SitesBLAST
Comparing WP_028486698.1 NCBI__GCF_000483485.1:WP_028486698.1 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)
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)
61% identity, 80% coverage: 122:592/592 of query aligns to 4:473/474 of P0A9P0
- K220 (= K339) 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)
61% identity, 79% coverage: 122:591/592 of query aligns to 3:471/471 of 4jdrA
- active site: P15 (= P134), L40 (≠ I159), C44 (= C163), C49 (= C168), S52 (= S171), E77 (= E196), P78 (= P197), I184 (= I304), E188 (= E308), V324 (= V444), H442 (= H562), H444 (= H564), E449 (= E569), N467 (≠ P587), P468 (= P588)
- binding flavin-adenine dinucleotide: G12 (= G131), G14 (= G133), P15 (= P134), A16 (≠ G135), E35 (= E154), R36 (= R155), Y37 (= Y156), V43 (= V162), C44 (= C163), G48 (= G167), C49 (= C168), K53 (= K172), L115 (≠ Y234), G116 (= G235), A144 (= A264), G145 (= G265), I185 (= I305), G311 (= G431), D312 (= D432), M318 (= M438), L319 (= L439), A320 (= A440), H321 (= H441)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
57% identity, 77% coverage: 137:591/592 of query aligns to 19:482/482 of 1bhyA
- active site: L41 (≠ I159), C45 (= C163), C50 (= C168), S53 (= S171), I195 (= I304), E199 (= E308), H454 (= H562), H456 (= H564), E461 (= E569), P479 (= P588), Q480 (≠ K589)
- binding flavin-adenine dinucleotide: E36 (= E154), R37 (= R155), Y38 (= Y156), G43 (= G161), V44 (= V162), C45 (= C163), G49 (= G167), C50 (= C168), K54 (= K172), D116 (≠ Y234), G117 (= G235), Y135 (vs. gap), A156 (= A264), G157 (= G265), D324 (= D432), L331 (= L439), A332 (= A440)
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)
46% identity, 78% coverage: 123:581/592 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 154:163, 60% identical) binding FAD
- K56 (= K172) binding FAD
- D314 (= D432) binding FAD
- A322 (= A440) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
46% identity, 77% coverage: 123:578/592 of query aligns to 2:454/455 of 1ebdA
- active site: P13 (= P134), L37 (≠ I159), C41 (= C163), C46 (= C168), S49 (= S171), N74 (≠ E196), V75 (≠ P197), Y180 (≠ I304), E184 (= E308), S320 (≠ V444), H438 (= H562), H440 (= H564), E445 (= E569)
- binding flavin-adenine dinucleotide: G10 (= G131), G12 (= G133), P13 (= P134), V32 (≠ I153), E33 (= E154), K34 (≠ R155), G39 (= G161), V40 (= V162), C41 (= C163), G45 (= G167), C46 (= C168), K50 (= K172), E112 (≠ Y234), A113 (≠ G235), T141 (≠ A264), G142 (= G265), Y180 (≠ I304), I181 (= I305), R268 (= R392), D308 (= D432), A314 (≠ M438), L315 (= L439), A316 (= A440)
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, 79% coverage: 124:591/592 of query aligns to 4:478/478 of P14218
- 34:49 (vs. 154:163, 31% identical) binding FAD
- C49 (= C163) modified: Disulfide link with 54, Redox-active
- C54 (= C168) modified: Disulfide link with 49, Redox-active
- K58 (= K172) binding FAD
- G122 (= G235) binding FAD
- D319 (= D432) binding FAD
- A327 (= A440) 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)
44% identity, 77% coverage: 124:580/592 of query aligns to 2:465/472 of 5u8vA
- active site: P12 (= P134), L43 (≠ I159), C47 (= C163), C52 (= C168), S55 (= S171), G81 (≠ E196), V82 (≠ P197), V189 (≠ I304), E193 (= E308), S329 (≠ V444), F447 (≠ H562), H449 (= H564), E454 (= E569)
- binding flavin-adenine dinucleotide: I8 (≠ L130), G11 (= G133), P12 (= P134), G13 (= G135), E32 (= E154), G45 (= G161), T46 (≠ V162), C47 (= C163), G51 (= G167), C52 (= C168), K56 (= K172), H119 (≠ Y234), G120 (= G235), A148 (= A263), S149 (≠ A264), G150 (= G265), S169 (= S284), I190 (= I305), R277 (= R392), G316 (= G431), D317 (= D432), M323 (= M438), L324 (= L439), A325 (= A440), H326 (= H441), H449 (= H564), P450 (= P565)
- binding nicotinamide-adenine-dinucleotide: I185 (= I300), G186 (= G301), G188 (= G303), V189 (≠ I304), I190 (= I305), L208 (≠ V323), E209 (= E324), A210 (≠ L325), V243 (= V358), V275 (= V390), G276 (= G391)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
44% identity, 77% coverage: 124:580/592 of query aligns to 3:466/473 of 5u8wA
- active site: P13 (= P134), L44 (≠ I159), C48 (= C163), C53 (= C168), S56 (= S171), G82 (≠ E196), V83 (≠ P197), V190 (≠ I304), E194 (= E308), S330 (≠ V444), F448 (≠ H562), H450 (= H564), E455 (= E569)
- binding flavin-adenine dinucleotide: I9 (≠ L130), G12 (= G133), P13 (= P134), G14 (= G135), E33 (= E154), K34 (≠ R155), G46 (= G161), T47 (≠ V162), C48 (= C163), G52 (= G167), C53 (= C168), K57 (= K172), H120 (≠ Y234), G121 (= G235), A149 (= A263), S150 (≠ A264), G151 (= G265), S170 (= S284), G317 (= G431), D318 (= D432), M324 (= M438), L325 (= L439), A326 (= A440), H327 (= H441), Y357 (= Y471), H450 (= H564), P451 (= P565)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I300), G189 (= G303), V190 (≠ I304), I191 (= I305), E194 (= E308), E210 (= E324), A211 (≠ L325), L212 (≠ G326), A275 (= A389), V276 (= V390), G277 (= G391), R278 (= R392), M324 (= M438), L325 (= L439), V355 (= V469), Y357 (= Y471)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
44% identity, 77% coverage: 124:580/592 of query aligns to 6:469/477 of 5u8uD
- active site: P16 (= P134), L47 (≠ I159), C51 (= C163), C56 (= C168), S59 (= S171), G85 (≠ E196), V86 (≠ P197), V193 (≠ I304), E197 (= E308), S333 (≠ V444), F451 (≠ H562), H453 (= H564), E458 (= E569)
- binding flavin-adenine dinucleotide: I12 (≠ L130), G15 (= G133), P16 (= P134), G17 (= G135), E36 (= E154), K37 (≠ R155), G49 (= G161), T50 (≠ V162), C51 (= C163), G55 (= G167), C56 (= C168), K60 (= K172), H123 (≠ Y234), G124 (= G235), A152 (= A263), S153 (≠ A264), G154 (= G265), I194 (= I305), R281 (= R392), G320 (= G431), D321 (= D432), M327 (= M438), L328 (= L439), A329 (= A440), H330 (= H441), H453 (= H564), P454 (= P565)
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.
43% identity, 77% coverage: 124:580/592 of query aligns to 4:467/475 of 6awaA
- active site: L45 (≠ I159), C49 (= C163), C54 (= C168), S57 (= S171), V191 (≠ I304), E195 (= E308), F449 (≠ H562), H451 (= H564), E456 (= E569)
- binding adenosine monophosphate: I187 (= I300), E211 (= E324), A212 (≠ L325), L213 (≠ G326), V245 (= V358), V277 (= V390)
- binding flavin-adenine dinucleotide: I10 (≠ L130), G13 (= G133), P14 (= P134), G15 (= G135), E34 (= E154), K35 (≠ R155), T48 (≠ V162), C49 (= C163), G53 (= G167), C54 (= C168), K58 (= K172), H121 (≠ Y234), G122 (= G235), S151 (≠ A264), G152 (= G265), I192 (= I305), R279 (= R392), G318 (= G431), D319 (= D432), M325 (= M438), L326 (= L439), A327 (= A440), Y358 (= Y471)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
46% identity, 77% coverage: 124:580/592 of query aligns to 6:464/470 of 6uziC
- active site: C45 (= C163), C50 (= C168), S53 (= S171), V187 (≠ I304), E191 (= E308), H448 (= H564), E453 (= E569)
- binding flavin-adenine dinucleotide: I12 (≠ L130), G13 (= G131), G15 (= G133), P16 (= P134), G17 (= G135), E36 (= E154), K37 (≠ R155), G43 (= G161), T44 (≠ V162), C45 (= C163), G49 (= G167), C50 (= C168), S53 (= S171), K54 (= K172), V117 (≠ Y234), G118 (= G235), T147 (≠ A264), G148 (= G265), I188 (= I305), R276 (= R392), D316 (= D432), M322 (= M438), L323 (= L439), A324 (= A440)
- binding zinc ion: H448 (= H564), E453 (= E569)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
42% identity, 79% coverage: 124:590/592 of query aligns to 4:477/477 of P18925
- 34:49 (vs. 154:163, 31% identical) binding FAD
- C49 (= C163) modified: Disulfide link with 54, Redox-active
- C54 (= C168) modified: Disulfide link with 49, Redox-active
- K58 (= K172) binding FAD
- D319 (= D432) binding FAD
- A327 (= A440) binding FAD
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)
42% identity, 77% coverage: 124:580/592 of query aligns to 3:466/472 of 3ladA
- active site: L44 (≠ I159), C48 (= C163), C53 (= C168), S56 (= S171), V190 (≠ I304), E194 (= E308), F448 (≠ H562), H450 (= H564), E455 (= E569)
- binding flavin-adenine dinucleotide: I9 (≠ L130), G10 (= G131), G12 (= G133), P13 (= P134), E33 (= E154), K34 (≠ R155), G46 (= G161), T47 (≠ V162), C48 (= C163), G52 (= G167), C53 (= C168), H120 (≠ Y234), G121 (= G235), A149 (= A263), S150 (≠ A264), G151 (= G265), I191 (= I305), R278 (= R392), D318 (= D432), L325 (= L439), A326 (= A440)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
44% identity, 76% coverage: 119:569/592 of query aligns to 7:465/482 of 6hg8B
- active site: C53 (= C163), C58 (= C168), S61 (= S171), V196 (≠ I304), E200 (= E308), H460 (= H564), E465 (= E569)
- binding flavin-adenine dinucleotide: I20 (≠ L130), G23 (= G133), P24 (= P134), G25 (= G135), E44 (= E154), K45 (≠ R155), N46 (≠ Y156), G51 (= G161), T52 (≠ V162), C53 (= C163), G57 (= G167), C58 (= C168), K62 (= K172), Y126 (= Y234), G127 (= G235), T156 (≠ A264), G157 (= G265), I197 (= I305), R288 (= R392), F291 (≠ N395), G327 (= G431), D328 (= D432), M334 (= M438), L335 (= L439), A336 (= A440), H337 (= H441)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
44% identity, 77% coverage: 116:569/592 of query aligns to 36:492/509 of P09622
- 71:80 (vs. 154:163, 40% identical) binding FAD
- K72 (≠ R155) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K172) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ R185) to T: in dbSNP:rs1130477
- G154 (= G235) binding FAD
- TGS 183:185 (≠ AGS 264:266) binding FAD
- 220:227 (vs. 301:308, 63% identical) binding NAD(+)
- E243 (= E324) binding NAD(+)
- V278 (= V358) binding NAD(+)
- G314 (= G391) binding NAD(+)
- D355 (= D432) binding FAD
- MLAH 361:364 (= MLAH 438:441) binding FAD
- E375 (= E452) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A460) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H525) 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 (= E543) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M550) 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 (= D556) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L559) 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 (= H562) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P565) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S568) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E569) 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.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
45% identity, 75% coverage: 126:569/592 of query aligns to 6:455/472 of 1zmdA
- active site: L39 (≠ I159), C43 (= C163), C48 (= C168), S51 (= S171), V186 (≠ I304), E190 (= E308), H448 (= H562), H450 (= H564), E455 (= E569)
- binding flavin-adenine dinucleotide: I10 (≠ L130), G11 (= G131), G13 (= G133), P14 (= P134), G15 (= G135), E34 (= E154), K35 (≠ R155), N36 (≠ Y156), G41 (= G161), T42 (≠ V162), C43 (= C163), G47 (= G167), C48 (= C168), K52 (= K172), Y116 (= Y234), G117 (= G235), T146 (≠ A264), G147 (= G265), S166 (= S284), R278 (= R392), F281 (≠ N395), G317 (= G431), D318 (= D432), M324 (= M438), L325 (= L439), A326 (= A440), H327 (= H441)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I300), G183 (= G301), G185 (= G303), V186 (≠ I304), I187 (= I305), E190 (= E308), E206 (= E324), F207 (vs. gap), L208 (= L325), I276 (≠ V390), G277 (= G391), R278 (= R392), M324 (= M438), L325 (= L439), V355 (= V469), Y357 (= Y471)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
45% identity, 75% coverage: 126:569/592 of query aligns to 6:455/472 of 1zmcA
- active site: L39 (≠ I159), C43 (= C163), C48 (= C168), S51 (= S171), V186 (≠ I304), E190 (= E308), H448 (= H562), H450 (= H564), E455 (= E569)
- binding flavin-adenine dinucleotide: I10 (≠ L130), G11 (= G131), G13 (= G133), P14 (= P134), G15 (= G135), E34 (= E154), K35 (≠ R155), N36 (≠ Y156), G41 (= G161), T42 (≠ V162), C43 (= C163), G47 (= G167), C48 (= C168), K52 (= K172), Y116 (= Y234), G117 (= G235), T146 (≠ A264), G147 (= G265), S166 (= S284), I187 (= I305), F281 (≠ N395), G317 (= G431), D318 (= D432), M324 (= M438), L325 (= L439), A326 (= A440), H327 (= H441)
- binding nicotinamide-adenine-dinucleotide: G183 (= G301), G185 (= G303), V205 (= V323), E206 (= E324), F207 (vs. gap), L208 (= L325), K240 (= K357), V241 (= V358), I276 (≠ V390), G277 (= G391), R278 (= R392), R297 (≠ W411), M324 (= M438)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
42% identity, 76% coverage: 126:575/592 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ I159), C39 (= C163), C44 (= C168), S47 (= S171), V183 (≠ I304), E187 (= E308), H443 (= H562), H445 (= H564), E450 (= E569)
- binding flavin-adenine dinucleotide: I6 (≠ L130), G7 (= G131), G9 (= G133), P10 (= P134), G11 (= G135), E30 (= E154), K31 (≠ R155), G37 (= G161), T38 (≠ V162), C39 (= C163), G43 (= G167), C44 (= C168), K48 (= K172), T111 (≠ Y234), G112 (= G235), A140 (= A263), T141 (≠ A264), G142 (= G265), I184 (= I305), R273 (= R392), G312 (= G431), D313 (= D432), M319 (= M438), L320 (= L439), A321 (= A440), H322 (= H441)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
46% identity, 76% coverage: 126:576/592 of query aligns to 5:449/460 of 2eq6A
- active site: V37 (≠ I159), C41 (= C163), C46 (= C168), T49 (≠ S171), A176 (≠ I304), E180 (= E308), H435 (= H562), H437 (= H564), E442 (= E569)
- binding flavin-adenine dinucleotide: I9 (≠ L130), G10 (= G131), G12 (= G133), P13 (= P134), G14 (= G135), E33 (= E154), A34 (≠ Y156), G39 (= G161), V40 (= V162), C41 (= C163), G45 (= G167), C46 (= C168), K50 (= K172), F111 (≠ Y234), A112 (≠ G235), A135 (= A263), T136 (≠ A264), G137 (= G265), S155 (= S284), R269 (≠ N395), D306 (= D432), L312 (≠ M438), L313 (= L439), A314 (= A440), H315 (= H441), Y344 (= Y471)
Sites not aligning to the query:
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
42% identity, 76% coverage: 126:575/592 of query aligns to 5:457/467 of 1dxlA
- active site: L38 (≠ I159), C42 (= C163), C47 (= C168), S50 (= S171), Y184 (≠ I304), E188 (= E308), H444 (= H562), H446 (= H564), E451 (= E569)
- binding flavin-adenine dinucleotide: I9 (≠ L130), P13 (= P134), G14 (= G135), E33 (= E154), K34 (≠ R155), R35 (≠ Y156), G40 (= G161), T41 (≠ V162), C42 (= C163), G46 (= G167), C47 (= C168), K51 (= K172), Y114 (= Y234), G115 (= G235), T144 (≠ A264), G145 (= G265), Y184 (≠ I304), I185 (= I305), R274 (= R392), D314 (= D432), M320 (= M438), L321 (= L439), A322 (= A440), H323 (= H441)
Query Sequence
>WP_028486698.1 NCBI__GCF_000483485.1:WP_028486698.1
MSKIVDIVVPDIGDFAEVDIIEVLVAAGEEVAQDDSLVTLESDKATMEIPAPFAGKVVTF
TAAVGDKVKEGSILGTIEIADSESVAANVETSVAASAAPAEEPKTEQPAPQAVSAADLPP
ADMQCEVLVLGSGPGGYTAAFRAADLGKKVVMIERYDNIGGVCLNVGCIPSKALLHMSVV
LNETREMGAHGITFAEPKIDTNKMREYKDSVIGKLTGGLAGLAKARKVEVVQGYGKFSSA
NTVTVEMADGSSKTIAFENAIIAAGSRVVKLPFIPHDDPRVMDSTDALELEEVPNRMLVI
GGGIIGLEMAQVYDSLGANITVVELGDTIIPGADKDISKPLLKKIKKQYENIYLKSKVTN
VEAKEEGLVVTFEGKDCPETDTFDRILVAVGRAPNGKLIDADKAGVAVNDWGFIEVDERQ
KTNVDHIYAIGDIVGQPMLAHKAVHEGKVAAEVINGMPSAFTPMSIPSVAYTDPEVAWAG
KTEQELKDEGIEYEKGAFPWAASGRSLSLGRDEGMTKALFCAETHRLLGCGIVGPNAGEL
IAEAMLAIEMGADMQDIGLTIHPHPTLSETICFAAEMAEGTITDLMPPKKKK
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