SitesBLAST
Comparing WP_011320179.1 NCBI__GCF_000204075.1:WP_011320179.1 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)
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
32% identity, 95% coverage: 5:440/458 of query aligns to 171:612/631 of P16171
- Y264 (≠ I96) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (≠ H433) 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.
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
31% identity, 95% coverage: 5:440/458 of query aligns to 5:446/454 of 5x1yB
- active site: A13 (≠ Q13), V37 (≠ L37), C41 (= C41), C46 (= C46), S49 (= S49), A74 (≠ V74), G75 (vs. gap), Y178 (= Y176), E182 (= E180), A318 (≠ S312), A437 (≠ H431), Y439 (≠ H433), E444 (= E438)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), I32 (≠ F32), E33 (= E33), R34 (= R34), G39 (= G39), T40 (≠ S40), C41 (= C41), G45 (= G45), C46 (= C46), K50 (= K50), A114 (= A112), T138 (= T136), G139 (= G137), Y178 (= Y176), R266 (= R261), G305 (= G300), D306 (= D301), F313 (= F308), V314 (≠ T309), A317 (vs. gap)
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
31% identity, 95% coverage: 5:440/458 of query aligns to 86:527/546 of D9J041
- C122 (= C41) modified: Disulfide link with 127, Redox-active
- C127 (= C46) modified: Disulfide link with 122, Redox-active
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
30% identity, 98% coverage: 1:447/458 of query aligns to 1:440/441 of 6kgyB
- active site: C43 (= C41), C48 (= C46), T51 (≠ S49), Y168 (= Y176), E172 (= E180), H426 (= H433), E431 (= E438)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), E33 (= E33), Q34 (≠ R34), M38 (≠ A36), G41 (= G39), T42 (≠ S40), G47 (= G45), C48 (= C46), A99 (= A112), N126 (= N135), T127 (= T136), G128 (= G137), G291 (= G300), D292 (= D301), F299 (= F308), T300 (= T309), Y301 (≠ H310), S303 (= S312), F333 (≠ Y340)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
31% identity, 96% coverage: 3:443/458 of query aligns to 1:435/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G12), E31 (= E33), Q32 (≠ R34), M36 (vs. gap), G39 (= G39), T40 (≠ S40), C41 (= C41), C46 (= C46), K50 (= K50), A97 (= A112), N126 (= N135), T127 (= T136), G128 (= G137), I169 (= I177), N255 (= N264), G290 (= G300), D291 (= D301), Q297 (≠ A307), F298 (= F308), T299 (= T309), Y300 (≠ H310), S302 (= S312)
- binding histidine: D353 (≠ N361), Y354 (≠ A362)
Sites not aligning to the query:
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
30% identity, 96% coverage: 7:447/458 of query aligns to 3:431/432 of 6kyyA
- active site: C39 (= C41), C44 (= C46), T47 (≠ S49), Y159 (= Y176), E163 (= E180), H417 (= H433), E422 (= E438)
- binding copper (ii) ion: C39 (= C41), C44 (= C46), H226 (≠ T243), H229 (≠ G247), T291 (= T309)
- binding flavin-adenine dinucleotide: F7 (≠ S11), G8 (= G12), E29 (= E33), Q30 (≠ R34), M34 (≠ A36), T38 (≠ S40), C39 (= C41), C44 (= C46), K48 (= K50), A95 (= A112), N117 (= N135), T118 (= T136), G119 (= G137), I160 (= I177), R243 (= R261), D283 (= D301), F290 (= F308), T291 (= T309), S294 (= S312)
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
31% identity, 97% coverage: 1:443/458 of query aligns to 2:438/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), E34 (= E33), Q35 (≠ R34), M39 (vs. gap), G42 (= G39), T43 (≠ S40), G48 (= G45), C49 (= C46), K53 (= K50), K99 (≠ E111), A100 (= A112), N129 (= N135), T130 (= T136), G131 (= G137), G293 (= G300), D294 (= D301), Q300 (≠ A307), F301 (= F308), T302 (= T309), Y303 (≠ H310), S305 (= S312)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
32% identity, 96% coverage: 5:444/458 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ L37), C39 (= C41), C44 (= C46), S47 (= S49), V183 (≠ Y176), E187 (= E180), H443 (= H431), H445 (= H433), E450 (= E438)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (≠ Q13), G11 (= G14), E30 (= E33), K31 (vs. gap), G37 (= G39), T38 (≠ S40), C39 (= C41), G43 (= G45), C44 (= C46), K48 (= K50), T111 (≠ E111), G112 (≠ A112), A140 (≠ N135), T141 (= T136), G142 (= G137), I184 (= I177), R273 (= R261), G312 (= G300), D313 (= D301), M319 (≠ A307), L320 (≠ F308), A321 (≠ T309), H322 (= H310)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 96% coverage: 5:444/458 of query aligns to 3:445/455 of 2yquB
- active site: P11 (≠ Q13), L36 (= L37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (vs. gap), V73 (= V74), V177 (≠ Y176), E181 (= E180), S314 (≠ W313), H432 (= H431), H434 (= H433), E439 (= E438)
- binding carbonate ion: A310 (≠ T309), S314 (≠ W313), S423 (≠ T422), D426 (≠ L425)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (≠ Q13), G12 (= G14), E31 (= E33), K32 (≠ R34), G38 (= G39), T39 (≠ S40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (≠ E111), A111 (= A112), T137 (= T136), G138 (= G137), I178 (= I177), Y265 (≠ N264), G301 (= G300), D302 (= D301), M308 (≠ A307), L309 (≠ F308), A310 (≠ T309), H311 (= H310)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
32% identity, 96% coverage: 5:444/458 of query aligns to 3:445/455 of 2yquA
- active site: P11 (≠ Q13), L36 (= L37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (vs. gap), V73 (= V74), V177 (≠ Y176), E181 (= E180), S314 (≠ W313), H432 (= H431), H434 (= H433), E439 (= E438)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (≠ Q13), G12 (= G14), E31 (= E33), K32 (≠ R34), G38 (= G39), T39 (≠ S40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (≠ E111), A111 (= A112), T137 (= T136), G138 (= G137), S157 (≠ N156), I178 (= I177), Y265 (≠ N264), G301 (= G300), D302 (= D301), M308 (≠ A307), L309 (≠ F308), A310 (≠ T309)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
32% identity, 96% coverage: 5:444/458 of query aligns to 3:445/452 of 2eq7A
- active site: P11 (≠ Q13), L36 (= L37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (vs. gap), V73 (= V74), V177 (≠ Y176), E181 (= E180), S314 (≠ W313), H432 (= H431), H434 (= H433), E439 (= E438)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (≠ Q13), G12 (= G14), E31 (= E33), K32 (≠ R34), G38 (= G39), T39 (≠ S40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (≠ E111), A111 (= A112), T137 (= T136), G138 (= G137), S157 (≠ N156), I178 (= I177), R262 (= R261), Y265 (≠ N264), D302 (= D301), M308 (≠ A307), L309 (≠ F308), A310 (≠ T309), H311 (= H310), Y341 (= Y340)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I145), G174 (= G173), G176 (= G175), V177 (≠ Y176), I178 (= I177), E197 (≠ V196), Y198 (≠ R197), V231 (= V230), V260 (≠ I259), G261 (= G260), R262 (= R261), M308 (≠ A307), L309 (≠ F308), V339 (≠ A338)
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)
32% identity, 98% coverage: 6:452/458 of query aligns to 20:457/459 of P09063
- 36:44 (vs. 33:41, 67% identical) binding FAD
- C44 (= C41) modified: Disulfide link with 49, Redox-active
- C49 (= C46) modified: Disulfide link with 44, Redox-active
- K53 (= K50) binding FAD
- A119 (= A112) binding FAD
- A142 (≠ N135) binding FAD
- GGGYI 179:183 (= GGGYI 173:177) binding NAD(+)
- Y182 (= Y176) binding FAD
- E202 (≠ V196) binding NAD(+)
- V236 (= V230) binding NAD(+)
- AVGR 264:267 (≠ VIGR 258:261) binding NAD(+)
- D306 (= D301) binding FAD
- M312 (≠ A307) binding NAD(+)
- A314 (≠ T309) binding FAD
1lvlA The refined structure of pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 angstroms resolution (see paper)
32% identity, 98% coverage: 6:452/458 of query aligns to 19:456/458 of 1lvlA
- active site: L39 (= L37), C43 (= C41), C48 (= C46), S51 (= S49), S79 (≠ E73), P80 (≠ V74), Y181 (= Y176), E185 (= E180), M317 (≠ W313), H435 (= H431), H437 (= H433), E442 (= E438)
- binding flavin-adenine dinucleotide: E35 (= E33), G36 (≠ R34), G41 (= G39), T42 (≠ S40), C43 (= C41), G47 (= G45), C48 (= C46), K52 (= K50), W117 (≠ E111), A118 (= A112), A141 (≠ N135), T142 (= T136), G143 (= G137), Y181 (= Y176), R266 (= R261), R269 (≠ N264), D305 (= D301), L312 (≠ F308), A313 (≠ T309), H314 (= H310)
- binding nicotinamide-adenine-dinucleotide: V177 (≠ I172), G178 (= G173), Y181 (= Y176), I182 (= I177), E201 (≠ V196), A263 (≠ V258), V264 (≠ I259), G265 (= G260), R266 (= R261), E309 (≠ Q305), M311 (≠ A307)
Sites not aligning to the query:
8uubA Structure of hypothiocyanous acid reductase (har) from streptococcus pneumoniae (see paper)
30% identity, 97% coverage: 1:443/458 of query aligns to 5:439/442 of 8uubA
- binding flavin-adenine dinucleotide: G14 (= G10), G16 (= G12), E37 (= E33), R38 (= R34), M42 (vs. gap), G45 (= G39), T46 (≠ S40), G51 (= G45), C52 (= C46), K56 (= K50), E101 (= E111), A102 (= A112), N129 (= N135), T130 (= T136), G131 (= G137), I172 (= I177), R255 (= R261), G294 (= G300), D295 (= D301), Q301 (≠ A307), F302 (= F308), T303 (= T309), Y304 (≠ H310), S306 (= S312)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
32% identity, 96% coverage: 1:440/458 of query aligns to 1:444/460 of 2eq6A
- active site: V37 (≠ L37), C41 (= C41), C46 (= C46), T49 (≠ S49), A176 (≠ Y176), E180 (= E180), H435 (= H431), H437 (= H433), E442 (= E438)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (≠ Q13), G14 (= G14), E33 (= E33), A34 (≠ R34), G39 (= G39), V40 (≠ S40), C41 (= C41), G45 (= G45), C46 (= C46), K50 (= K50), F111 (≠ E111), A112 (= A112), A135 (≠ N135), T136 (= T136), G137 (= G137), S155 (≠ T155), R269 (≠ N264), D306 (= D301), L312 (≠ A307), L313 (≠ F308), A314 (≠ T309), H315 (= H310), Y344 (= Y340)
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)
29% identity, 97% coverage: 5:449/458 of query aligns to 11:462/470 of P11959
- 39:47 (vs. 33:41, 56% identical) binding FAD
- K56 (= K50) binding FAD
- D314 (= D301) binding FAD
- A322 (≠ T309) binding FAD
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)
31% identity, 95% coverage: 5:440/458 of query aligns to 5:457/472 of 3ladA
- active site: L44 (= L37), C48 (= C41), C53 (= C46), S56 (= S49), V190 (≠ Y176), E194 (= E180), F448 (≠ H431), H450 (= H433), E455 (= E438)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (≠ Q13), E33 (= E33), K34 (≠ R34), G46 (= G39), T47 (≠ S40), C48 (= C41), G52 (= G45), C53 (= C46), H120 (≠ E111), G121 (≠ A112), A149 (≠ N135), S150 (≠ T136), G151 (= G137), I191 (= I177), R278 (= R261), D318 (= D301), L325 (≠ F308), A326 (≠ T309)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
31% identity, 95% coverage: 5:440/458 of query aligns to 6:458/477 of P18925
- 34:49 (vs. 33:41, 38% identical) binding FAD
- C49 (= C41) modified: Disulfide link with 54, Redox-active
- C54 (= C46) modified: Disulfide link with 49, Redox-active
- K58 (= K50) binding FAD
- D319 (= D301) binding FAD
- A327 (≠ T309) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
29% identity, 97% coverage: 5:448/458 of query aligns to 5:455/455 of 1ebdA
- active site: P13 (≠ Q13), L37 (= L37), C41 (= C41), C46 (= C46), S49 (= S49), N74 (vs. gap), V75 (= V74), Y180 (= Y176), E184 (= E180), S320 (≠ W313), H438 (= H431), H440 (= H433), E445 (= E438)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), P13 (≠ Q13), V32 (≠ F32), E33 (= E33), K34 (≠ R34), G39 (= G39), V40 (≠ S40), C41 (= C41), G45 (= G45), C46 (= C46), K50 (= K50), E112 (= E111), A113 (= A112), T141 (= T136), G142 (= G137), Y180 (= Y176), I181 (= I177), R268 (= R261), D308 (= D301), A314 (= A307), L315 (≠ F308), A316 (≠ T309)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
32% identity, 97% coverage: 1:444/458 of query aligns to 4:459/470 of 6uziC
- active site: C45 (= C41), C50 (= C46), S53 (= S49), V187 (≠ Y176), E191 (= E180), H448 (= H433), E453 (= E438)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (≠ Q13), G17 (= G14), E36 (= E33), K37 (≠ R34), G43 (= G39), T44 (≠ S40), C45 (= C41), G49 (= G45), C50 (= C46), S53 (= S49), K54 (= K50), V117 (≠ E111), G118 (≠ A112), T147 (= T136), G148 (= G137), I188 (= I177), R276 (= R261), D316 (= D301), M322 (≠ A307), L323 (≠ F308), A324 (≠ T309)
- binding zinc ion: H448 (= H433), E453 (= E438)
Query Sequence
>WP_011320179.1 NCBI__GCF_000204075.1:WP_011320179.1
METADVIVIGSGQGGIPLAADFANEGRKVVLFERDALGGSCINYGCTPSKAFLAAAHTAG
RANQGKKLGIHTEVEVDFPAVMERVREIRSSFNQGIRQRLESAGVKVICAEASFVGERTV
KGGDVTLQAPLVIINTGTSSLIPDIPGLAGTPYLTNRNFFDLNTLPARLLVIGGGYIGLE
LGQGLARLGSQTHLIVRGDRVLGQEEADVSEVLAEALKQDGIGLHFGVNVNHVAHENNVF
KLTLSSGEQLQGEALLVVIGRKPNTGALNAANSGIELDDKGFVKIDDQFHTTCSGVYAIG
DAAKQPAFTHVSWEDYRRLKAILCGENRTRSDRVLGYAVYTEPQVGRVGMTLEQAQKQGI
NACAVTLPMSQIARAIEWGHDLGFYRMVIDSDTDKILGATLVGYETAELVHVFLSLIEAG
ATWQLLERSVHIHPTYGEALPSLARLLLGDNMPGCPNM
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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