SitesBLAST
Comparing WP_079650193.1 NCBI__GCF_900167915.1:WP_079650193.1 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)
3lxdA Crystal structure of ferredoxin reductase arr from novosphingobium aromaticivorans (see paper)
70% identity, 99% coverage: 5:408/410 of query aligns to 5:408/409 of 3lxdA
- active site: H13 (= H13), R44 (= R44), P45 (= P45), N302 (= N302)
- binding flavin-adenine dinucleotide: V9 (= V9), G10 (= G10), G12 (= G12), H13 (= H13), G14 (= G14), R36 (≠ D36), E37 (= E37), R44 (= R44), P45 (= P45), S48 (= S48), K49 (= K49), E81 (≠ R81), V82 (= V82), T109 (= T109), I157 (= I156), G278 (= G278), D279 (= D279), S297 (= S297), V298 (= V298), F325 (= F325), W326 (= W326)
P16640 Putidaredoxin reductase CamA; Pdr; Putidaredoxin--NAD(+) reductase; EC 1.18.1.5 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
40% identity, 100% coverage: 2:410/410 of query aligns to 3:414/422 of P16640
- A15 (≠ G14) binding FAD
- D37 (= D36) binding FAD
- K50 (= K49) binding FAD
- V83 (= V82) binding FAD
- R134 (= R130) binding FAD
- D284 (= D279) binding FAD
- V302 (= V298) binding FAD
1q1wA Crystal structure of putidaredoxin reductase from pseudomonas putida (see paper)
40% identity, 100% coverage: 2:410/410 of query aligns to 2:413/422 of 1q1wA
- active site: L13 (≠ H13), L44 (≠ R44), P45 (= P45), L305 (≠ N302)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), L13 (≠ H13), A14 (≠ G14), G35 (= G35), D36 (= D36), L44 (≠ R44), P45 (= P45), K49 (= K49), V82 (= V82), A108 (= A108), T109 (= T109), G110 (= G110), R133 (= R130), I159 (= I156), D283 (= D279), S300 (= S297), V301 (= V298), W329 (= W326)
3fg2P Crystal structure of ferredoxin reductase for the cyp199a2 system from rhodopseudomonas palustris (see paper)
40% identity, 98% coverage: 6:405/410 of query aligns to 4:400/404 of 3fg2P
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), H11 (= H13), A12 (≠ G14), D34 (= D36), E35 (= E37), R42 (= R44), P43 (= P45), S46 (= S48), K47 (= K49), R78 (= R81), M79 (≠ V82), T106 (= T109), R127 (= R130), I153 (= I156), D275 (= D279), S292 (= S297), V293 (= V298), W321 (= W326)
8pxkA Structure of nadh-dependent ferredoxin reductase, bpha4, solved at wavelength 5.76 a (see paper)
39% identity, 98% coverage: 6:407/410 of query aligns to 7:399/403 of 8pxkA
- binding flavin-adenine dinucleotide: G13 (= G12), A15 (≠ G14), D37 (= D36), E38 (= E37), R45 (= R44), P46 (= P45), K50 (= K49), A79 (≠ V82), T106 (= T109), G107 (= G110), R127 (= R130), I153 (= I156), G269 (= G278), D270 (= D279), E286 (= E296), T287 (≠ S297), W288 (≠ V298), A291 (= A301), W317 (= W326)
1f3pA Ferredoxin reductase (bpha4)-nadh complex (see paper)
39% identity, 98% coverage: 6:407/410 of query aligns to 6:398/401 of 1f3pA
- active site: L13 (≠ H13), R44 (= R44), P45 (= P45), Q291 (≠ N302)
- binding flavin-adenine dinucleotide: A14 (≠ G14), V34 (= V34), D36 (= D36), E37 (= E37), R44 (= R44), P45 (= P45), A78 (≠ V82), T105 (= T109), G106 (= G110), R126 (= R130), G268 (= G278), D269 (= D279), E285 (= E296), T286 (≠ S297), W287 (≠ V298), A290 (= A301), W316 (= W326)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I151), G148 (= G152), G150 (= G154), V151 (≠ Y155), I152 (= I156), E155 (= E159), E171 (= E175), T172 (≠ A176), R179 (= R183), G230 (= G240), I231 (= I241), G232 (= G242), V233 (≠ I243), E285 (= E296), W316 (= W326), S317 (= S327)
2gr2A Crystal structure of ferredoxin reductase, bpha4 (oxidized form)
39% identity, 98% coverage: 6:407/410 of query aligns to 5:397/401 of 2gr2A
- active site: L12 (≠ H13), R43 (= R44), P44 (= P45), Q290 (≠ N302)
- binding adenosine-5-diphosphoribose: R109 (= R114), V146 (≠ I151), G147 (= G152), G149 (= G154), V150 (≠ Y155), I151 (= I156), E170 (= E175), T171 (≠ A176), R178 (= R183), G229 (= G240), I230 (= I241), G231 (= G242), E284 (= E296)
- binding flavin-adenine dinucleotide: G11 (= G12), A13 (≠ G14), D35 (= D36), E36 (= E37), R43 (= R44), P44 (= P45), K48 (= K49), A77 (≠ V82), T104 (= T109), G105 (= G110), R125 (= R130), G267 (= G278), D268 (= D279), T285 (≠ S297), W286 (≠ V298), A289 (= A301), W315 (= W326)
2gr0A Crystal structure of ferredoxin reductase, bpha4 (oxidized form, NAD+ complex) (see paper)
39% identity, 98% coverage: 6:407/410 of query aligns to 5:397/401 of 2gr0A
- active site: L12 (≠ H13), R43 (= R44), P44 (= P45), Q290 (≠ N302)
- binding adenosine-5'-diphosphate: V146 (≠ I151), G147 (= G152), G149 (= G154), I151 (= I156), E170 (= E175), T171 (≠ A176), R178 (= R183), G229 (= G240), I230 (= I241), G231 (= G242)
- binding flavin-adenine dinucleotide: G11 (= G12), A13 (≠ G14), D35 (= D36), E36 (= E37), R43 (= R44), P44 (= P45), K48 (= K49), T76 (≠ R81), A77 (≠ V82), T104 (= T109), G105 (= G110), R125 (= R130), I151 (= I156), G267 (= G278), D268 (= D279), E284 (= E296), T285 (≠ S297), W286 (≠ V298), A289 (= A301), W315 (= W326)
2yvjA Crystal structure of the ferredoxin-ferredoxin reductase (bpha3- bpha4)complex (see paper)
39% identity, 98% coverage: 6:407/410 of query aligns to 6:398/402 of 2yvjA
- active site: L13 (≠ H13), R44 (= R44), P45 (= P45), Q291 (≠ N302)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), G35 (= G35), D36 (= D36), E37 (= E37), R44 (= R44), P45 (= P45), A78 (≠ V82), T105 (= T109), G106 (= G110), R126 (= R130), G268 (= G278), D269 (= D279), T286 (≠ S297), W287 (≠ V298), A290 (= A301), W316 (= W326)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I151), G148 (= G152), G149 (= G153), G150 (= G154), I152 (= I156), V170 (≠ L174), E171 (= E175), T172 (≠ A176), R179 (= R183), G230 (= G240), I231 (= I241), G232 (= G242), V233 (≠ I243), E285 (= E296)
4h4uA Crystal structure of ferredoxin reductase, bpha4 t176r mutant (reduced form)
39% identity, 98% coverage: 6:407/410 of query aligns to 6:398/401 of 4h4uA
- active site: L13 (≠ H13), R44 (= R44), P45 (= P45), Q291 (≠ N302)
- binding flavin-adenine dinucleotide: G12 (= G12), A14 (≠ G14), D36 (= D36), R44 (= R44), P45 (= P45), A78 (≠ V82), T105 (= T109), G106 (= G110), L125 (≠ V129), R126 (= R130), I152 (= I156), E155 (= E159), G268 (= G278), D269 (= D279), E285 (= E296), T286 (≠ S297), W287 (≠ V298), A290 (= A301), W316 (= W326)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V151 (≠ Y155), I152 (= I156), E171 (= E175), R172 (≠ A176), Q173 (≠ L177), G230 (= G240), I231 (= I241), G232 (= G242), I284 (≠ L295), E285 (= E296), Y315 (≠ F325)
4h4wA Crystal structure of ferredoxin reductase, bpha4 e175c/t176r/q177g mutant (reduced form)
39% identity, 98% coverage: 6:407/410 of query aligns to 5:397/399 of 4h4wA
- active site: L12 (≠ H13), R43 (= R44), P44 (= P45), Q290 (≠ N302)
- binding flavin-adenine dinucleotide: G11 (= G12), A13 (≠ G14), D35 (= D36), R43 (= R44), P44 (= P45), A77 (≠ V82), T104 (= T109), G105 (= G110), R125 (= R130), I151 (= I156), E154 (= E159), G267 (= G278), D268 (= D279), T285 (≠ S297), W286 (≠ V298), A289 (= A301), W315 (= W326)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G148 (= G153), I151 (= I156), R171 (≠ A176), S177 (≠ A182), R178 (= R183), G229 (= G240), I230 (= I241), G231 (= G242)
4emjA Complex between the reductase and ferredoxin components of toluene dioxygenase (see paper)
33% identity, 99% coverage: 6:410/410 of query aligns to 5:404/406 of 4emjA
- binding flavin-adenine dinucleotide: G11 (= G12), V12 (≠ H13), G13 (= G14), D35 (= D36), E36 (= E37), R43 (= R44), P44 (= P45), S47 (= S48), K48 (= K49), V80 (= V82), T107 (= T109), G108 (= G110), R128 (= R130), G274 (= G278), D275 (= D279), T291 (≠ S297), Y292 (≠ V298), S319 (≠ F325), W320 (= W326)
4emiA Toluene dioxygenase reductase in reduced state in complex with NAD+ (see paper)
34% identity, 96% coverage: 6:399/410 of query aligns to 4:392/402 of 4emiA
- binding flavin-adenine dinucleotide: G10 (= G12), V11 (≠ H13), G12 (= G14), D34 (= D36), E35 (= E37), R42 (= R44), P43 (= P45), K47 (= K49), E78 (≠ R81), V79 (= V82), T106 (= T109), G107 (= G110), G273 (= G278), D274 (= D279), T290 (≠ S297), Y291 (≠ V298), W319 (= W326)
- binding nicotinamide-adenine-dinucleotide: R111 (= R114), G149 (= G152), L152 (≠ Y155), I153 (= I156), E156 (= E159), E172 (= E175), A173 (= A176), R180 (= R183), V236 (≠ I241), G237 (= G242), A238 (≠ I243), E289 (= E296), W319 (= W326), T320 (≠ S327)
6tukB Crystal structure of fdr9 (see paper)
33% identity, 97% coverage: 6:404/410 of query aligns to 4:390/393 of 6tukB
- binding flavin-adenine dinucleotide: V7 (= V9), G8 (= G10), G9 (≠ A11), G10 (= G12), A12 (≠ G14), A34 (≠ D36), E35 (= E37), R42 (= R44), P43 (= P45), K47 (= K49), A75 (≠ R81), A76 (≠ V82), T102 (= T109), G103 (= G110), V118 (= V129), R119 (= R130), G259 (= G278), D260 (= D279), H277 (≠ S297), W278 (≠ V298), F311 (= F325), W312 (= W326)
5jclA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
29% identity, 94% coverage: 23:407/410 of query aligns to 24:418/429 of 5jclA
- active site: R45 (= R44), P46 (= P45), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ N302)
- binding flavin-adenine dinucleotide: S36 (≠ G35), K37 (≠ D36), E38 (= E37), R45 (= R44), P46 (= P45), K50 (= K49), I93 (≠ V82), A119 (= A108), T120 (= T109), G121 (= G110), R144 (= R130), E145 (≠ T131), D295 (= D279), E311 (= E296), H312 (≠ S297), V313 (= V298), A316 (= A301), Y346 (≠ W326)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G170 (= G154), Y171 (= Y155), I172 (= I156), E175 (= E159), P192 (≠ A176), R199 (= R183), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E296), H312 (≠ S297), Y346 (≠ W326)
Sites not aligning to the query:
5jciA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
29% identity, 84% coverage: 23:368/410 of query aligns to 24:390/432 of 5jciA
- active site: R45 (= R44), P46 (= P45), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ N302)
- binding flavin-adenine dinucleotide: S36 (≠ G35), K37 (≠ D36), E38 (= E37), R45 (= R44), P46 (= P45), K50 (= K49), I93 (≠ V82), A119 (= A108), T120 (= T109), G121 (= G110), R144 (= R130), E145 (≠ T131), Y171 (= Y155), I172 (= I156), L262 (≠ A246), D295 (= D279), H312 (≠ S297), V313 (= V298), A316 (= A301), F345 (= F325), Y346 (≠ W326)
Sites not aligning to the query:
5jcnA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
29% identity, 94% coverage: 23:407/410 of query aligns to 24:418/429 of 5jcnA
- active site: R45 (= R44), P46 (= P45), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ N302)
- binding ascorbic acid: P46 (= P45), G69 (vs. gap), R317 (≠ N302), F346 (≠ W326)
- binding flavin-adenine dinucleotide: K37 (≠ D36), E38 (= E37), R45 (= R44), P46 (= P45), K50 (= K49), I93 (≠ V82), A119 (= A108), T120 (= T109), R144 (= R130), E145 (≠ T131), L262 (≠ A246), D295 (= D279), E311 (= E296), H312 (≠ S297), V313 (= V298), F346 (≠ W326)
- binding nicotinamide-adenine-dinucleotide: G170 (= G154), Y171 (= Y155), I172 (= I156), P192 (≠ A176), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E296), H312 (≠ S297), F346 (≠ W326)
Sites not aligning to the query:
5jcmA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
29% identity, 94% coverage: 23:407/410 of query aligns to 24:418/429 of 5jcmA
- active site: R45 (= R44), P46 (= P45), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ N302)
- binding flavin-adenine dinucleotide: S36 (≠ G35), K37 (≠ D36), E38 (= E37), R45 (= R44), P46 (= P45), K50 (= K49), I93 (≠ V82), A119 (= A108), T120 (= T109), G121 (= G110), R144 (= R130), E145 (≠ T131), D295 (= D279), E311 (= E296), H312 (≠ S297), V313 (= V298), A316 (= A301), F346 (≠ W326)
- binding isoascorbic acid: E44 (= E43), P46 (= P45), K50 (= K49), G69 (vs. gap), R317 (≠ N302), F346 (≠ W326)
- binding nicotinamide-adenine-dinucleotide: G170 (= G154), Y171 (= Y155), I172 (= I156), E175 (= E159), P192 (≠ A176), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E296), H312 (≠ S297), F346 (≠ W326)
Sites not aligning to the query:
Q652L6 Monodehydroascorbate reductase 3, cytosolic; OsMDAR3; OsMDHAR3; EC 1.6.5.4 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 84% coverage: 23:368/410 of query aligns to 27:393/435 of Q652L6
- E41 (= E37) binding FAD
- R48 (= R44) binding FAD
- K53 (= K49) binding FAD
- C70 (vs. gap) mutation to A: No effect on catalytic activity.; mutation to S: Slight reduction of catalytic activity.
- G72 (vs. gap) mutation to N: Slight reduction of catalytic activity.
- I96 (≠ V82) binding FAD
- RE 147:148 (≠ RT 130:131) binding FAD
- 172:178 (vs. 153:159, 100% identical) binding NAD(+)
- YIGLE 174:178 (= YIGLE 155:159) binding NADP(+)
- E196 (≠ L177) binding NAD(+); mutation to A: Reduces catalytic activity 2-fold.
- R202 (= R183) binding NAD(+); binding NADP(+)
- G261 (= G242) binding NAD(+); binding NADP(+)
- D298 (= D279) binding FAD
- EH 314:315 (≠ ES 296:297) binding NAD(+); binding NADP(+)
- V316 (= V298) binding FAD
- R320 (≠ N302) binding L-ascorbate; mutation to A: Reduces catalytic activity 5-fold.
- Y349 (≠ W326) binding FAD; binding NAD(+); binding NADP(+); mutation Y->A,F,W: Abolishes catalytic activity.
- R351 (≠ N328) binding L-ascorbate; mutation to A: No effect on catalytic activity.
Sites not aligning to the query:
Q9LK94 Monodehydroascorbate reductase 4, peroxisomal; AtMDAR4; EC 1.6.5.4 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 84% coverage: 23:368/410 of query aligns to 25:385/488 of Q9LK94
Sites not aligning to the query:
- 11 G→Q: In sdp2-2; loss of ascorbate recycling.
- 14 V→A: In sdp2-1; loss of ascorbate recycling.
- 386 G→Q: In sdp2-3; loss of ascorbate recycling.
- 483:488 mutation Missing: Loss of peroxisomal targeting.
- 488 mutation Missing: No effect on peroxisomal targeting.
Query Sequence
>WP_079650193.1 NCBI__GCF_900167915.1:WP_079650193.1
MAQYDVLIVGAGHGGAQAAVALRQNKFEGTIAIVGDEPELPYERPPLSKEYFSGEKSFDR
ILIRPATFWAERNVDMLLGKRVESVDPAGHAVTLTDGSTIGYGKLIWATGGAPRKLTCSG
HHLSGVHGVRTREDADRMLGEMERTTNVVVIGGGYIGLEAAAVLSKFGKKVTVLEALDRV
LARVAGEALSRFYEAEHRAHGVDVQLGAKVDCIVGDDQDRVTGVQMHDGTVIPADMVIVG
IGIVPAVEPLIAAGAAGGNGVDVDEYCRTSLPDIYAIGDCAMHANPFADGARIRLESVQN
ANDQATTAAKHILGGTDAYHAVPWFWSNQYDLRLQTMGLSMGYDETIVRGDPANRSFSVV
YLKNGRVLALDCVNAVKDYVQGKALVTGGVSPDKASLADPEIPLKSLLPA
Or try a new SitesBLAST search
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