SitesBLAST
Comparing Pf1N1B4_4477 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4477 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)
1lvlA The refined structure of pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 angstroms resolution (see paper)
76% identity, 100% coverage: 2:460/460 of query aligns to 2:458/458 of 1lvlA
- active site: P15 (= P15), L39 (= L39), C43 (= C43), C48 (= C48), S51 (= S51), S79 (≠ A79), P80 (= P80), Y181 (= Y181), E185 (= E185), M317 (= M319), H435 (= H437), H437 (= H439), E442 (= E444)
- binding flavin-adenine dinucleotide: I11 (= I11), G12 (= G12), E35 (= E35), G36 (= G36), G41 (= G41), T42 (= T42), C43 (= C43), G47 (= G47), C48 (= C48), K52 (= K52), W117 (= W117), A118 (= A118), A141 (= A141), T142 (= T142), G143 (= G143), Y181 (= Y181), R266 (= R268), R269 (≠ N271), D305 (= D307), L312 (= L314), A313 (= A315), H314 (= H316)
- binding nicotinamide-adenine-dinucleotide: V177 (= V177), G178 (= G178), Y181 (= Y181), I182 (= I182), E201 (= E201), A263 (= A265), V264 (= V266), G265 (= G267), R266 (= R268), E309 (= E311), M311 (= M313)
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)
76% identity, 100% coverage: 2:460/460 of query aligns to 3:459/459 of P09063
- 36:44 (vs. 35:43, 89% identical) binding
- C44 (= C43) modified: Disulfide link with 49, Redox-active
- C49 (= C48) modified: Disulfide link with 44, Redox-active
- K53 (= K52) binding
- A119 (= A118) binding
- A142 (= A141) binding
- GGGYI 179:183 (= GGGYI 178:182) binding
- Y182 (= Y181) binding
- E202 (= E201) binding
- V236 (= V235) binding
- AVGR 264:267 (= AVGR 265:268) binding
- D306 (= D307) binding
- M312 (= M313) binding
- A314 (= A315) binding
6cmzA 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
68% identity, 99% coverage: 5:460/460 of query aligns to 4:462/462 of 6cmzA
- active site: C42 (= C43), C47 (= C48), S50 (= S51), Y184 (= Y181), E188 (= E185), H441 (= H439), E446 (= E444)
- binding flavin-adenine dinucleotide: G11 (= G12), G13 (= G14), P14 (= P15), E34 (= E35), R35 (≠ G36), G40 (= G41), T41 (= T42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), E116 (≠ W117), A117 (= A118), T145 (= T142), G146 (= G143), V180 (= V177), G181 (= G178), Y184 (= Y181), I185 (= I182), E204 (= E201), V268 (= V266), R270 (= R268), R273 (≠ N271), F277 (≠ W275), R289 (≠ S287), G308 (= G306), D309 (= D307), M315 (= M313), L316 (= L314), A317 (= A315), H318 (= H316)
- binding flavin mononucleotide: L152 (= L149), P153 (= P150)
6cmzB 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
68% identity, 98% coverage: 5:457/460 of query aligns to 4:459/459 of 6cmzB
- active site: C42 (= C43), C47 (= C48), S50 (= S51), Y184 (= Y181), E188 (= E185), H441 (= H439), E446 (= E444)
- binding adenosine-5'-diphosphate: V150 (= V147), L152 (= L149), G181 (= G178), G183 (= G180), A205 (= A202), V268 (= V266), G269 (= G267)
- binding flavin-adenine dinucleotide: G11 (= G12), G13 (= G14), P14 (= P15), E34 (= E35), R35 (≠ G36), T41 (= T42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), E116 (≠ W117), A117 (= A118), T145 (= T142), G146 (= G143), S164 (= S161), Y184 (= Y181), I185 (= I182), R270 (= R268), F277 (≠ W275), G308 (= G306), D309 (= D307), M315 (= M313), L316 (= L314), A317 (= A315), H318 (= H316)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
41% identity, 99% coverage: 4:460/460 of query aligns to 8:467/470 of P11959
- 39:47 (vs. 35:43, 56% identical) binding
- K56 (= K52) binding
- D314 (= D307) binding
- A322 (= A315) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
41% identity, 98% coverage: 4:454/460 of query aligns to 2:455/455 of 1ebdA
- active site: P13 (= P15), L37 (= L39), C41 (= C43), C46 (= C48), S49 (= S51), N74 (≠ A79), V75 (≠ P80), Y180 (= Y181), E184 (= E185), S320 (≠ M319), H438 (= H437), H440 (= H439), E445 (= E444)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), P13 (= P15), V32 (= V34), E33 (= E35), K34 (≠ G36), G39 (= G41), V40 (≠ T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), E112 (≠ W117), A113 (= A118), T141 (= T142), G142 (= G143), Y180 (= Y181), I181 (= I182), R268 (= R268), D308 (= D307), A314 (≠ M313), L315 (= L314), A316 (= A315)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
42% identity, 98% coverage: 8:459/460 of query aligns to 3:465/465 of 3urhB
- active site: Y35 (≠ L39), C39 (= C43), C44 (= C48), S47 (= S51), V183 (≠ Y181), E187 (= E185), H443 (= H437), H445 (= H439), E450 (= E444)
- binding flavin-adenine dinucleotide: I6 (= I11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (= G16), E30 (= E35), K31 (≠ G36), G37 (= G41), T38 (= T42), C39 (= C43), G43 (= G47), C44 (= C48), K48 (= K52), T111 (≠ W117), G112 (≠ A118), A140 (= A141), T141 (= T142), G142 (= G143), I184 (= I182), R273 (= R268), G312 (= G306), D313 (= D307), M319 (= M313), L320 (= L314), A321 (= A315), H322 (= H316)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
41% identity, 100% coverage: 1:460/460 of query aligns to 1:458/460 of 2eq6A
- active site: V37 (≠ L39), C41 (= C43), C46 (= C48), T49 (≠ S51), A176 (≠ Y181), E180 (= E185), H435 (= H437), H437 (= H439), E442 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I11), G10 (= G12), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), A34 (≠ G36), G39 (= G41), V40 (≠ T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), F111 (≠ W117), A112 (= A118), A135 (= A141), T136 (= T142), G137 (= G143), S155 (= S161), R269 (≠ N271), D306 (= D307), L312 (≠ M313), L313 (= L314), A314 (= A315), H315 (= H316), Y344 (≠ F346)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
39% identity, 98% coverage: 10:460/460 of query aligns to 11:470/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (= S51), V187 (≠ Y181), E191 (= E185), H448 (= H439), E453 (= E444)
- binding flavin-adenine dinucleotide: I12 (= I11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (≠ G36), G43 (= G41), T44 (= T42), C45 (= C43), G49 (= G47), C50 (= C48), S53 (= S51), K54 (= K52), V117 (≠ W117), G118 (≠ A118), T147 (= T142), G148 (= G143), I188 (= I182), R276 (= R268), D316 (= D307), M322 (= M313), L323 (= L314), A324 (= A315)
- binding zinc ion: H448 (= H439), E453 (= E444)
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)
40% identity, 98% coverage: 8:460/460 of query aligns to 6:471/472 of 3ladA
- active site: L44 (= L39), C48 (= C43), C53 (= C48), S56 (= S51), V190 (≠ Y181), E194 (= E185), F448 (≠ H437), H450 (= H439), E455 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I11), G10 (= G12), G12 (= G14), P13 (= P15), E33 (= E35), K34 (≠ G36), G46 (= G41), T47 (= T42), C48 (= C43), G52 (= G47), C53 (= C48), H120 (≠ W117), G121 (≠ A118), A149 (= A141), S150 (≠ T142), G151 (= G143), I191 (= I182), R278 (= R268), D318 (= D307), L325 (= L314), A326 (= A315)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
40% identity, 98% coverage: 8:460/460 of query aligns to 7:472/477 of P18925
- 34:49 (vs. 35:43, 38% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- D319 (= D307) binding
- A327 (= A315) binding
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
38% identity, 97% coverage: 4:450/460 of query aligns to 4:455/471 of 4jdrA
- active site: P15 (= P15), L40 (= L39), C44 (= C43), C49 (= C48), S52 (= S51), E77 (≠ A79), P78 (= P80), I184 (≠ Y181), E188 (= E185), V324 (≠ M319), H442 (= H437), H444 (= H439), E449 (= E444)
- binding flavin-adenine dinucleotide: G12 (= G12), G14 (= G14), P15 (= P15), A16 (≠ G16), E35 (= E35), R36 (≠ G36), Y37 (vs. gap), V43 (≠ T42), C44 (= C43), G48 (= G47), C49 (= C48), K53 (= K52), L115 (≠ W117), G116 (≠ A118), A144 (≠ T142), G145 (= G143), I185 (= I182), G311 (= G306), D312 (= D307), M318 (= M313), L319 (= L314), A320 (= A315), H321 (= H316)
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, 97% coverage: 4:450/460 of query aligns to 5:456/474 of P0A9P0
- K220 (≠ H216) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
38% identity, 98% coverage: 8:460/460 of query aligns to 40:501/501 of P31023
- 67:76 (vs. 35:43, 60% identical) binding
- C76 (= C43) modified: Disulfide link with 81, Redox-active
- C81 (= C48) modified: Disulfide link with 76, Redox-active
- G149 (≠ A118) binding
- D348 (= D307) binding
- MLAH 354:357 (= MLAH 313:316) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
38% identity, 98% coverage: 8:460/460 of query aligns to 6:467/467 of 1dxlA
- active site: L38 (= L39), C42 (= C43), C47 (= C48), S50 (= S51), Y184 (= Y181), E188 (= E185), H444 (= H437), H446 (= H439), E451 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I11), P13 (= P15), G14 (= G16), E33 (= E35), K34 (≠ G36), R35 (≠ Q37), G40 (= G41), T41 (= T42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y114 (≠ W117), G115 (≠ A118), T144 (= T142), G145 (= G143), Y184 (= Y181), I185 (= I182), R274 (= R268), D314 (= D307), M320 (= M313), L321 (= L314), A322 (= A315), H323 (= H316)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
39% identity, 98% coverage: 8:460/460 of query aligns to 7:472/478 of P14218
- 34:49 (vs. 35:43, 38% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- G122 (≠ A118) binding
- D319 (= D307) binding
- A327 (= A315) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
39% identity, 98% coverage: 8:460/460 of query aligns to 9:474/477 of 5u8uD
- active site: P16 (= P15), L47 (= L39), C51 (= C43), C56 (= C48), S59 (= S51), G85 (≠ A79), V86 (≠ P80), V193 (≠ Y181), E197 (= E185), S333 (≠ M319), F451 (≠ H437), H453 (= H439), E458 (= E444)
- binding flavin-adenine dinucleotide: I12 (= I11), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (≠ G36), G49 (= G41), T50 (= T42), C51 (= C43), G55 (= G47), C56 (= C48), K60 (= K52), H123 (≠ W117), G124 (≠ A118), A152 (= A141), S153 (≠ T142), G154 (= G143), I194 (= I182), R281 (= R268), G320 (= G306), D321 (= D307), M327 (= M313), L328 (= L314), A329 (= A315), H330 (= H316), H453 (= H439), P454 (= P440)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
39% identity, 98% coverage: 8:460/460 of query aligns to 5:470/472 of 5u8vA
- active site: P12 (= P15), L43 (= L39), C47 (= C43), C52 (= C48), S55 (= S51), G81 (≠ A79), V82 (≠ P80), V189 (≠ Y181), E193 (= E185), S329 (≠ M319), F447 (≠ H437), H449 (= H439), E454 (= E444)
- binding flavin-adenine dinucleotide: I8 (= I11), G11 (= G14), P12 (= P15), G13 (= G16), E32 (= E35), G45 (= G41), T46 (= T42), C47 (= C43), G51 (= G47), C52 (= C48), K56 (= K52), H119 (≠ W117), G120 (≠ A118), A148 (= A141), S149 (≠ T142), G150 (= G143), S169 (= S161), I190 (= I182), R277 (= R268), G316 (= G306), D317 (= D307), M323 (= M313), L324 (= L314), A325 (= A315), H326 (= H316), H449 (= H439), P450 (= P440)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V177), G186 (= G178), G188 (= G180), V189 (≠ Y181), I190 (= I182), L208 (≠ V200), E209 (= E201), A210 (= A202), V243 (≠ H233), V275 (= V266), G276 (= G267)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
39% identity, 98% coverage: 8:460/460 of query aligns to 6:471/473 of 5u8wA
- active site: P13 (= P15), L44 (= L39), C48 (= C43), C53 (= C48), S56 (= S51), G82 (≠ A79), V83 (≠ P80), V190 (≠ Y181), E194 (= E185), S330 (≠ M319), F448 (≠ H437), H450 (= H439), E455 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I11), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), K34 (≠ G36), G46 (= G41), T47 (= T42), C48 (= C43), G52 (= G47), C53 (= C48), K57 (= K52), H120 (≠ W117), G121 (≠ A118), A149 (= A141), S150 (≠ T142), G151 (= G143), S170 (= S161), G317 (= G306), D318 (= D307), M324 (= M313), L325 (= L314), A326 (= A315), H327 (= H316), Y357 (≠ F346), H450 (= H439), P451 (= P440)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V177), G189 (= G180), V190 (≠ Y181), I191 (= I182), E194 (= E185), E210 (= E201), A211 (= A202), L212 (≠ Q203), A275 (= A265), V276 (= V266), G277 (= G267), R278 (= R268), M324 (= M313), L325 (= L314), V355 (= V344), Y357 (≠ F346)
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.
39% identity, 98% coverage: 8:460/460 of query aligns to 7:472/475 of 6awaA
- active site: L45 (= L39), C49 (= C43), C54 (= C48), S57 (= S51), V191 (≠ Y181), E195 (= E185), F449 (≠ H437), H451 (= H439), E456 (= E444)
- binding adenosine monophosphate: I187 (≠ V177), E211 (= E201), A212 (= A202), L213 (≠ Q203), V245 (= V235), V277 (= V266)
- binding flavin-adenine dinucleotide: I10 (= I11), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (≠ G36), T48 (= T42), C49 (= C43), G53 (= G47), C54 (= C48), K58 (= K52), H121 (≠ W117), G122 (≠ A118), S151 (≠ T142), G152 (= G143), I192 (= I182), R279 (= R268), G318 (= G306), D319 (= D307), M325 (= M313), L326 (= L314), A327 (= A315), Y358 (≠ F346)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_4477 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4477
MQTLNTTLLIIGGGPGGYVTAIRAGQLGISTILVEGQSLGGTCLNIGCIPSKALIHVAEQ
FHQTQHHSQHSALGISVSAPTLNIGKSVEWKDGIVDRLTTGVSALLKKHKVQVIQGWAKV
IDGKTVEVGDTRIQCEHLVLATGSKSVNLPMLPIGGPIISSTEALAPTSVPKRLIVVGGG
YIGLELGIAYRKLGAEVSVVEAQDRILPAYDAELTHPVHEALKQLDVKLYLKHSVQGFDS
VNNTLQVIDPSGDSLNLKTDQVLVAVGRKPNTQGWNLEALNLDMNGSAIKIDNRCQTSMR
NVYAIGDLSGEPMLAHRAMAQGEMVAELISGKHREFNPTAIAAVCFTDPELVVVGKTPDE
AKAAGLDCIVSSFPFAANGRAMTLESRSGFVRVVARRDNHVIVGWQAVGVGVSELSTAFG
QSLEMGARLEDIAGTIHAHPTLGEAVQEAALRALGHALHL
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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