SitesBLAST
Comparing BPHYT_RS13020 FitnessBrowser__BFirm:BPHYT_RS13020 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)
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
38% identity, 98% coverage: 5:463/466 of query aligns to 4:441/441 of 6kgyB
- active site: C43 (= C42), C48 (= C47), T51 (= T50), Y168 (= Y186), E172 (= E190), H426 (= H448), E431 (= E453)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), E33 (= E34), Q34 (≠ R35), M38 (≠ A37), G41 (= G40), T42 (= T41), G47 (= G46), C48 (= C47), A99 (= A116), N126 (= N145), T127 (= T146), G128 (= G147), G291 (= G314), D292 (= D315), F299 (= F322), T300 (= T323), Y301 (≠ H324), S303 (= S326), F333 (= F355)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
38% identity, 98% coverage: 7:463/466 of query aligns to 2:432/432 of 6kyyA
- active site: C39 (= C42), C44 (= C47), T47 (= T50), Y159 (= Y186), E163 (= E190), H417 (= H448), E422 (= E453)
- binding copper (ii) ion: C39 (= C42), C44 (= C47), H226 (≠ G256), H229 (≠ Q259), T291 (= T323)
- binding flavin-adenine dinucleotide: F7 (≠ T12), G8 (= G13), E29 (= E34), Q30 (≠ R35), M34 (≠ A37), T38 (= T41), C39 (= C42), C44 (= C47), K48 (= K51), A95 (= A116), N117 (= N145), T118 (= T146), G119 (= G147), I160 (= I187), R243 (= R275), D283 (= D315), F290 (= F322), T291 (= T323), S294 (= S326)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
32% identity, 98% coverage: 5:460/466 of query aligns to 2:437/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G13), E31 (= E34), Q32 (≠ R35), M36 (≠ A37), G39 (= G40), T40 (= T41), C41 (= C42), C46 (= C47), K50 (= K51), A97 (= A116), N126 (= N145), T127 (= T146), G128 (= G147), I169 (= I187), N255 (= N278), G290 (= G314), D291 (= D315), Q297 (≠ A321), F298 (= F322), T299 (= T323), Y300 (≠ H324), S302 (= S326)
- binding histidine: D353 (= D376), Y354 (≠ A377)
Sites not aligning to the query:
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
32% identity, 98% coverage: 5:460/466 of query aligns to 5:440/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G11), G13 (= G13), E34 (= E34), Q35 (≠ R35), M39 (≠ A37), G42 (= G40), T43 (= T41), G48 (= G46), C49 (= C47), K53 (= K51), K99 (≠ H115), A100 (= A116), N129 (= N145), T130 (= T146), G131 (= G147), G293 (= G314), D294 (= D315), Q300 (≠ A321), F301 (= F322), T302 (= T323), Y303 (≠ H324), S305 (= S326)
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
30% identity, 95% coverage: 4:447/466 of query aligns to 3:448/454 of 5x1yB
- active site: A13 (≠ Q14), V37 (≠ F38), C41 (= C42), C46 (= C47), S49 (≠ T50), A74 (≠ G75), G75 (≠ A76), Y178 (= Y186), E182 (= E190), A318 (≠ Y327), A437 (= A436), Y439 (= Y438), E444 (≠ Y443)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), I32 (= I33), E33 (= E34), R34 (= R35), G39 (= G40), T40 (= T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), A114 (= A116), T138 (= T146), G139 (= G147), Y178 (= Y186), R266 (= R275), G305 (= G314), D306 (= D315), F313 (= F322), V314 (≠ T323), A317 (≠ S326)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
30% identity, 95% coverage: 4:447/466 of query aligns to 84:529/546 of D9J041
- C122 (= C42) modified: Disulfide link with 127, Redox-active
- C127 (= C47) modified: Disulfide link with 122, Redox-active
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
32% identity, 97% coverage: 5:455/466 of query aligns to 1:452/465 of 3urhB
- active site: Y35 (≠ F38), C39 (= C42), C44 (= C47), S47 (≠ T50), V183 (≠ Y186), E187 (= E190), H443 (= H446), H445 (= H448), E450 (= E453)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (≠ Q14), G11 (= G15), E30 (= E34), K31 (vs. gap), G37 (= G40), T38 (= T41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (≠ H115), G112 (≠ A116), A140 (≠ N145), T141 (= T146), G142 (= G147), I184 (= I187), R273 (= R275), G312 (= G314), D313 (= D315), M319 (≠ F322), L320 (≠ T323), A321 (≠ H324), H322 (≠ T325)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
31% identity, 96% coverage: 6:454/466 of query aligns to 11:452/470 of P11959
- 39:47 (vs. 34:42, 44% identical) binding
- K56 (= K51) binding
- D314 (= D315) binding
- A322 (≠ T323) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
31% identity, 96% coverage: 6:454/466 of query aligns to 5:446/455 of 1ebdA
- active site: P13 (≠ Q14), L37 (≠ F38), C41 (= C42), C46 (= C47), S49 (≠ T50), N74 (≠ G75), V75 (≠ I77), Y180 (= Y186), E184 (= E190), S320 (= S326), H438 (= H446), H440 (= H448), E445 (= E453)
- binding flavin-adenine dinucleotide: G10 (= G11), G12 (= G13), P13 (≠ Q14), V32 (≠ I33), E33 (= E34), K34 (≠ R35), G39 (= G40), V40 (≠ T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E112 (≠ H115), A113 (= A116), T141 (= T146), G142 (= G147), Y180 (= Y186), I181 (= I187), R268 (= R275), D308 (= D315), A314 (= A321), L315 (≠ F322), A316 (≠ T323)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
29% identity, 97% coverage: 3:455/466 of query aligns to 5:455/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (≠ T50), V187 (≠ Y186), E191 (= E190), H448 (= H448), E453 (= E453)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (≠ Q14), G17 (= G15), E36 (= E34), K37 (≠ R35), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (≠ T50), K54 (= K51), V117 (≠ H115), G118 (≠ A116), T147 (= T146), G148 (= G147), I188 (= I187), R276 (= R275), D316 (= D315), M322 (≠ F322), L323 (≠ T323), A324 (≠ H324)
- binding zinc ion: H448 (= H448), E453 (= E453)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
32% identity, 97% coverage: 5:455/466 of query aligns to 2:441/452 of 2eq7A
- active site: P11 (≠ Q14), L36 (≠ F38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (= G75), V73 (≠ I77), V177 (≠ Y186), E181 (= E190), S314 (≠ Y327), H432 (= H446), H434 (= H448), E439 (= E453)
- binding flavin-adenine dinucleotide: G10 (= G13), P11 (≠ Q14), G12 (= G15), E31 (= E34), K32 (≠ R35), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ H115), A111 (= A116), T137 (= T146), G138 (= G147), S157 (≠ N166), I178 (= I187), R262 (= R275), Y265 (≠ N278), D302 (= D315), M308 (≠ A321), L309 (≠ F322), A310 (≠ T323), H311 (= H324), Y341 (≠ F355)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ L155), G174 (= G183), G176 (≠ S185), V177 (≠ Y186), I178 (= I187), E197 (≠ V206), Y198 (≠ R207), V231 (≠ P240), V260 (≠ T273), G261 (= G274), R262 (= R275), M308 (≠ A321), L309 (≠ F322), V339 (≠ A353)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 97% coverage: 5:455/466 of query aligns to 2:441/455 of 2yquB
- active site: P11 (≠ Q14), L36 (≠ F38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (= G75), V73 (≠ I77), V177 (≠ Y186), E181 (= E190), S314 (≠ Y327), H432 (= H446), H434 (= H448), E439 (= E453)
- binding carbonate ion: A310 (≠ T323), S314 (≠ Y327), S423 (≠ M432), D426 (= D435)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (≠ Q14), G12 (= G15), E31 (= E34), K32 (≠ R35), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ H115), A111 (= A116), T137 (= T146), G138 (= G147), I178 (= I187), Y265 (≠ N278), G301 (= G314), D302 (= D315), M308 (≠ A321), L309 (≠ F322), A310 (≠ T323), H311 (= H324)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 97% coverage: 5:455/466 of query aligns to 2:441/455 of 2yquA
- active site: P11 (≠ Q14), L36 (≠ F38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (= G75), V73 (≠ I77), V177 (≠ Y186), E181 (= E190), S314 (≠ Y327), H432 (= H446), H434 (= H448), E439 (= E453)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (≠ Q14), G12 (= G15), E31 (= E34), K32 (≠ R35), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ H115), A111 (= A116), T137 (= T146), G138 (= G147), S157 (≠ N166), I178 (= I187), Y265 (≠ N278), G301 (= G314), D302 (= D315), M308 (≠ A321), L309 (≠ F322), A310 (≠ T323)
D0VWY5 Glutathione amide reductase; GAR; EC 1.8.1.16 from Marichromatium gracile (Chromatium gracile) (see 2 papers)
33% identity, 98% coverage: 1:458/466 of query aligns to 1:447/463 of D0VWY5
- M1 (= M1) modified: Initiator methionine, Removed
- T2 (≠ P2) binding
- Q3 (= Q3) binding
- H4 (= H4) binding
- SG 14:15 (≠ QG 14:15) binding
- E34 (= E34) binding
- T41 (= T41) binding
- C42 (= C42) modified: Disulfide link with 47, Redox-active
- C47 (= C47) modified: Disulfide link with 42, Redox-active
- K50 (≠ T50) binding ; binding
- HA 113:114 (= HA 115:116) binding
- 174:180 (vs. 184:190, 57% identical) binding
- LE 197:198 (≠ RG 207:208) binding
- V230 (≠ P240) binding
- G261 (= G274) binding
- D302 (= D315) binding
- Q308 (≠ A321) binding
- QLT 308:310 (≠ AFT 321:323) binding
- V341 (≠ A353) binding
- H437 (= H448) active site, Proton acceptor; binding
Sites not aligning to the query:
- 2:463 modified: mature protein, Glutathione amide reductase
2r9zB Glutathione amide reductase from chromatium gracile (see paper)
33% identity, 98% coverage: 3:458/466 of query aligns to 2:445/453 of 2r9zB
- active site: S13 (≠ Q14), L37 (≠ F38), C41 (= C42), C46 (= C47), K49 (≠ T50), G74 (= G75), Y174 (= Y186), E178 (= E190), I312 (≠ Y327), A433 (≠ H446), H435 (= H448), E440 (= E453)
- binding flavin-adenine dinucleotide: G12 (= G13), S13 (≠ Q14), G14 (= G15), I32 (= I33), E33 (= E34), S34 (≠ R35), G39 (= G40), T40 (= T41), C41 (= C42), G45 (= G46), C46 (= C47), K49 (≠ T50), H111 (= H115), A112 (= A116), T136 (= T146), G137 (= G147), I175 (= I187), R260 (= R275), G299 (= G314), D300 (= D315), Q306 (≠ A321), L307 (≠ F322), T308 (= T323)
2rabA Structure of glutathione amide reductase from chromatium gracile in complex with NAD (see paper)
33% identity, 98% coverage: 3:458/466 of query aligns to 2:443/451 of 2rabA
- active site: S13 (≠ Q14), L37 (≠ F38), C41 (= C42), C46 (= C47), K49 (≠ T50), Y173 (= Y186), E177 (= E190), I310 (≠ Y327), A431 (≠ H446), H433 (= H448), E438 (= E453)
- binding flavin-adenine dinucleotide: G10 (= G11), G12 (= G13), S13 (≠ Q14), G14 (= G15), I32 (= I33), E33 (= E34), S34 (≠ R35), T40 (= T41), G45 (= G46), C46 (= C47), K49 (≠ T50), H110 (= H115), A111 (= A116), T135 (= T146), G136 (= G147), R258 (= R275), G297 (= G314), D298 (= D315), Q304 (≠ A321), L305 (≠ F322), T306 (= T323)
- binding nicotinamide-adenine-dinucleotide: K49 (≠ T50), I169 (≠ V182), G172 (≠ S185), Y173 (= Y186), I174 (= I187), E177 (= E190), A193 (≠ V206), L194 (≠ R207), E195 (≠ G208), V227 (≠ P240), V256 (≠ T273), G257 (= G274), Q304 (≠ A321), V337 (≠ A353)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
32% identity, 96% coverage: 8:455/466 of query aligns to 9:451/471 of 4jdrA
- active site: P15 (≠ Q14), L40 (≠ F38), C44 (= C42), C49 (= C47), S52 (≠ T50), E77 (≠ A76), P78 (≠ I77), I184 (≠ Y186), E188 (= E190), V324 (≠ Y327), H442 (= H446), H444 (= H448), E449 (= E453)
- binding flavin-adenine dinucleotide: G12 (= G11), G14 (= G13), P15 (≠ Q14), A16 (≠ G15), E35 (= E34), R36 (= R35), Y37 (vs. gap), V43 (≠ T41), C44 (= C42), G48 (= G46), C49 (= C47), K53 (= K51), L115 (≠ H115), G116 (≠ A116), A144 (≠ T146), G145 (= G147), I185 (= I187), G311 (= G314), D312 (= D315), M318 (≠ A321), L319 (≠ F322), A320 (≠ T323), H321 (= H324)
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)
32% identity, 96% coverage: 8:455/466 of query aligns to 10:452/474 of P0A9P0
- K220 (≠ D221) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
28% identity, 95% coverage: 5:447/466 of query aligns to 170:614/631 of P16171
- Y264 (≠ E100) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (= Y438) 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.
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
32% identity, 97% coverage: 1:453/466 of query aligns to 1:456/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:42, 38% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- G122 (≠ A116) binding
- D319 (= D315) binding
- A327 (≠ H324) binding
Query Sequence
>BPHYT_RS13020 FitnessBrowser__BFirm:BPHYT_RS13020
MPQHFDAVVIGTGQGGSPLAVRLAKSGRETAVIERAAFGGTCVNVGCTPTKSYVASARAA
HVARHCAELGVQVGGAISVDLAAVKARKDKIIGQSRDGVEAWLRGTQNMSVFKGHARFTG
PRALAISGPDGNLLDEISADEVFINTGTRAVVPPLDGLERIRYYTNSNLLDLTELPSHLV
IVGASYIALEFAQIFRRFGSQVTVLVRGERLLTREDADFADSVQKVLAREGVEFRFNVQP
SRVEPHPHRENEVCVGFEQNIPALEASHLLFATGREPNTDDLGLAAAGIAVDKHGTIPVD
GQLRTNVPGVWAIGDVNGRGAFTHTSYDDYQIVAANLLDGASRSVDTRIMAYAVFVDPPL
ARVGASEAEVRKSGRDALIATMPMTRVGRARERGETDGFMKVMVDKESKRVLGAAIHGIE
GDEALHTFIDIMTADAPYPTLQYAMHIHPTISELVPTLLDGLKPMK
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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