SitesBLAST
Comparing H281DRAFT_02737 FitnessBrowser__Burk376:H281DRAFT_02737 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)
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
34% identity, 98% coverage: 7:460/465 of query aligns to 4:440/441 of 6kgyB
- active site: C43 (= C44), C48 (= C49), T51 (≠ S52), Y168 (= Y185), E172 (= E189), H426 (= H446), E431 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G12 (= G15), E33 (= E36), Q34 (≠ R37), M38 (≠ W39), G41 (= G42), T42 (≠ S43), G47 (≠ A48), C48 (= C49), A99 (≠ G116), N126 (= N144), T127 (≠ V145), G128 (= G146), G291 (= G313), D292 (≠ E314), F299 (= F321), T300 (= T322), Y301 (≠ H323), S303 (= S325), F333 (= F353)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
35% identity, 97% coverage: 10:460/465 of query aligns to 3:431/432 of 6kyyA
- active site: C39 (= C44), C44 (= C49), T47 (≠ S52), Y159 (= Y185), E163 (= E189), H417 (= H446), E422 (= E451)
- binding copper (ii) ion: C39 (= C44), C44 (= C49), H226 (≠ R255), H229 (≠ S258), T291 (= T322)
- binding flavin-adenine dinucleotide: F7 (≠ S14), G8 (= G15), E29 (= E36), Q30 (≠ R37), M34 (≠ W39), T38 (≠ S43), C39 (= C44), C44 (= C49), K48 (= K53), A95 (≠ G116), N117 (= N144), T118 (≠ V145), G119 (= G146), I160 (= I186), R243 (= R274), D283 (≠ E314), F290 (= F321), T291 (= T322), S294 (= S325)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
32% identity, 97% coverage: 7:458/465 of query aligns to 2:437/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G15), E31 (= E36), Q32 (≠ R37), M36 (≠ W39), G39 (= G42), T40 (≠ S43), C41 (= C44), C46 (= C49), K50 (= K53), A97 (≠ G116), N126 (= N144), T127 (≠ V145), G128 (= G146), I169 (= I186), N255 (= N277), G290 (= G313), D291 (≠ E314), Q297 (= Q320), F298 (= F321), T299 (= T322), Y300 (≠ H323), S302 (= S325)
- binding histidine: D353 (≠ A374), Y354 (≠ V375)
Sites not aligning to the query:
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
32% identity, 96% coverage: 7:453/465 of query aligns to 170:612/631 of P16171
- Y264 (≠ H100) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (≠ H446) mutation to F: 10-fold decrease in activity. 300-fold decrease in activity; when associated with F-264.; mutation to H: 2-fold decrease in activity.
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
32% identity, 97% coverage: 7:458/465 of query aligns to 5:440/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G13), G13 (= G15), E34 (= E36), Q35 (≠ R37), M39 (≠ W39), G42 (= G42), T43 (≠ S43), G48 (≠ A48), C49 (= C49), K53 (= K53), K99 (≠ S115), A100 (≠ G116), N129 (= N144), T130 (≠ V145), G131 (= G146), G293 (= G313), D294 (≠ E314), Q300 (= Q320), F301 (= F321), T302 (= T322), Y303 (≠ H323), S305 (= S325)
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
32% identity, 97% coverage: 5:453/465 of query aligns to 2:446/454 of 5x1yB
- active site: A13 (≠ Q16), V37 (= V40), C41 (= C44), C46 (= C49), S49 (= S52), A74 (≠ P77), G75 (≠ I78), Y178 (= Y185), E182 (= E189), A318 (≠ V326), A437 (≠ I444), Y439 (≠ H446), E444 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G12 (= G15), I32 (≠ V35), E33 (= E36), R34 (= R37), G39 (= G42), T40 (≠ S43), C41 (= C44), G45 (≠ A48), C46 (= C49), K50 (= K53), A114 (≠ G116), T138 (≠ V145), G139 (= G146), Y178 (= Y185), R266 (= R274), G305 (= G313), D306 (≠ E314), F313 (= F321), V314 (≠ T322), A317 (≠ S325)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
32% identity, 97% coverage: 5:453/465 of query aligns to 83:527/546 of D9J041
- C122 (= C44) modified: Disulfide link with 127, Redox-active
- C127 (= C49) modified: Disulfide link with 122, Redox-active
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
31% identity, 95% coverage: 11:453/465 of query aligns to 8:447/466 of 4k8dA
- active site: G13 (≠ Q16), I37 (≠ V40), C41 (= C44), C46 (= C49), S49 (= S52), V75 (≠ P77), P76 (≠ I78), V185 (≠ Y185), E189 (= E189), A320 (≠ V326), F438 (≠ I444), Y440 (≠ H446), E445 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G10 (= G13), G12 (= G15), A14 (≠ G17), E33 (= E36), R34 (= R37), G39 (= G42), T40 (≠ S43), C41 (= C44), G45 (≠ A48), C46 (= C49), K50 (= K53), E115 (≠ S115), A116 (≠ G116), T145 (≠ V145), G146 (= G146), R268 (= R274), G307 (= G313), D308 (≠ E314), F315 (= F321), V316 (≠ T322), Y317 (≠ H323)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ G183), S184 (≠ G184), V185 (≠ Y185), V186 (≠ I186), E189 (= E189), R206 (= R206), N207 (≠ G207), R212 (= R213), T266 (≠ A272), G267 (= G273), Q314 (= Q320), F315 (= F321), V345 (≠ T351)
Sites not aligning to the query:
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
31% identity, 95% coverage: 11:453/465 of query aligns to 103:542/561 of P00392
- A110 (≠ G18) binding
- G130 (≠ Q38) binding
- T135 (≠ S43) binding
- C136 (= C44) modified: Disulfide link with 141, Redox-active
- C141 (= C49) modified: Disulfide link with 136, Redox-active
- K145 (= K53) binding
- A211 (≠ G116) binding
- D403 (≠ E314) binding
- V411 (≠ T322) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 558 binding
- 559 binding
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
32% identity, 92% coverage: 3:430/465 of query aligns to 3:432/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (≠ Y185), E191 (= E189)
- binding flavin-adenine dinucleotide: I12 (≠ L12), G13 (= G13), G15 (= G15), P16 (≠ Q16), G17 (= G17), E36 (= E36), K37 (≠ R37), G43 (= G42), T44 (≠ S43), C45 (= C44), G49 (≠ A48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ S115), G118 (= G116), T147 (≠ V145), G148 (= G146), I188 (= I186), R276 (= R274), D316 (≠ E314), M322 (≠ Q320), L323 (≠ F321), A324 (≠ T322)
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.
31% identity, 97% coverage: 5:453/465 of query aligns to 3:458/475 of 6awaA
- active site: L45 (≠ V40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (≠ Y185), E195 (= E189), F449 (≠ I444), H451 (= H446), E456 (= E451)
- binding adenosine monophosphate: I187 (≠ L181), E211 (= E205), A212 (≠ R206), L213 (≠ G207), V245 (= V242), V277 (≠ A272)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G13 (= G15), P14 (≠ Q16), G15 (= G17), E34 (= E36), K35 (≠ R37), T48 (≠ S43), C49 (= C44), G53 (≠ A48), C54 (= C49), K58 (= K53), H121 (≠ S115), G122 (= G116), S151 (≠ V145), G152 (= G146), I192 (= I186), R279 (= R274), G318 (= G313), D319 (≠ E314), M325 (≠ Q320), L326 (≠ F321), A327 (≠ T322), Y358 (≠ F353)
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)
30% identity, 95% coverage: 8:451/465 of query aligns to 11:451/470 of P11959
- 39:47 (vs. 36:44, 44% identical) binding
- K56 (= K53) binding
- D314 (≠ E314) binding
- A322 (≠ T322) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
30% identity, 95% coverage: 8:451/465 of query aligns to 5:445/455 of 1ebdA
- active site: P13 (≠ Q16), L37 (≠ V40), C41 (= C44), C46 (= C49), S49 (= S52), N74 (≠ P77), V75 (≠ I78), Y180 (= Y185), E184 (= E189), S320 (≠ V326), H438 (≠ I444), H440 (= H446), E445 (= E451)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (≠ Q16), V32 (= V35), E33 (= E36), K34 (≠ R37), G39 (= G42), V40 (≠ S43), C41 (= C44), G45 (≠ A48), C46 (= C49), K50 (= K53), E112 (≠ S115), A113 (≠ G116), T141 (≠ V145), G142 (= G146), Y180 (= Y185), I181 (= I186), R268 (= R274), D308 (≠ E314), A314 (≠ Q320), L315 (≠ F321), A316 (≠ T322)
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
31% identity, 95% coverage: 11:453/465 of query aligns to 9:448/467 of 4k7zA
- active site: G14 (≠ Q16), I38 (≠ V40), A42 (≠ C44), A47 (≠ C49), S50 (= S52), V76 (≠ P77), P77 (≠ I78), V186 (≠ Y185), E190 (= E189), A321 (≠ V326), F439 (≠ I444), Y441 (≠ H446), E446 (= E451)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G11 (= G13), G13 (= G15), A15 (≠ G17), E34 (= E36), R35 (= R37), G40 (= G42), T41 (≠ S43), A42 (≠ C44), G46 (≠ A48), A47 (≠ C49), K51 (= K53), E116 (≠ S115), A117 (≠ G116), T146 (≠ V145), G147 (= G146), R269 (= R274), G308 (= G313), D309 (≠ E314), Q315 (= Q320), F316 (= F321), V317 (≠ T322), Y318 (≠ H323)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ G183), S185 (≠ G184), V186 (≠ Y185), V187 (≠ I186), E190 (= E189), R207 (= R206), N208 (≠ G207), R213 (= R213), T267 (≠ A272), G268 (= G273), R269 (= R274), Q315 (= Q320), F316 (= F321), V346 (≠ T351)
Sites not aligning to the query:
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
31% identity, 97% coverage: 1:453/465 of query aligns to 1:458/477 of P18925
- 34:49 (vs. 36:44, 25% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- D319 (≠ E314) binding
- A327 (≠ T322) 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)
30% identity, 97% coverage: 5:453/465 of query aligns to 2:457/472 of 3ladA
- active site: L44 (≠ V40), C48 (= C44), C53 (= C49), S56 (= S52), V190 (≠ Y185), E194 (= E189), F448 (≠ I444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G10 (= G13), G12 (= G15), P13 (≠ Q16), E33 (= E36), K34 (≠ R37), G46 (= G42), T47 (≠ S43), C48 (= C44), G52 (≠ A48), C53 (= C49), H120 (≠ S115), G121 (= G116), A149 (≠ N144), S150 (≠ V145), G151 (= G146), I191 (= I186), R278 (= R274), D318 (≠ E314), L325 (≠ F321), A326 (≠ T322)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
30% identity, 97% coverage: 5:453/465 of query aligns to 1:456/472 of 5u8vA
- active site: P12 (≠ Q16), L43 (≠ V40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (≠ P77), V82 (≠ I78), V189 (≠ Y185), E193 (= E189), S329 (≠ V326), F447 (≠ I444), H449 (= H446), E454 (= E451)
- binding flavin-adenine dinucleotide: I8 (≠ L12), G11 (= G15), P12 (≠ Q16), G13 (= G17), E32 (= E36), G45 (= G42), T46 (≠ S43), C47 (= C44), G51 (≠ A48), C52 (= C49), K56 (= K53), H119 (≠ S115), G120 (= G116), A148 (≠ N144), S149 (≠ V145), G150 (= G146), S169 (≠ H165), I190 (= I186), R277 (= R274), G316 (= G313), D317 (≠ E314), M323 (≠ Q320), L324 (≠ F321), A325 (≠ T322), H326 (= H323), H449 (= H446), P450 (≠ L447)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ L181), G186 (= G182), G188 (= G184), V189 (≠ Y185), I190 (= I186), L208 (≠ V204), E209 (= E205), A210 (≠ R206), V243 (≠ T239), V275 (≠ A272), G276 (= G273)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
31% identity, 97% coverage: 1:453/465 of query aligns to 3:460/477 of 5u8uD
- active site: P16 (≠ Q16), L47 (≠ V40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ P77), V86 (≠ I78), V193 (≠ Y185), E197 (= E189), S333 (≠ V326), F451 (≠ I444), H453 (= H446), E458 (= E451)
- binding flavin-adenine dinucleotide: I12 (≠ L12), G15 (= G15), P16 (≠ Q16), G17 (= G17), E36 (= E36), K37 (≠ R37), G49 (= G42), T50 (≠ S43), C51 (= C44), G55 (≠ A48), C56 (= C49), K60 (= K53), H123 (≠ S115), G124 (= G116), A152 (≠ N144), S153 (≠ V145), G154 (= G146), I194 (= I186), R281 (= R274), G320 (= G313), D321 (≠ E314), M327 (≠ Q320), L328 (≠ F321), A329 (≠ T322), H330 (= H323), H453 (= H446), P454 (≠ L447)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
30% identity, 97% coverage: 5:453/465 of query aligns to 2:457/473 of 5u8wA
- active site: P13 (≠ Q16), L44 (≠ V40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ P77), V83 (≠ I78), V190 (≠ Y185), E194 (= E189), S330 (≠ V326), F448 (≠ I444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G12 (= G15), P13 (≠ Q16), G14 (= G17), E33 (= E36), K34 (≠ R37), G46 (= G42), T47 (≠ S43), C48 (= C44), G52 (≠ A48), C53 (= C49), K57 (= K53), H120 (≠ S115), G121 (= G116), A149 (≠ N144), S150 (≠ V145), G151 (= G146), S170 (≠ H165), G317 (= G313), D318 (≠ E314), M324 (≠ Q320), L325 (≠ F321), A326 (≠ T322), H327 (= H323), Y357 (≠ F353), H450 (= H446), P451 (≠ L447)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ L181), G189 (= G184), V190 (≠ Y185), I191 (= I186), E194 (= E189), E210 (= E205), A211 (≠ R206), L212 (≠ G207), A275 (= A271), V276 (≠ A272), G277 (= G273), R278 (= R274), M324 (≠ Q320), L325 (≠ F321), V355 (≠ T351), Y357 (≠ F353)
Sites not aligning to the query:
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
31% identity, 97% coverage: 1:453/465 of query aligns to 1:458/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 36:44, 25% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (= G116) binding
- D319 (≠ E314) binding
- A327 (≠ T322) binding
Query Sequence
>H281DRAFT_02737 FitnessBrowser__Burk376:H281DRAFT_02737
MSQVEHFDTLILGSGQGGKLLAWHLGRSGQRVAVVERQWVGGSCPAVACLPSKNEIWSAR
VAHLARHAGDFGTTTGPIAVDMAKVRERKRGMIEREAAFHVQAYASSGAELIMGSGRFIG
PKTIAVQLNDGGTRTLAGDQVVVNVGTHAAIPDVPGLLAAGPLTHIGALDLDYAPAHLVV
LGGGYIGIEMAQAYRRFGSRVTIVERGARLMAREDVDISEEMRGILSNEGIDIVTGAETV
RVEGRSGTQVRVVLRTASGERVIEGSDILVAAGRVPNTAGIGLEQAGIELDERGYIRVND
RLQASAPGVWAIGEVAGSPQFTHVSVDDFRIVRDNLAGTDRTTTGRLVPYTLFTDPPLAR
VGLNERDALRYGIAVRVATLPMSNVLRTEATDETQGFMKVLVDAKDDRILGFSMIGPEAG
EVMASVQTAMIAELPYPKLRDAVISHLTFAEGLGPLLSKVPARAA
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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