SitesBLAST
Comparing PP_4404 FitnessBrowser__Putida:PP_4404 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)
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)
98% identity, 100% coverage: 1:459/459 of query aligns to 1:459/459 of P09063
- 36:44 (vs. 36:44, 100% identical) binding
- C44 (= C44) modified: Disulfide link with 49, Redox-active
- C49 (= C49) modified: Disulfide link with 44, Redox-active
- K53 (= K53) binding
- A119 (= A119) binding
- A142 (= A142) binding
- GGGYI 179:183 (= GGGYI 179:183) binding
- Y182 (= Y182) binding
- E202 (= E202) binding
- V236 (= V236) binding
- AVGR 264:267 (= AVGR 264:267) binding
- D306 (= D306) binding
- M312 (= M312) binding
- A314 (= A314) binding
1lvlA The refined structure of pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 angstroms resolution (see paper)
98% identity, 100% coverage: 2:459/459 of query aligns to 1:458/458 of 1lvlA
- active site: P15 (= P16), L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), S79 (= S80), P80 (= P81), Y181 (= Y182), E185 (= E186), M317 (= M318), H435 (= H436), H437 (= H438), E442 (= E443)
- binding flavin-adenine dinucleotide: I11 (= I12), G12 (= G13), E35 (= E36), G36 (= G37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), W117 (= W118), A118 (= A119), A141 (= A142), T142 (= T143), G143 (= G144), Y181 (= Y182), R266 (= R267), R269 (= R270), D305 (= D306), L312 (= L313), A313 (= A314), H314 (= H315)
- binding nicotinamide-adenine-dinucleotide: V177 (= V178), G178 (= G179), Y181 (= Y182), I182 (= I183), E201 (= E202), A263 (= A264), V264 (= V265), G265 (= G266), R266 (= R267), E309 (= E310), M311 (= M312)
6cmzA 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
70% identity, 99% coverage: 6:459/459 of query aligns to 4:462/462 of 6cmzA
- active site: C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y182), E188 (= E186), H441 (= H438), E446 (= E443)
- binding flavin-adenine dinucleotide: G11 (= G13), G13 (= G15), P14 (= P16), E34 (= E36), R35 (≠ G37), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), E116 (≠ W118), A117 (= A119), T145 (= T143), G146 (= G144), V180 (= V178), G181 (= G179), Y184 (= Y182), I185 (= I183), E204 (= E202), V268 (= V265), R270 (= R267), R273 (= R270), F277 (= F274), R289 (≠ A286), G308 (= G305), D309 (= D306), M315 (= M312), L316 (= L313), A317 (= A314), H318 (= H315)
- binding flavin mononucleotide: L152 (= L150), P153 (= P151)
6cmzB 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
70% identity, 98% coverage: 6:456/459 of query aligns to 4:459/459 of 6cmzB
- active site: C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y182), E188 (= E186), H441 (= H438), E446 (= E443)
- binding adenosine-5'-diphosphate: V150 (= V148), L152 (= L150), G181 (= G179), G183 (= G181), A205 (= A203), V268 (= V265), G269 (= G266)
- binding flavin-adenine dinucleotide: G11 (= G13), G13 (= G15), P14 (= P16), E34 (= E36), R35 (≠ G37), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), E116 (≠ W118), A117 (= A119), T145 (= T143), G146 (= G144), S164 (= S162), Y184 (= Y182), I185 (= I183), R270 (= R267), F277 (= F274), G308 (= G305), D309 (= D306), M315 (= M312), L316 (= L313), A317 (= A314), H318 (= H315)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
42% identity, 99% coverage: 5:459/459 of query aligns to 8:467/470 of P11959
- 39:47 (vs. 36:44, 56% identical) binding
- K56 (= K53) binding
- D314 (= D306) binding
- A322 (= A314) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
42% identity, 98% coverage: 5:453/459 of query aligns to 2:455/455 of 1ebdA
- active site: P13 (= P16), L37 (= L40), C41 (= C44), C46 (= C49), S49 (= S52), N74 (≠ S80), V75 (≠ P81), Y180 (= Y182), E184 (= E186), S320 (≠ M318), H438 (= H436), H440 (= H438), E445 (= E443)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (= P16), V32 (= V35), E33 (= E36), K34 (≠ G37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E112 (≠ W118), A113 (= A119), T141 (= T143), G142 (= G144), Y180 (= Y182), I181 (= I183), R268 (= R267), D308 (= D306), A314 (≠ M312), L315 (= L313), A316 (= A314)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
43% identity, 98% coverage: 9:459/459 of query aligns to 6:458/460 of 2eq6A
- active site: V37 (≠ L40), C41 (= C44), C46 (= C49), T49 (≠ S52), A176 (≠ Y182), E180 (= E186), H435 (= H436), H437 (= H438), E442 (= E443)
- binding flavin-adenine dinucleotide: I9 (= I12), G10 (= G13), G12 (= G15), P13 (= P16), G14 (= G17), E33 (= E36), A34 (≠ G37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), F111 (≠ W118), A112 (= A119), A135 (= A142), T136 (= T143), G137 (= G144), S155 (= S162), R269 (= R270), D306 (= D306), L312 (≠ M312), L313 (= L313), A314 (= A314), H315 (= H315), Y344 (≠ F345)
Sites not aligning to the query:
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)
38% identity, 98% coverage: 1:449/459 of query aligns to 1:456/474 of P0A9P0
- M1 (= M1) modified: Initiator methionine, Removed
- K220 (≠ A217) modified: N6-acetyllysine
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
38% identity, 97% coverage: 5:449/459 of query aligns to 4:455/471 of 4jdrA
- active site: P15 (= P16), L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), E77 (≠ S80), P78 (= P81), I184 (≠ Y182), E188 (= E186), V324 (≠ M318), H442 (= H436), H444 (= H438), E449 (= E443)
- binding flavin-adenine dinucleotide: G12 (= G13), G14 (= G15), P15 (= P16), A16 (≠ G17), E35 (= E36), R36 (≠ G37), Y37 (vs. gap), V43 (≠ T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), L115 (≠ W118), G116 (≠ A119), A144 (≠ T143), G145 (= G144), I185 (= I183), G311 (= G305), D312 (= D306), M318 (= M312), L319 (= L313), A320 (= A314), H321 (= H315)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
40% identity, 98% coverage: 9:458/459 of query aligns to 3:465/465 of 3urhB
- active site: Y35 (≠ L40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (≠ Y182), E187 (= E186), H443 (= H436), H445 (= H438), E450 (= E443)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), P10 (= P16), G11 (= G17), E30 (= E36), K31 (≠ G37), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ W118), G112 (≠ A119), A140 (= A142), T141 (= T143), G142 (= G144), I184 (= I183), R273 (= R267), G312 (= G305), D313 (= D306), M319 (= M312), L320 (= L313), A321 (= A314), H322 (= H315)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
39% identity, 99% coverage: 6:459/459 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (≠ Y182), E191 (= E186), H448 (= H438), E453 (= E443)
- binding flavin-adenine dinucleotide: I12 (= I12), G13 (= G13), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ G37), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ W118), G118 (≠ A119), T147 (= T143), G148 (= G144), I188 (= I183), R276 (= R267), D316 (= D306), M322 (= M312), L323 (= L313), A324 (= A314)
- binding zinc ion: H448 (= H438), E453 (= E443)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
41% identity, 98% coverage: 9:459/459 of query aligns to 7:472/477 of P18925
- 34:49 (vs. 36:44, 44% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- D319 (= D306) binding
- A327 (= A314) 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)
41% identity, 98% coverage: 9:459/459 of query aligns to 6:471/472 of 3ladA
- active site: L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), V190 (≠ Y182), E194 (= E186), F448 (≠ H436), H450 (= H438), E455 (= E443)
- binding flavin-adenine dinucleotide: I9 (= I12), G10 (= G13), G12 (= G15), P13 (= P16), E33 (= E36), K34 (≠ G37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), H120 (≠ W118), G121 (≠ A119), A149 (= A142), S150 (≠ T143), G151 (= G144), I191 (= I183), R278 (= R267), D318 (= D306), L325 (= L313), A326 (= A314)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
40% identity, 98% coverage: 9:459/459 of query aligns to 7:472/478 of P14218
- 34:49 (vs. 36:44, 44% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (≠ A119) binding
- D319 (= D306) binding
- A327 (= A314) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
40% identity, 98% coverage: 9:459/459 of query aligns to 9:474/477 of 5u8uD
- active site: P16 (= P16), L47 (= L40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ S80), V86 (≠ P81), V193 (≠ Y182), E197 (= E186), S333 (≠ M318), F451 (≠ H436), H453 (= H438), E458 (= E443)
- binding flavin-adenine dinucleotide: I12 (= I12), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ G37), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ W118), G124 (≠ A119), A152 (= A142), S153 (≠ T143), G154 (= G144), I194 (= I183), R281 (= R267), G320 (= G305), D321 (= D306), M327 (= M312), L328 (= L313), A329 (= A314), H330 (= H315), H453 (= H438), P454 (= P439)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
40% identity, 98% coverage: 9:459/459 of query aligns to 6:471/473 of 5u8wA
- active site: P13 (= P16), L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ S80), V83 (≠ P81), V190 (≠ Y182), E194 (= E186), S330 (≠ M318), F448 (≠ H436), H450 (= H438), E455 (= E443)
- binding flavin-adenine dinucleotide: I9 (= I12), G12 (= G15), P13 (= P16), G14 (= G17), E33 (= E36), K34 (≠ G37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ W118), G121 (≠ A119), A149 (= A142), S150 (≠ T143), G151 (= G144), S170 (= S162), G317 (= G305), D318 (= D306), M324 (= M312), L325 (= L313), A326 (= A314), H327 (= H315), Y357 (≠ F345), H450 (= H438), P451 (= P439)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V178), G189 (= G181), V190 (≠ Y182), I191 (= I183), E194 (= E186), E210 (= E202), A211 (= A203), L212 (≠ R204), A275 (= A264), V276 (= V265), G277 (= G266), R278 (= R267), M324 (= M312), L325 (= L313), V355 (= V343), Y357 (≠ F345)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
40% identity, 98% coverage: 9:459/459 of query aligns to 5:470/472 of 5u8vA
- active site: P12 (= P16), L43 (= L40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (≠ S80), V82 (≠ P81), V189 (≠ Y182), E193 (= E186), S329 (≠ M318), F447 (≠ H436), H449 (= H438), E454 (= E443)
- binding flavin-adenine dinucleotide: I8 (= I12), G11 (= G15), P12 (= P16), G13 (= G17), E32 (= E36), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ W118), G120 (≠ A119), A148 (= A142), S149 (≠ T143), G150 (= G144), S169 (= S162), I190 (= I183), R277 (= R267), G316 (= G305), D317 (= D306), M323 (= M312), L324 (= L313), A325 (= A314), H326 (= H315), H449 (= H438), P450 (= P439)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V178), G186 (= G179), G188 (= G181), V189 (≠ Y182), I190 (= I183), L208 (≠ V201), E209 (= E202), A210 (= A203), V243 (= V236), V275 (= V265), G276 (= G266)
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)
39% identity, 99% coverage: 6:459/459 of query aligns to 37:501/501 of P31023
- 67:76 (vs. 36:44, 70% identical) binding
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (≠ A119) binding
- D348 (= D306) binding
- MLAH 354:357 (= MLAH 312:315) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
39% identity, 99% coverage: 6:459/459 of query aligns to 3:467/467 of 1dxlA
- active site: L38 (= L40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y182), E188 (= E186), H444 (= H436), H446 (= H438), E451 (= E443)
- binding flavin-adenine dinucleotide: I9 (= I12), P13 (= P16), G14 (= G17), E33 (= E36), K34 (≠ G37), R35 (≠ Q38), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (≠ W118), G115 (≠ A119), T144 (= T143), G145 (= G144), Y184 (= Y182), I185 (= I183), R274 (= R267), D314 (= D306), M320 (= M312), L321 (= L313), A322 (= A314), H323 (= H315)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
39% identity, 98% coverage: 9:459/459 of query aligns to 7:472/475 of 6awaA
- active site: L45 (= L40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (≠ Y182), E195 (= E186), F449 (≠ H436), H451 (= H438), E456 (= E443)
- binding adenosine monophosphate: I187 (≠ V178), E211 (= E202), A212 (= A203), L213 (≠ R204), V245 (= V236), V277 (= V265)
- binding flavin-adenine dinucleotide: I10 (= I12), G13 (= G15), P14 (= P16), G15 (= G17), E34 (= E36), K35 (≠ G37), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ W118), G122 (≠ A119), S151 (≠ T143), G152 (= G144), I192 (= I183), R279 (= R267), G318 (= G305), D319 (= D306), M325 (= M312), L326 (= L313), A327 (= A314), Y358 (≠ F345)
Sites not aligning to the query:
Query Sequence
>PP_4404 FitnessBrowser__Putida:PP_4404
MQQIIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAE
QFHQASRFTEPSPLGISVASPRLDIGQSVTWKDGIVDRLTTGVAALLKKHGVKVVHGWAK
VLDGKQVEVDGQRIQCEHLLLATGSSSVELPMLPLGGPVISSTEALAPKTLPQHLVVVGG
GYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYE
NGCLLASDGKGGQLRLEADQVLVAVGRRPRTKGFNLECLDLKMNGAAIAIDERCHTSMHN
VWAIGDVAGEPMLAHRAMAQGEMVAEIIAGKARRFEPTAIAAVCFTDPEVVVVGKTPEQA
SQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLIVGWQAVGVAVSELSTAFAQ
SLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI
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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