SitesBLAST
Comparing Pf6N2E2_1861 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1861 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)
P16640 Putidaredoxin reductase CamA; Pdr; Putidaredoxin--NAD(+) reductase; EC 1.18.1.5 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
50% identity, 99% coverage: 5:410/411 of query aligns to 4:415/422 of P16640
- A15 (= A16) binding
- D37 (= D38) binding
- K50 (= K51) binding
- V83 (= V84) binding
- R134 (= R132) binding
- D284 (= D279) binding
- V302 (= V297) binding
1q1wA Crystal structure of putidaredoxin reductase from pseudomonas putida (see paper)
50% identity, 99% coverage: 5:410/411 of query aligns to 3:414/422 of 1q1wA
- active site: L13 (≠ H15), L44 (≠ R46), P45 (= P47), L305 (≠ Q301)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), L13 (≠ H15), A14 (= A16), G35 (= G37), D36 (= D38), L44 (≠ R46), P45 (= P47), K49 (= K51), V82 (= V84), A108 (= A110), T109 (= T111), G110 (= G112), R133 (= R132), I159 (= I158), D283 (= D279), S300 (= S296), V301 (= V297), W329 (= W325)
3lxdA Crystal structure of ferredoxin reductase arr from novosphingobium aromaticivorans (see paper)
48% identity, 94% coverage: 24:408/411 of query aligns to 22:409/409 of 3lxdA
- active site: R44 (= R46), P45 (= P47), N302 (≠ Q301)
- binding flavin-adenine dinucleotide: R36 (≠ D38), E37 (= E39), R44 (= R46), P45 (= P47), S48 (= S50), K49 (= K51), E81 (≠ Q83), V82 (= V84), T109 (= T111), I157 (= I158), G278 (= G278), D279 (= D279), S297 (= S296), V298 (= V297), F325 (= F324), W326 (= W325)
Sites not aligning to the query:
3fg2P Crystal structure of ferredoxin reductase for the cyp199a2 system from rhodopseudomonas palustris (see paper)
43% identity, 98% coverage: 5:408/411 of query aligns to 1:404/404 of 3fg2P
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), H11 (= H15), A12 (= A16), D34 (= D38), E35 (= E39), R42 (= R46), P43 (= P47), S46 (= S50), K47 (= K51), R78 (≠ Q83), M79 (≠ V84), T106 (= T111), R127 (= R132), I153 (= I158), D275 (= D279), S292 (= S296), V293 (= V297), W321 (= W325)
2yvjA Crystal structure of the ferredoxin-ferredoxin reductase (bpha3-bpha4)complex (see paper)
40% identity, 98% coverage: 9:409/411 of query aligns to 7:401/402 of 2yvjA
- active site: L13 (≠ H15), R44 (= R46), P45 (= P47), Q291 (= Q301)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), G35 (= G37), D36 (= D38), E37 (= E39), R44 (= R46), P45 (= P47), A78 (≠ V84), T105 (= T111), G106 (= G112), R126 (= R132), G268 (= G278), D269 (= D279), T286 (≠ S296), W287 (≠ V297), A290 (= A300), W316 (= W325)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I153), G148 (= G154), G149 (= G155), G150 (= G156), I152 (= I158), V170 (≠ L176), E171 (= E177), T172 (≠ A178), R179 (= R185), G230 (= G240), I231 (= I241), G232 (= G242), V233 (≠ I243), E285 (= E295)
1f3pA Ferredoxin reductase (bpha4)-nadh complex (see paper)
40% identity, 98% coverage: 9:409/411 of query aligns to 7:401/401 of 1f3pA
- active site: L13 (≠ H15), R44 (= R46), P45 (= P47), Q291 (= Q301)
- binding flavin-adenine dinucleotide: A14 (= A16), V34 (≠ I36), D36 (= D38), E37 (= E39), R44 (= R46), P45 (= P47), A78 (≠ V84), T105 (= T111), G106 (= G112), R126 (= R132), G268 (= G278), D269 (= D279), E285 (= E295), T286 (≠ S296), W287 (≠ V297), A290 (= A300), W316 (= W325)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I153), G148 (= G154), G150 (= G156), V151 (≠ Y157), I152 (= I158), E155 (= E161), E171 (= E177), T172 (≠ A178), R179 (= R185), G230 (= G240), I231 (= I241), G232 (= G242), V233 (≠ I243), E285 (= E295), W316 (= W325), S317 (= S326)
8pxkA Structure of nadh-dependent ferredoxin reductase, bpha4, solved at wavelength 5.76 a (see paper)
40% identity, 98% coverage: 9:409/411 of query aligns to 8:402/403 of 8pxkA
- binding flavin-adenine dinucleotide: G13 (= G14), A15 (= A16), D37 (= D38), E38 (= E39), R45 (= R46), P46 (= P47), K50 (= K51), A79 (≠ V84), T106 (= T111), G107 (= G112), R127 (= R132), I153 (= I158), G269 (= G278), D270 (= D279), E286 (= E295), T287 (≠ S296), W288 (≠ V297), A291 (= A300), W317 (= W325)
2gr2A Crystal structure of ferredoxin reductase, bpha4 (oxidized form)
40% identity, 98% coverage: 9:409/411 of query aligns to 6:400/401 of 2gr2A
- active site: L12 (≠ H15), R43 (= R46), P44 (= P47), Q290 (= Q301)
- binding adenosine-5-diphosphoribose: R109 (= R116), V146 (≠ I153), G147 (= G154), G149 (= G156), V150 (≠ Y157), I151 (= I158), E170 (= E177), T171 (≠ A178), R178 (= R185), G229 (= G240), I230 (= I241), G231 (= G242), E284 (= E295)
- binding flavin-adenine dinucleotide: G11 (= G14), A13 (= A16), D35 (= D38), E36 (= E39), R43 (= R46), P44 (= P47), K48 (= K51), A77 (≠ V84), T104 (= T111), G105 (= G112), R125 (= R132), G267 (= G278), D268 (= D279), T285 (≠ S296), W286 (≠ V297), A289 (= A300), W315 (= W325)
2gr0A Crystal structure of ferredoxin reductase, bpha4 (oxidized form, NAD+ complex) (see paper)
40% identity, 98% coverage: 9:409/411 of query aligns to 6:400/401 of 2gr0A
- active site: L12 (≠ H15), R43 (= R46), P44 (= P47), Q290 (= Q301)
- binding adenosine-5'-diphosphate: V146 (≠ I153), G147 (= G154), G149 (= G156), I151 (= I158), E170 (= E177), T171 (≠ A178), R178 (= R185), G229 (= G240), I230 (= I241), G231 (= G242)
- binding flavin-adenine dinucleotide: G11 (= G14), A13 (= A16), D35 (= D38), E36 (= E39), R43 (= R46), P44 (= P47), K48 (= K51), T76 (≠ Q83), A77 (≠ V84), T104 (= T111), G105 (= G112), R125 (= R132), I151 (= I158), G267 (= G278), D268 (= D279), E284 (= E295), T285 (≠ S296), W286 (≠ V297), A289 (= A300), W315 (= W325)
4h4uA Crystal structure of ferredoxin reductase, bpha4 t176r mutant (reduced form)
40% identity, 98% coverage: 9:409/411 of query aligns to 7:401/401 of 4h4uA
- active site: L13 (≠ H15), R44 (= R46), P45 (= P47), Q291 (= Q301)
- binding flavin-adenine dinucleotide: G12 (= G14), A14 (= A16), D36 (= D38), R44 (= R46), P45 (= P47), A78 (≠ V84), T105 (= T111), G106 (= G112), L125 (≠ I131), R126 (= R132), I152 (= I158), E155 (= E161), G268 (= G278), D269 (= D279), E285 (= E295), T286 (≠ S296), W287 (≠ V297), A290 (= A300), W316 (= W325)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V151 (≠ Y157), I152 (= I158), E171 (= E177), R172 (≠ A178), Q173 (≠ A179), G230 (= G240), I231 (= I241), G232 (= G242), I284 (= I294), E285 (= E295), Y315 (≠ F324)
4h4wA Crystal structure of ferredoxin reductase, bpha4 e175c/t176r/q177g mutant (reduced form)
40% identity, 97% coverage: 9:408/411 of query aligns to 6:399/399 of 4h4wA
- active site: L12 (≠ H15), R43 (= R46), P44 (= P47), Q290 (= Q301)
- binding flavin-adenine dinucleotide: G11 (= G14), A13 (= A16), D35 (= D38), R43 (= R46), P44 (= P47), A77 (≠ V84), T104 (= T111), G105 (= G112), R125 (= R132), I151 (= I158), E154 (= E161), G267 (= G278), D268 (= D279), T285 (≠ S296), W286 (≠ V297), A289 (= A300), W315 (= W325)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G148 (= G155), I151 (= I158), R171 (≠ A178), S177 (≠ A184), R178 (= R185), G229 (= G240), I230 (= I241), G231 (= G242)
4emjA Complex between the reductase and ferredoxin components of toluene dioxygenase (see paper)
38% identity, 97% coverage: 10:409/411 of query aligns to 7:404/406 of 4emjA
- binding flavin-adenine dinucleotide: G11 (= G14), V12 (≠ H15), G13 (≠ A16), D35 (= D38), E36 (= E39), R43 (= R46), P44 (= P47), S47 (= S50), K48 (= K51), V80 (= V84), T107 (= T111), G108 (= G112), R128 (= R132), G274 (= G278), D275 (= D279), T291 (≠ S296), Y292 (≠ V297), S319 (≠ F324), W320 (= W325)
4emiA Toluene dioxygenase reductase in reduced state in complex with NAD+ (see paper)
38% identity, 97% coverage: 10:407/411 of query aligns to 6:401/402 of 4emiA
- binding flavin-adenine dinucleotide: G10 (= G14), V11 (≠ H15), G12 (≠ A16), D34 (= D38), E35 (= E39), R42 (= R46), P43 (= P47), K47 (= K51), E78 (≠ Q83), V79 (= V84), T106 (= T111), G107 (= G112), G273 (= G278), D274 (= D279), T290 (≠ S296), Y291 (≠ V297), W319 (= W325)
- binding nicotinamide-adenine-dinucleotide: R111 (= R116), G149 (= G154), L152 (≠ Y157), I153 (= I158), E156 (= E161), E172 (= E177), A173 (= A178), R180 (= R185), V236 (≠ I241), G237 (= G242), A238 (≠ I243), E289 (= E295), W319 (= W325), T320 (≠ S326)
6tukB Crystal structure of fdr9 (see paper)
32% identity, 97% coverage: 6:403/411 of query aligns to 2:390/393 of 6tukB
- binding flavin-adenine dinucleotide: V7 (= V11), G8 (= G12), G9 (≠ A13), G10 (= G14), A12 (= A16), A34 (≠ D38), E35 (= E39), R42 (= R46), P43 (= P47), K47 (= K51), A75 (≠ Q83), A76 (≠ V84), T102 (= T111), G103 (= G112), V118 (≠ I131), R119 (= R132), G259 (= G278), D260 (= D279), H277 (≠ S296), W278 (≠ V297), F311 (= F324), W312 (= W325)
Q9LK94 Monodehydroascorbate reductase 4, peroxisomal; AtMDAR4; EC 1.6.5.4 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
35% identity, 81% coverage: 31:364/411 of query aligns to 31:382/488 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.
5jclA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
30% identity, 83% coverage: 25:367/411 of query aligns to 24:390/429 of 5jclA
- active site: R45 (= R46), P46 (= P47), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ Q301)
- binding flavin-adenine dinucleotide: S36 (≠ G37), K37 (≠ D38), E38 (= E39), R45 (= R46), P46 (= P47), K50 (= K51), I93 (≠ V84), A119 (= A110), T120 (= T111), G121 (= G112), R144 (= R132), E145 (≠ N133), D295 (= D279), E311 (= E295), H312 (≠ S296), V313 (= V297), A316 (= A300), Y346 (≠ W325)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G170 (= G156), Y171 (= Y157), I172 (= I158), E175 (= E161), P192 (≠ A178), R199 (= R185), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E295), H312 (≠ S296), Y346 (≠ W325)
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)
30% identity, 83% coverage: 25:367/411 of query aligns to 27:393/435 of Q652L6
- E41 (= E39) binding
- R48 (= R46) binding
- K53 (= K51) binding
- 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 (≠ V84) binding
- RE 147:148 (≠ RN 132:133) binding
- 172:178 (vs. 155:161, 100% identical) binding
- YIGLE 174:178 (= YIGLE 157:161) binding
- E196 (≠ A179) binding ; mutation to A: Reduces catalytic activity 2-fold.
- R202 (= R185) binding ; binding
- G261 (= G242) binding ; binding
- D298 (= D279) binding
- EH 314:315 (≠ ES 295:296) binding ; binding
- V316 (= V297) binding
- R320 (≠ Q301) binding ; mutation to A: Reduces catalytic activity 5-fold.
- Y349 (≠ W325) binding ; binding ; binding ; mutation Y->A,F,W: Abolishes catalytic activity.
- R351 (≠ D327) binding ; mutation to A: No effect on catalytic activity.
Sites not aligning to the query:
5jciA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
30% identity, 83% coverage: 25:367/411 of query aligns to 24:390/432 of 5jciA
- active site: R45 (= R46), P46 (= P47), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ Q301)
- binding flavin-adenine dinucleotide: S36 (≠ G37), K37 (≠ D38), E38 (= E39), R45 (= R46), P46 (= P47), K50 (= K51), I93 (≠ V84), A119 (= A110), T120 (= T111), G121 (= G112), R144 (= R132), E145 (≠ N133), Y171 (= Y157), I172 (= I158), L262 (≠ N246), D295 (= D279), H312 (≠ S296), V313 (= V297), A316 (= A300), F345 (= F324), Y346 (≠ W325)
Sites not aligning to the query:
5jcnA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
30% identity, 83% coverage: 25:367/411 of query aligns to 24:390/429 of 5jcnA
- active site: R45 (= R46), P46 (= P47), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ Q301)
- binding ascorbic acid: P46 (= P47), G69 (vs. gap), R317 (≠ Q301), F346 (≠ W325)
- binding flavin-adenine dinucleotide: K37 (≠ D38), E38 (= E39), R45 (= R46), P46 (= P47), K50 (= K51), I93 (≠ V84), A119 (= A110), T120 (= T111), R144 (= R132), E145 (≠ N133), L262 (≠ N246), D295 (= D279), E311 (= E295), H312 (≠ S296), V313 (= V297), F346 (≠ W325)
- binding nicotinamide-adenine-dinucleotide: G170 (= G156), Y171 (= Y157), I172 (= I158), P192 (≠ A178), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E295), H312 (≠ S296), F346 (≠ W325)
Sites not aligning to the query:
5jcmA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
30% identity, 83% coverage: 25:367/411 of query aligns to 24:390/429 of 5jcmA
- active site: R45 (= R46), P46 (= P47), L61 (vs. gap), H65 (vs. gap), S70 (vs. gap), R317 (≠ Q301)
- binding flavin-adenine dinucleotide: S36 (≠ G37), K37 (≠ D38), E38 (= E39), R45 (= R46), P46 (= P47), K50 (= K51), I93 (≠ V84), A119 (= A110), T120 (= T111), G121 (= G112), R144 (= R132), E145 (≠ N133), D295 (= D279), E311 (= E295), H312 (≠ S296), V313 (= V297), A316 (= A300), F346 (≠ W325)
- binding isoascorbic acid: E44 (≠ R45), P46 (= P47), K50 (= K51), G69 (vs. gap), R317 (≠ Q301), F346 (≠ W325)
- binding nicotinamide-adenine-dinucleotide: G170 (= G156), Y171 (= Y157), I172 (= I158), E175 (= E161), P192 (≠ A178), G256 (= G240), V257 (≠ I241), G258 (= G242), E311 (= E295), H312 (≠ S296), F346 (≠ W325)
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_1861 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1861
MYPQNETAVIVGAGHAGAELVATLRQNGYPGRIILIGDEPELPYRRPPLSKTYLSGEASR
ESLLIRSAAAYDKLQVACWTGVQVCAIDRERRTVTLSDGRTQAYDKLVLATGGRPRRLEE
PAAQKPNVHYIRNLADIERLQPDFVAGKRLLVIGGGYIGLEAASVGIKNGLQVTVLEAAP
RVLARVAAPEISAFYEGVHRRRGVDVRTETSVQVFQGAERVESVQLSDGSELPVDLIIVG
IGILPNDQLARDAGLEIDNGIVVDSYAQTLDPDILAVGDCARHVNGFLGCLIRIESVPSA
QEQARTAAHTICGKNLPHIAVPWFWSDQFDLKLQMVGLSQGYDQLVLRGDMAAESFCAFY
LRKGVVLSVDAVNRPQDFMVGKRLVAERVQVDPQVLADESIDLKSLLAAAL
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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