SitesBLAST
Comparing WP_028312512.1 NCBI__GCF_000482785.1:WP_028312512.1 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)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
70% identity, 75% coverage: 150:610/611 of query aligns to 19:482/482 of 1bhyA
- active site: L41 (= L172), C45 (= C176), C50 (= C181), S53 (= S184), I195 (= I323), E199 (= E327), H454 (= H582), H456 (= H584), E461 (= E589), P479 (= P607), Q480 (≠ A608)
- binding flavin-adenine dinucleotide: E36 (= E167), R37 (= R168), Y38 (= Y169), G43 (= G174), V44 (= V175), C45 (= C176), G49 (= G180), C50 (= C181), K54 (= K185), D116 (≠ V247), G117 (= G248), Y135 (≠ Q266), A156 (= A284), G157 (= G285), D324 (= D452), L331 (= L459), A332 (= A460)
Sites not aligning to the query:
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
64% identity, 77% coverage: 139:611/611 of query aligns to 7:471/471 of 4jdrA
- active site: P15 (= P147), L40 (= L172), C44 (= C176), C49 (= C181), S52 (= S184), E77 (≠ A209), P78 (= P210), I184 (= I323), E188 (= E327), V324 (= V464), H442 (= H582), H444 (= H584), E449 (= E589), N467 (≠ P607), P468 (≠ A608)
- binding flavin-adenine dinucleotide: G12 (= G144), G14 (= G146), P15 (= P147), A16 (≠ G148), E35 (= E167), R36 (= R168), Y37 (= Y169), V43 (= V175), C44 (= C176), G48 (= G180), C49 (= C181), K53 (= K185), L115 (≠ V247), G116 (= G248), A144 (= A284), G145 (= G285), I185 (= I324), G311 (= G451), D312 (= D452), M318 (= M458), L319 (= L459), A320 (= A460), H321 (= H461)
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)
64% identity, 77% coverage: 139:611/611 of query aligns to 8:472/474 of P0A9P0
- K220 (≠ N358) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 75% coverage: 141:600/611 of query aligns to 13:462/470 of P11959
- 39:47 (vs. 167:176, 60% identical) binding FAD
- K56 (= K185) binding FAD
- D314 (= D452) binding FAD
- A322 (= A460) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 75% coverage: 141:598/611 of query aligns to 7:454/455 of 1ebdA
- active site: P13 (= P147), L37 (= L172), C41 (= C176), C46 (= C181), S49 (= S184), N74 (≠ A209), V75 (≠ P210), Y180 (≠ I323), E184 (= E327), S320 (≠ V464), H438 (= H582), H440 (= H584), E445 (= E589)
- binding flavin-adenine dinucleotide: G10 (= G144), G12 (= G146), P13 (= P147), V32 (= V166), E33 (= E167), K34 (≠ R168), G39 (= G174), V40 (= V175), C41 (= C176), G45 (= G180), C46 (= C181), K50 (= K185), E112 (≠ V247), A113 (≠ G248), T141 (≠ A284), G142 (= G285), Y180 (≠ I323), I181 (= I324), R268 (= R412), D308 (= D452), A314 (≠ M458), L315 (= L459), A316 (= A460)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
43% identity, 75% coverage: 142:600/611 of query aligns to 11:464/470 of 6uziC
- active site: C45 (= C176), C50 (= C181), S53 (= S184), V187 (≠ I323), E191 (= E327), H448 (= H584), E453 (= E589)
- binding flavin-adenine dinucleotide: I12 (≠ L143), G13 (= G144), G15 (= G146), P16 (= P147), G17 (= G148), E36 (= E167), K37 (≠ R168), G43 (= G174), T44 (≠ V175), C45 (= C176), G49 (= G180), C50 (= C181), S53 (= S184), K54 (= K185), V117 (= V247), G118 (= G248), T147 (≠ A284), G148 (= G285), I188 (= I324), R276 (= R412), D316 (= D452), M322 (= M458), L323 (= L459), A324 (= A460)
- binding zinc ion: H448 (= H584), E453 (= E589)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
40% identity, 75% coverage: 140:595/611 of query aligns to 3:456/465 of 3urhB
- active site: Y35 (≠ L172), C39 (= C176), C44 (= C181), S47 (= S184), V183 (≠ I323), E187 (= E327), H443 (= H582), H445 (= H584), E450 (= E589)
- binding flavin-adenine dinucleotide: I6 (≠ L143), G7 (= G144), G9 (= G146), P10 (= P147), G11 (= G148), E30 (= E167), K31 (≠ R168), G37 (= G174), T38 (≠ V175), C39 (= C176), G43 (= G180), C44 (= C181), K48 (= K185), T111 (≠ V247), G112 (= G248), A140 (= A283), T141 (≠ A284), G142 (= G285), I184 (= I324), R273 (= R412), G312 (= G451), D313 (= D452), M319 (= M458), L320 (= L459), A321 (= A460), H322 (= H461)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
45% identity, 75% coverage: 137:596/611 of query aligns to 3:449/460 of 2eq6A
- active site: V37 (≠ L172), C41 (= C176), C46 (= C181), T49 (≠ S184), A176 (≠ I323), E180 (= E327), H435 (= H582), H437 (= H584), E442 (= E589)
- binding flavin-adenine dinucleotide: I9 (≠ L143), G10 (= G144), G12 (= G146), P13 (= P147), G14 (= G148), E33 (= E167), A34 (≠ Y169), G39 (= G174), V40 (= V175), C41 (= C176), G45 (= G180), C46 (= C181), K50 (= K185), F111 (≠ V247), A112 (≠ G248), A135 (= A283), T136 (≠ A284), G137 (= G285), S155 (= S303), R269 (≠ N415), D306 (= D452), L312 (≠ M458), L313 (= L459), A314 (= A460), H315 (= H461), Y344 (= Y491)
Sites not aligning to the query:
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
41% identity, 74% coverage: 142:594/611 of query aligns to 19:470/482 of 6hg8B
- active site: C53 (= C176), C58 (= C181), S61 (= S184), V196 (≠ I323), E200 (= E327), H460 (= H584), E465 (= E589)
- binding flavin-adenine dinucleotide: I20 (≠ L143), G23 (= G146), P24 (= P147), G25 (= G148), E44 (= E167), K45 (≠ R168), N46 (≠ Y169), G51 (= G174), T52 (≠ V175), C53 (= C176), G57 (= G180), C58 (= C181), K62 (= K185), Y126 (≠ V247), G127 (= G248), T156 (≠ A284), G157 (= G285), I197 (= I324), R288 (= R412), F291 (≠ N415), G327 (= G451), D328 (= D452), M334 (= M458), L335 (= L459), A336 (= A460), H337 (= H461)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
41% identity, 74% coverage: 142:591/611 of query aligns to 9:457/472 of 1zmdA
- active site: L39 (= L172), C43 (= C176), C48 (= C181), S51 (= S184), V186 (≠ I323), E190 (= E327), H448 (= H582), H450 (= H584), E455 (= E589)
- binding flavin-adenine dinucleotide: I10 (≠ L143), G11 (= G144), G13 (= G146), P14 (= P147), G15 (= G148), E34 (= E167), K35 (≠ R168), N36 (≠ Y169), G41 (= G174), T42 (≠ V175), C43 (= C176), G47 (= G180), C48 (= C181), K52 (= K185), Y116 (≠ V247), G117 (= G248), T146 (≠ A284), G147 (= G285), S166 (= S303), R278 (= R412), F281 (≠ N415), G317 (= G451), D318 (= D452), M324 (= M458), L325 (= L459), A326 (= A460), H327 (= H461)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I319), G183 (= G320), G185 (= G322), V186 (≠ I323), I187 (= I324), E190 (= E327), E206 (= E343), F207 (≠ M344), L208 (≠ M345), I276 (≠ V410), G277 (= G411), R278 (= R412), M324 (= M458), L325 (= L459), V355 (= V489), Y357 (= Y491)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
41% identity, 74% coverage: 142:591/611 of query aligns to 9:457/472 of 1zmcA
- active site: L39 (= L172), C43 (= C176), C48 (= C181), S51 (= S184), V186 (≠ I323), E190 (= E327), H448 (= H582), H450 (= H584), E455 (= E589)
- binding flavin-adenine dinucleotide: I10 (≠ L143), G11 (= G144), G13 (= G146), P14 (= P147), G15 (= G148), E34 (= E167), K35 (≠ R168), N36 (≠ Y169), G41 (= G174), T42 (≠ V175), C43 (= C176), G47 (= G180), C48 (= C181), K52 (= K185), Y116 (≠ V247), G117 (= G248), T146 (≠ A284), G147 (= G285), S166 (= S303), I187 (= I324), F281 (≠ N415), G317 (= G451), D318 (= D452), M324 (= M458), L325 (= L459), A326 (= A460), H327 (= H461)
- binding nicotinamide-adenine-dinucleotide: G183 (= G320), G185 (= G322), V205 (= V342), E206 (= E343), F207 (≠ M344), L208 (≠ M345), K240 (= K376), V241 (≠ T377), I276 (≠ V410), G277 (= G411), R278 (= R412), R297 (= R431), M324 (= M458)
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, 74% coverage: 142:591/611 of query aligns to 46:494/509 of P09622
- 71:80 (vs. 167:176, 60% identical) binding FAD
- K72 (≠ R168) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K185) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ S198) to T: in dbSNP:rs1130477
- G154 (= G248) binding FAD
- TGS 183:185 (≠ AGS 284:286) binding FAD
- 220:227 (vs. 320:327, 63% identical) binding NAD(+)
- E243 (= E343) binding NAD(+)
- V278 (≠ T377) binding NAD(+)
- G314 (= G411) binding NAD(+)
- D355 (= D452) binding FAD
- MLAH 361:364 (= MLAH 458:461) binding FAD
- E375 (= E472) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ F480) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H545) 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 (= E563) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M570) 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 (= D576) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ K579) 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 (= H582) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P585) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ G588) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E589) 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.
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
41% identity, 77% coverage: 140:611/611 of query aligns to 7:478/478 of P14218
- 34:49 (vs. 167:176, 38% identical) binding FAD
- C49 (= C176) modified: Disulfide link with 54, Redox-active
- C54 (= C181) modified: Disulfide link with 49, Redox-active
- K58 (= K185) binding FAD
- G122 (= G248) binding FAD
- D319 (= D452) binding FAD
- A327 (= A460) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
42% identity, 75% coverage: 140:600/611 of query aligns to 6:466/473 of 5u8wA
- active site: P13 (= P147), L44 (= L172), C48 (= C176), C53 (= C181), S56 (= S184), G82 (≠ A209), V83 (≠ P210), V190 (≠ I323), E194 (= E327), S330 (≠ V464), F448 (≠ H582), H450 (= H584), E455 (= E589)
- binding flavin-adenine dinucleotide: I9 (≠ L143), G12 (= G146), P13 (= P147), G14 (= G148), E33 (= E167), K34 (≠ R168), G46 (= G174), T47 (≠ V175), C48 (= C176), G52 (= G180), C53 (= C181), K57 (= K185), H120 (≠ V247), G121 (= G248), A149 (= A283), S150 (≠ A284), G151 (= G285), S170 (= S303), G317 (= G451), D318 (= D452), M324 (= M458), L325 (= L459), A326 (= A460), H327 (= H461), Y357 (= Y491), H450 (= H584), P451 (= P585)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I319), G189 (= G322), V190 (≠ I323), I191 (= I324), E194 (= E327), E210 (= E343), A211 (≠ M344), L212 (≠ M345), A275 (= A409), V276 (= V410), G277 (= G411), R278 (= R412), M324 (= M458), L325 (= L459), V355 (= V489), Y357 (= Y491)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
42% identity, 75% coverage: 140:600/611 of query aligns to 5:465/472 of 5u8vA
- active site: P12 (= P147), L43 (= L172), C47 (= C176), C52 (= C181), S55 (= S184), G81 (≠ A209), V82 (≠ P210), V189 (≠ I323), E193 (= E327), S329 (≠ V464), F447 (≠ H582), H449 (= H584), E454 (= E589)
- binding flavin-adenine dinucleotide: I8 (≠ L143), G11 (= G146), P12 (= P147), G13 (= G148), E32 (= E167), G45 (= G174), T46 (≠ V175), C47 (= C176), G51 (= G180), C52 (= C181), K56 (= K185), H119 (≠ V247), G120 (= G248), A148 (= A283), S149 (≠ A284), G150 (= G285), S169 (= S303), I190 (= I324), R277 (= R412), G316 (= G451), D317 (= D452), M323 (= M458), L324 (= L459), A325 (= A460), H326 (= H461), H449 (= H584), P450 (= P585)
- binding nicotinamide-adenine-dinucleotide: I185 (= I319), G186 (= G320), G188 (= G322), V189 (≠ I323), I190 (= I324), L208 (≠ V342), E209 (= E343), A210 (≠ M344), V243 (≠ T377), V275 (= V410), G276 (= G411)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
42% identity, 75% coverage: 140:600/611 of query aligns to 9:469/477 of 5u8uD
- active site: P16 (= P147), L47 (= L172), C51 (= C176), C56 (= C181), S59 (= S184), G85 (≠ A209), V86 (≠ P210), V193 (≠ I323), E197 (= E327), S333 (≠ V464), F451 (≠ H582), H453 (= H584), E458 (= E589)
- binding flavin-adenine dinucleotide: I12 (≠ L143), G15 (= G146), P16 (= P147), G17 (= G148), E36 (= E167), K37 (≠ R168), G49 (= G174), T50 (≠ V175), C51 (= C176), G55 (= G180), C56 (= C181), K60 (= K185), H123 (≠ V247), G124 (= G248), A152 (= A283), S153 (≠ A284), G154 (= G285), I194 (= I324), R281 (= R412), G320 (= G451), D321 (= D452), M327 (= M458), L328 (= L459), A329 (= A460), H330 (= H461), H453 (= H584), P454 (= P585)
Sites not aligning to the query:
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)
41% identity, 75% coverage: 140:600/611 of query aligns to 6:466/472 of 3ladA
- active site: L44 (= L172), C48 (= C176), C53 (= C181), S56 (= S184), V190 (≠ I323), E194 (= E327), F448 (≠ H582), H450 (= H584), E455 (= E589)
- binding flavin-adenine dinucleotide: I9 (≠ L143), G10 (= G144), G12 (= G146), P13 (= P147), E33 (= E167), K34 (≠ R168), G46 (= G174), T47 (≠ V175), C48 (= C176), G52 (= G180), C53 (= C181), H120 (≠ V247), G121 (= G248), A149 (= A283), S150 (≠ A284), G151 (= G285), I191 (= I324), R278 (= R412), D318 (= D452), L325 (= L459), A326 (= A460)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
41% identity, 75% coverage: 140:600/611 of query aligns to 7:467/477 of P18925
- 34:49 (vs. 167:176, 38% identical) binding FAD
- C49 (= C176) modified: Disulfide link with 54, Redox-active
- C54 (= C181) modified: Disulfide link with 49, Redox-active
- K58 (= K185) binding FAD
- D319 (= D452) binding FAD
- A327 (= A460) binding FAD
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
40% identity, 75% coverage: 140:600/611 of query aligns to 7:467/475 of 6awaA
- active site: L45 (= L172), C49 (= C176), C54 (= C181), S57 (= S184), V191 (≠ I323), E195 (= E327), F449 (≠ H582), H451 (= H584), E456 (= E589)
- binding adenosine monophosphate: I187 (= I319), E211 (= E343), A212 (≠ M344), L213 (≠ M345), V245 (≠ T377), V277 (= V410)
- binding flavin-adenine dinucleotide: I10 (≠ L143), G13 (= G146), P14 (= P147), G15 (= G148), E34 (= E167), K35 (≠ R168), T48 (≠ V175), C49 (= C176), G53 (= G180), C54 (= C181), K58 (= K185), H121 (≠ V247), G122 (= G248), S151 (≠ A284), G152 (= G285), I192 (= I324), R279 (= R412), G318 (= G451), D319 (= D452), M325 (= M458), L326 (= L459), A327 (= A460), Y358 (= Y491)
Sites not aligning to the query:
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
42% identity, 72% coverage: 152:591/611 of query aligns to 17:451/465 of 2qaeA
- active site: L37 (= L172), C41 (= C176), C46 (= C181), S49 (= S184), V184 (≠ I323), E188 (= E327), H442 (= H582), H444 (= H584), E449 (= E589)
- binding flavin-adenine dinucleotide: E32 (= E167), K33 (≠ R168), R34 (≠ Y169), G39 (= G174), T40 (≠ V175), C41 (= C176), G45 (= G180), C46 (= C181), K50 (= K185), E114 (≠ V247), G115 (= G248), T144 (≠ A284), G145 (= G285), S164 (= S303), I185 (= I324), F274 (≠ N415), G310 (= G451), D311 (= D452), M318 (= M458), L319 (= L459), A320 (= A460), H321 (= H461)
Sites not aligning to the query:
Query Sequence
>WP_028312512.1 NCBI__GCF_000482785.1:WP_028312512.1
MSQIIEVTVPDIGDFDAVEVIEVLVKPGDKIAKEQSLITLESDKASMEVPSDAAGVVKEI
KVKVGDKVSKGSVILLAESDGAAAPATAPAAPASAATPVPAPAVQSSPAPVPAAAPAPAS
VPAPNAAPAYTGKVDHTCRMLVLGAGPGGYSAAFRSADLGMDTIIVERYATLGGVCLNVG
CIPSKALLHVAAVMDEASHFADLGVEFAAPKIDIDKLRAHKEKVVGKLTGGLAGMAKARK
VRTVRGVGRFIDSHHLEVSVASGTGQELTGEKQVIKFEQAIIAAGSQPVKLPFVPEDPRI
VDSTGALELRQVPKKMLVIGGGIIGLEMATVYSTLGARIDVVEMMDGLMVGPDRDLVNVW
QKYNAKRFDKVMLKTKTVGVEAKPEGIAVTFEGEQAPAEPQLYDLVLVAVGRSPNGKKIG
AEAAGVAVTDRGFIPVDRQMRTNVPHIFAIGDLVGQPMLAHKAVHEAHVAAEAAAGEKAF
FDARVIPGVAYTDPEVAWVGTTEDEAKKAGIKVKVGKFPWAASGRAIANTRDEGFTKLIF
DEASHKIIGGGIVGTHAGDFIGEVALAIEMGADVVDIAKTIHPHPTLGESIGMAAEVAEG
VCTDLPPARKK
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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