (= I298), R268 (= R382), D308 (= D422), A314 (≠ M428), L315 (= L429), A316 (= A430)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
44% identity, 80% coverage: 119:581/581 of query aligns to 6:478/478 of P14218
- 34:49 (vs. 147:156, 38% identical) binding
- C49 (= C156) modified: Disulfide link with 54, Redox-active
- C54 (= C161) modified: Disulfide link with 49, Redox-active
- K58 (= K165) binding
- G122 (= G228) binding
- D319 (= D422) binding
- A327 (= A430) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
44% identity, 78% coverage: 119:570/581 of query aligns to 5:466/473 of 5u8wA
- active site: P13 (= P127), L44 (= L152), C48 (= C156), C53 (= C161), S56 (= S164), G82 (≠ A189), V83 (≠ P190), V190 (≠ I297), E194 (= E301), S330 (≠ V434), F448 (≠ H552), H450 (= H554), E455 (= E559)
- binding flavin-adenine dinucleotide: I9 (≠ L123), G12 (= G126), P13 (= P127), G14 (= G128), E33 (= E147), K34 (≠ R148), G46 (= G154), T47 (≠ V155), C48 (= C156), G52 (= G160), C53 (= C161), K57 (= K165), H120 (≠ V227), G121 (= G228), A149 (= A256), S150 (≠ A257), G151 (= G258), S170 (= S277), G317 (= G421), D318 (= D422), M324 (= M428), L325 (= L429), A326 (= A430), H327 (= H431), Y357 (= Y461), H450 (= H554), P451 (= P555)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I293), G189 (= G296), V190 (≠ I297), I191 (= I298), E194 (= E301), E210 (= E317), A211 (≠ L318), L212 (≠ G319), A275 (= A379), V276 (= V380), G277 (= G381), R278 (= R382), M324 (= M428), L325 (= L429), V355 (= V459), Y357 (= Y461)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
44% identity, 78% coverage: 119:570/581 of query aligns to 4:465/472 of 5u8vA
- active site: P12 (= P127), L43 (= L152), C47 (= C156), C52 (= C161), S55 (= S164), G81 (≠ A189), V82 (≠ P190), V189 (≠ I297), E193 (= E301), S329 (≠ V434), F447 (≠ H552), H449 (= H554), E454 (= E559)
- binding flavin-adenine dinucleotide: I8 (≠ L123), G11 (= G126), P12 (= P127), G13 (= G128), E32 (= E147), G45 (= G154), T46 (≠ V155), C47 (= C156), G51 (= G160), C52 (= C161), K56 (= K165), H119 (≠ V227), G120 (= G228), A148 (= A256), S149 (≠ A257), G150 (= G258), S169 (= S277), I190 (= I298), R277 (= R382), G316 (= G421), D317 (= D422), M323 (= M428), L324 (= L429), A325 (= A430), H326 (= H431), H449 (= H554), P450 (= P555)
- binding nicotinamide-adenine-dinucleotide: I185 (= I293), G186 (= G294), G188 (= G296), V189 (≠ I297), I190 (= I298), L208 (≠ V316), E209 (= E317), A210 (≠ L318), V243 (= V351), V275 (= V380), G276 (= G381)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
44% identity, 78% coverage: 119:570/581 of query aligns to 8:469/477 of 5u8uD
- active site: P16 (= P127), L47 (= L152), C51 (= C156), C56 (= C161), S59 (= S164), G85 (≠ A189), V86 (≠ P190), V193 (≠ I297), E197 (= E301), S333 (≠ V434), F451 (≠ H552), H453 (= H554), E458 (= E559)
- binding flavin-adenine dinucleotide: I12 (≠ L123), G15 (= G126), P16 (= P127), G17 (= G128), E36 (= E147), K37 (≠ R148), G49 (= G154), T50 (≠ V155), C51 (= C156), G55 (= G160), C56 (= C161), K60 (= K165), H123 (≠ V227), G124 (= G228), A152 (= A256), S153 (≠ A257), G154 (= G258), I194 (= I298), R281 (= R382), G320 (= G421), D321 (= D422), M327 (= M428), L328 (= L429), A329 (= A430), H330 (= H431), H453 (= H554), P454 (= P555)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
43% identity, 78% coverage: 117:570/581 of query aligns to 6:464/470 of 6uziC
- active site: C45 (= C156), C50 (= C161), S53 (= S164), V187 (≠ I297), E191 (= E301), H448 (= H554), E453 (= E559)
- binding flavin-adenine dinucleotide: I12 (≠ L123), G13 (= G124), G15 (= G126), P16 (= P127), G17 (= G128), E36 (= E147), K37 (≠ R148), G43 (= G154), T44 (≠ V155), C45 (= C156), G49 (= G160), C50 (= C161), S53 (= S164), K54 (= K165), V117 (= V227), G118 (= G228), T147 (≠ A257), G148 (= G258), I188 (= I298), R276 (= R382), D316 (= D422), M322 (= M428), L323 (= L429), A324 (= A430)
- binding zinc ion: H448 (= H554), E453 (= E559)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
43% identity, 80% coverage: 119:580/581 of query aligns to 6:477/477 of P18925
- 34:49 (vs. 147:156, 38% identical) binding
- C49 (= C156) modified: Disulfide link with 54, Redox-active
- C54 (= C161) modified: Disulfide link with 49, Redox-active
- K58 (= K165) binding
- D319 (= D422) binding
- A327 (= A430) binding
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)
44% identity, 77% coverage: 119:565/581 of query aligns to 5:461/472 of 3ladA
- active site: L44 (= L152), C48 (= C156), C53 (= C161), S56 (= S164), V190 (≠ I297), E194 (= E301), F448 (≠ H552), H450 (= H554), E455 (= E559)
- binding flavin-adenine dinucleotide: I9 (≠ L123), G10 (= G124), G12 (= G126), P13 (= P127), E33 (= E147), K34 (≠ R148), G46 (= G154), T47 (≠ V155), C48 (= C156), G52 (= G160), C53 (= C161), H120 (≠ V227), G121 (= G228), A149 (= A256), S150 (≠ A257), G151 (= G258), I191 (= I298), R278 (= R382), D318 (= D422), L325 (= L429), A326 (= A430)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
42% identity, 78% coverage: 119:570/581 of query aligns to 6:467/475 of 6awaA
- active site: L45 (= L152), C49 (= C156), C54 (= C161), S57 (= S164), V191 (≠ I297), E195 (= E301), F449 (≠ H552), H451 (= H554), E456 (= E559)
- binding adenosine monophosphate: I187 (= I293), E211 (= E317), A212 (≠ L318), L213 (≠ G319), V245 (= V351), V277 (= V380)
- binding flavin-adenine dinucleotide: I10 (≠ L123), G13 (= G126), P14 (= P127), G15 (= G128), E34 (= E147), K35 (≠ R148), T48 (≠ V155), C49 (= C156), G53 (= G160), C54 (= C161), K58 (= K165), H121 (≠ V227), G122 (= G228), S151 (≠ A257), G152 (= G258), I192 (= I298), R279 (= R382), G318 (= G421), D319 (= D422), M325 (= M428), L326 (= L429), A327 (= A430), Y358 (= Y461)
Sites not aligning to the query:
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
41% identity, 78% coverage: 110:564/581 of query aligns to 5:470/482 of 6hg8B
- active site: C53 (= C156), C58 (= C161), S61 (= S164), V196 (≠ I297), E200 (= E301), H460 (= H554), E465 (= E559)
- binding flavin-adenine dinucleotide: I20 (≠ L123), G23 (= G126), P24 (= P127), G25 (= G128), E44 (= E147), K45 (≠ R148), N46 (≠ Y149), G51 (= G154), T52 (≠ V155), C53 (= C156), G57 (= G160), C58 (= C161), K62 (= K165), Y126 (≠ V227), G127 (= G228), T156 (≠ A257), G157 (= G258), I197 (= I298), R288 (= R382), F291 (≠ N385), G327 (= G421), D328 (= D422), M334 (= M428), L335 (= L429), A336 (= A430), H337 (= H431)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
40% identity, 77% coverage: 119:565/581 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ L152), C39 (= C156), C44 (= C161), S47 (= S164), V183 (≠ I297), E187 (= E301), H443 (= H552), H445 (= H554), E450 (= E559)
- binding flavin-adenine dinucleotide: I6 (≠ L123), G7 (= G124), G9 (= G126), P10 (= P127), G11 (= G128), E30 (= E147), K31 (≠ R148), G37 (= G154), T38 (≠ V155), C39 (= C156), G43 (= G160), C44 (= C161), K48 (= K165), T111 (≠ V227), G112 (= G228), A140 (= A256), T141 (≠ A257), G142 (= G258), I184 (= I298), R273 (= R382), G312 (= G421), D313 (= D422), M319 (= M428), L320 (= L429), A321 (= A430), H322 (= H431)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
41% identity, 77% coverage: 116:561/581 of query aligns to 3:457/472 of 1zmdA
- active site: L39 (= L152), C43 (= C156), C48 (= C161), S51 (= S164), V186 (≠ I297), E190 (= E301), H448 (= H552), H450 (= H554), E455 (= E559)
- binding flavin-adenine dinucleotide: I10 (≠ L123), G11 (= G124), G13 (= G126), P14 (= P127), G15 (= G128), E34 (= E147), K35 (≠ R148), N36 (≠ Y149), G41 (= G154), T42 (≠ V155), C43 (= C156), G47 (= G160), C48 (= C161), K52 (= K165), Y116 (≠ V227), G117 (= G228), T146 (≠ A257), G147 (= G258), S166 (= S277), R278 (= R382), F281 (≠ N385), G317 (= G421), D318 (= D422), M324 (= M428), L325 (= L429), A326 (= A430), H327 (= H431)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I293), G183 (= G294), G185 (= G296), V186 (≠ I297), I187 (= I298), E190 (= E301), E206 (= E317), F207 (vs. gap), L208 (= L318), I276 (≠ V380), G277 (= G381), R278 (= R382), M324 (= M428), L325 (= L429), V355 (= V459), Y357 (= Y461)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
41% identity, 77% coverage: 116:561/581 of query aligns to 3:457/472 of 1zmcA
- active site: L39 (= L152), C43 (= C156), C48 (= C161), S51 (= S164), V186 (≠ I297), E190 (= E301), H448 (= H552), H450 (= H554), E455 (= E559)
- binding flavin-adenine dinucleotide: I10 (≠ L123), G11 (= G124), G13 (= G126), P14 (= P127), G15 (= G128), E34 (= E147), K35 (≠ R148), N36 (≠ Y149), G41 (= G154), T42 (≠ V155), C43 (= C156), G47 (= G160), C48 (= C161), K52 (= K165), Y116 (≠ V227), G117 (= G228), T146 (≠ A257), G147 (= G258), S166 (= S277), I187 (= I298), F281 (≠ N385), G317 (= G421), D318 (= D422), M324 (= M428), L325 (= L429), A326 (= A430), H327 (= H431)
- binding nicotinamide-adenine-dinucleotide: G183 (= G294), G185 (= G296), V205 (= V316), E206 (= E317), F207 (vs. gap), L208 (= L318), K240 (≠ G350), V241 (= V351), I276 (≠ V380), G277 (= G381), R278 (= R382), R297 (= R401), M324 (= M428)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
41% identity, 77% coverage: 116:561/581 of query aligns to 40:494/509 of P09622
- 71:80 (vs. 147:156, 60% identical) binding
- K72 (≠ R148) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K165) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ Q178) to T: in dbSNP:rs1130477
- G154 (= G228) binding
- TGS 183:185 (≠ AGS 257:259) binding
- 220:227 (vs. 294:301, 63% identical) binding
- E243 (= E317) binding
- V278 (= V351) binding
- G314 (= G381) binding
- D355 (= D422) binding
- MLAH 361:364 (= MLAH 428:431) binding
- E375 (= E442) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A450) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H515) 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 (= E533) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M540) 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 (= D546) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ K549) 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 (= H552) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P555) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ C558) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E559) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
Sites not aligning to the query:
- 495 R → G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
42% identity, 74% coverage: 132:561/581 of query aligns to 17:451/465 of 2qaeA
- active site: L37 (= L152), C41 (= C156), C46 (= C161), S49 (= S164), V184 (≠ I297), E188 (= E301), H442 (= H552), H444 (= H554), E449 (= E559)
- binding flavin-adenine dinucleotide: E32 (= E147), K33 (≠ R148), R34 (≠ Y149), G39 (= G154), T40 (≠ V155), C41 (= C156), G45 (= G160), C46 (= C161), K50 (= K165), E114 (≠ V227), G115 (= G228), T144 (≠ A257), G145 (= G258), S164 (= S277), I185 (= I298), F274 (≠ N385), G310 (= G421), D311 (= D422), M318 (= M428), L319 (= L429), A320 (= A430), H321 (= H431)
Sites not aligning to the query:
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)
40% identity, 78% coverage: 113:565/581 of query aligns to 34:491/501 of P31023
- 67:76 (vs. 147:156, 50% identical) binding
- C76 (= C156) modified: Disulfide link with 81, Redox-active
- C81 (= C161) modified: Disulfide link with 76, Redox-active
- G149 (= G228) binding
- D348 (= D422) binding
- MLAH 354:357 (= MLAH 428:431) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
Query Sequence
>Dsui_1576 FitnessBrowser__PS:Dsui_1576
MSQLVEVKVPDIGDFKDVPVIEVFVKVGDTVKVEDPLVSLESDKATMDVPSSAAGVVKEI
KVKLGDKVAEGTVIVVVEAGAAAAAPAPQPAAPAAAPAPAAAPPPVAGSHGGGADVECDM
LVLGAGPGGYSAAFRSADLGLKTVLVERYPTLGGVCLNVGCIPSKALLHVAAVLEEAQHL
ADCGVTFAAPQVDVDKLRAHKEKVVGKLTGGLAGMAKGRKVQHVQGVGQFIDPHHIEVTA
ADGKKQVVKFKNAIIAAGSQPVALPFMPKDDPRVIDSTGALELRSVPKKMLVIGGGIIGL
EMATVYSALGTRITVVELGPGLMPGADRDLVKVWEKKNTQRFDRILLATGVTAAEAKAEG
IEVTYSTGEKEAFDLVLVAVGRTPNGKKIAADKAGVAVTDRGFINVDAQMRTNVPHIFAI
GDIVGQPMLAHKAVHEAHVAAEVAAGEKAAFDALQIPSVAYTHPEIAWAGKTEDQLKNDG
IKFEKAVFPWAASGRAIANGAEEGFTKLLFDAESHRLLGGGIVGMNAGDLIGEVCLAVEM
GCDAVDIGKTIHPHPTLCESIGMAAEVAHGSCTDLPPMKKK
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