SitesBLAST
Comparing GFF2177 FitnessBrowser__WCS417:GFF2177 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)
38% identity, 99% coverage: 2:397/399 of query aligns to 4:412/422 of P16640
- A15 (= A13) binding
- D37 (= D35) binding
- K50 (= K48) binding
- V83 (= V81) binding
- R134 (= R126) binding
- D284 (= D269) binding
- V302 (≠ W285) binding
1q1wA Crystal structure of putidaredoxin reductase from pseudomonas putida (see paper)
38% identity, 99% coverage: 2:397/399 of query aligns to 3:411/422 of 1q1wA
- active site: L13 (≠ H12), L44 (≠ R43), P45 (= P44), L305 (≠ E289)
- binding flavin-adenine dinucleotide: G10 (= G9), G12 (= G11), L13 (≠ H12), A14 (= A13), G35 (= G34), D36 (= D35), L44 (≠ R43), P45 (= P44), K49 (= K48), V82 (= V81), A108 (= A107), T109 (= T108), G110 (= G109), R133 (= R126), I159 (= I152), D283 (= D269), S300 (≠ T284), V301 (≠ W285), W329 (= W313)
3fg2P Crystal structure of ferredoxin reductase for the cyp199a2 system from rhodopseudomonas palustris (see paper)
43% identity, 81% coverage: 2:326/399 of query aligns to 1:334/404 of 3fg2P
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), H11 (= H12), A12 (= A13), D34 (= D35), E35 (= E36), R42 (= R43), P43 (= P44), S46 (= S47), K47 (= K48), R78 (≠ N79), M79 (≠ P80), T106 (= T108), R127 (= R126), I153 (= I152), D275 (= D269), S292 (≠ T284), V293 (≠ W285), W321 (= W313)
1f3pA Ferredoxin reductase (bpha4)-nadh complex (see paper)
38% identity, 99% coverage: 1:396/399 of query aligns to 2:398/401 of 1f3pA
- active site: L13 (≠ H12), R44 (= R43), P45 (= P44), Q291 (≠ E289)
- binding flavin-adenine dinucleotide: A14 (= A13), V34 (≠ I33), D36 (= D35), E37 (= E36), R44 (= R43), P45 (= P44), A78 (≠ V81), T105 (= T108), G106 (= G109), R126 (= R126), G268 (= G268), D269 (= D269), E285 (= E283), T286 (= T284), W287 (= W285), A290 (= A288), W316 (= W313)
- binding nicotinamide-adenine-dinucleotide: V147 (= V147), G148 (= G148), G150 (= G150), V151 (≠ F151), I152 (= I152), E155 (= E155), E171 (= E171), T172 (≠ A172), R179 (= R179), G230 (= G230), I231 (= I231), G232 (= G232), V233 (≠ M233), E285 (= E283), W316 (= W313), S317 (= S314)
2yvjA Crystal structure of the ferredoxin-ferredoxin reductase (bpha3-bpha4)complex (see paper)
38% identity, 99% coverage: 1:396/399 of query aligns to 2:398/402 of 2yvjA
- active site: L13 (≠ H12), R44 (= R43), P45 (= P44), Q291 (≠ E289)
- binding flavin-adenine dinucleotide: G10 (= G9), G12 (= G11), G35 (= G34), D36 (= D35), E37 (= E36), R44 (= R43), P45 (= P44), A78 (≠ V81), T105 (= T108), G106 (= G109), R126 (= R126), G268 (= G268), D269 (= D269), T286 (= T284), W287 (= W285), A290 (= A288), W316 (= W313)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (= V147), G148 (= G148), G149 (= G149), G150 (= G150), I152 (= I152), V170 (≠ L170), E171 (= E171), T172 (≠ A172), R179 (= R179), G230 (= G230), I231 (= I231), G232 (= G232), V233 (≠ M233), E285 (= E283)
8pxkA Structure of nadh-dependent ferredoxin reductase, bpha4, solved at wavelength 5.76 a (see paper)
38% identity, 99% coverage: 1:396/399 of query aligns to 3:399/403 of 8pxkA
- binding flavin-adenine dinucleotide: G13 (= G11), A15 (= A13), D37 (= D35), E38 (= E36), R45 (= R43), P46 (= P44), K50 (= K48), A79 (≠ V81), T106 (= T108), G107 (= G109), R127 (= R126), I153 (= I152), G269 (= G268), D270 (= D269), E286 (= E283), T287 (= T284), W288 (= W285), A291 (= A288), W317 (= W313)
2gr2A Crystal structure of ferredoxin reductase, bpha4 (oxidized form)
38% identity, 99% coverage: 1:396/399 of query aligns to 1:397/401 of 2gr2A
- active site: L12 (≠ H12), R43 (= R43), P44 (= P44), Q290 (≠ E289)
- binding adenosine-5-diphosphoribose: R109 (= R113), V146 (= V147), G147 (= G148), G149 (= G150), V150 (≠ F151), I151 (= I152), E170 (= E171), T171 (≠ A172), R178 (= R179), G229 (= G230), I230 (= I231), G231 (= G232), E284 (= E283)
- binding flavin-adenine dinucleotide: G11 (= G11), A13 (= A13), D35 (= D35), E36 (= E36), R43 (= R43), P44 (= P44), K48 (= K48), A77 (≠ V81), T104 (= T108), G105 (= G109), R125 (= R126), G267 (= G268), D268 (= D269), T285 (= T284), W286 (= W285), A289 (= A288), W315 (= W313)
2gr0A Crystal structure of ferredoxin reductase, bpha4 (oxidized form, NAD+ complex) (see paper)
38% identity, 99% coverage: 1:396/399 of query aligns to 1:397/401 of 2gr0A
- active site: L12 (≠ H12), R43 (= R43), P44 (= P44), Q290 (≠ E289)
- binding adenosine-5'-diphosphate: V146 (= V147), G147 (= G148), G149 (= G150), I151 (= I152), E170 (= E171), T171 (≠ A172), R178 (= R179), G229 (= G230), I230 (= I231), G231 (= G232)
- binding flavin-adenine dinucleotide: G11 (= G11), A13 (= A13), D35 (= D35), E36 (= E36), R43 (= R43), P44 (= P44), K48 (= K48), T76 (≠ P80), A77 (≠ V81), T104 (= T108), G105 (= G109), R125 (= R126), I151 (= I152), G267 (= G268), D268 (= D269), E284 (= E283), T285 (= T284), W286 (= W285), A289 (= A288), W315 (= W313)
4h4uA Crystal structure of ferredoxin reductase, bpha4 t176r mutant (reduced form)
38% identity, 99% coverage: 1:396/399 of query aligns to 2:398/401 of 4h4uA
- active site: L13 (≠ H12), R44 (= R43), P45 (= P44), Q291 (≠ E289)
- binding flavin-adenine dinucleotide: G12 (= G11), A14 (= A13), D36 (= D35), R44 (= R43), P45 (= P44), A78 (≠ V81), T105 (= T108), G106 (= G109), L125 (= L125), R126 (= R126), I152 (= I152), E155 (= E155), G268 (= G268), D269 (= D269), E285 (= E283), T286 (= T284), W287 (= W285), A290 (= A288), W316 (= W313)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V151 (≠ F151), I152 (= I152), E171 (= E171), R172 (≠ A172), Q173 (≠ G173), G230 (= G230), I231 (= I231), G232 (= G232), I284 (≠ Q282), E285 (= E283), Y315 (≠ F312)
4h4wA Crystal structure of ferredoxin reductase, bpha4 e175c/t176r/q177g mutant (reduced form)
38% identity, 99% coverage: 1:396/399 of query aligns to 1:397/399 of 4h4wA
- active site: L12 (≠ H12), R43 (= R43), P44 (= P44), Q290 (≠ E289)
- binding flavin-adenine dinucleotide: G11 (= G11), A13 (= A13), D35 (= D35), R43 (= R43), P44 (= P44), A77 (≠ V81), T104 (= T108), G105 (= G109), R125 (= R126), I151 (= I152), E154 (= E155), G267 (= G268), D268 (= D269), T285 (= T284), W286 (= W285), A289 (= A288), W315 (= W313)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G148 (= G149), I151 (= I152), R171 (≠ A172), S177 (≠ G178), R178 (= R179), G229 (= G230), I230 (= I231), G231 (= G232)
3lxdA Crystal structure of ferredoxin reductase arr from novosphingobium aromaticivorans (see paper)
37% identity, 99% coverage: 3:397/399 of query aligns to 4:408/409 of 3lxdA
- active site: H13 (= H12), R44 (= R43), P45 (= P44), N302 (≠ E289)
- binding flavin-adenine dinucleotide: V9 (= V8), G10 (= G9), G12 (= G11), H13 (= H12), G14 (≠ A13), R36 (≠ D35), E37 (= E36), R44 (= R43), P45 (= P44), S48 (= S47), K49 (= K48), E81 (≠ P80), V82 (= V81), T109 (= T108), I157 (= I152), G278 (= G268), D279 (= D269), S297 (≠ T284), V298 (≠ W285), F325 (= F312), W326 (= W313)
4emjA Complex between the reductase and ferredoxin components of toluene dioxygenase (see paper)
37% identity, 100% coverage: 1:398/399 of query aligns to 1:403/406 of 4emjA
- binding flavin-adenine dinucleotide: G11 (= G11), V12 (≠ H12), G13 (≠ A13), D35 (= D35), E36 (= E36), R43 (= R43), P44 (= P44), S47 (= S47), K48 (= K48), V80 (= V81), T107 (= T108), G108 (= G109), R128 (= R126), G274 (= G268), D275 (= D269), T291 (= T284), Y292 (≠ W285), S319 (≠ F312), W320 (= W313)
4emiA Toluene dioxygenase reductase in reduced state in complex with NAD+ (see paper)
38% identity, 98% coverage: 7:398/399 of query aligns to 6:402/402 of 4emiA
- binding flavin-adenine dinucleotide: G10 (= G11), V11 (≠ H12), G12 (≠ A13), D34 (= D35), E35 (= E36), R42 (= R43), P43 (= P44), K47 (= K48), E78 (≠ P80), V79 (= V81), T106 (= T108), G107 (= G109), G273 (= G268), D274 (= D269), T290 (= T284), Y291 (≠ W285), W319 (= W313)
- binding nicotinamide-adenine-dinucleotide: R111 (= R113), G149 (= G148), L152 (≠ F151), I153 (= I152), E156 (= E155), E172 (= E171), A173 (= A172), R180 (= R179), V236 (≠ I231), G237 (= G232), A238 (≠ M233), E289 (= E283), W319 (= W313), T320 (≠ S314)
6tukB Crystal structure of fdr9 (see paper)
35% identity, 87% coverage: 5:352/399 of query aligns to 4:353/393 of 6tukB
- binding flavin-adenine dinucleotide: V7 (= V8), G8 (= G9), G9 (≠ A10), G10 (= G11), A12 (= A13), A34 (≠ D35), E35 (= E36), R42 (= R43), P43 (= P44), K47 (= K48), A75 (≠ P80), A76 (≠ V81), T102 (= T108), G103 (= G109), V118 (≠ L125), R119 (= R126), G259 (= G268), D260 (= D269), H277 (≠ T284), W278 (= W285), F311 (= F312), W312 (= W313)
Q9LK94 Monodehydroascorbate reductase 4, peroxisomal; AtMDAR4; EC 1.6.5.4 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 75% coverage: 28:325/399 of query aligns to 31:356/488 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)
32% identity, 75% coverage: 28:325/399 of query aligns to 30:358/429 of 5jclA
- active site: R45 (= R43), P46 (= P44), L61 (= L57), H65 (≠ S61), S70 (≠ A66), R317 (≠ E289)
- binding flavin-adenine dinucleotide: S36 (≠ G34), K37 (≠ D35), E38 (= E36), R45 (= R43), P46 (= P44), K50 (= K48), I93 (≠ V81), A119 (= A107), T120 (= T108), G121 (= G109), R144 (= R126), E145 (≠ T127), D295 (= D269), E311 (= E283), H312 (≠ T284), V313 (≠ W285), A316 (= A288), Y346 (≠ W313)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G170 (= G150), Y171 (≠ F151), I172 (= I152), E175 (= E155), P192 (≠ A172), R199 (= R179), G256 (= G230), V257 (≠ I231), G258 (= G232), E311 (= E283), H312 (≠ T284), Y346 (≠ W313)
Sites not aligning to the query:
5jciA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
32% identity, 75% coverage: 28:325/399 of query aligns to 30:358/432 of 5jciA
- active site: R45 (= R43), P46 (= P44), L61 (= L57), H65 (≠ S61), S70 (≠ A66), R317 (≠ E289)
- binding flavin-adenine dinucleotide: S36 (≠ G34), K37 (≠ D35), E38 (= E36), R45 (= R43), P46 (= P44), K50 (= K48), I93 (≠ V81), A119 (= A107), T120 (= T108), G121 (= G109), R144 (= R126), E145 (≠ T127), Y171 (≠ F151), I172 (= I152), L262 (≠ N236), D295 (= D269), H312 (≠ T284), V313 (≠ W285), A316 (= A288), F345 (= F312), Y346 (≠ W313)
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)
32% identity, 75% coverage: 28:325/399 of query aligns to 33:361/435 of Q652L6
- E41 (= E36) binding
- R48 (= R43) binding
- K53 (= K48) binding
- C70 (= C63) mutation to A: No effect on catalytic activity.; mutation to S: Slight reduction of catalytic activity.
- G72 (≠ R65) mutation to N: Slight reduction of catalytic activity.
- I96 (≠ V81) binding
- RE 147:148 (≠ RT 126:127) binding
- 172:178 (vs. 149:155, 86% identical) binding
- YIGLE 174:178 (≠ FIGLE 151:155) binding
- E196 (≠ G173) binding ; mutation to A: Reduces catalytic activity 2-fold.
- R202 (= R179) binding ; binding
- G261 (= G232) binding ; binding
- D298 (= D269) binding
- EH 314:315 (≠ ET 283:284) binding ; binding
- V316 (≠ W285) binding
- R320 (≠ E289) binding ; mutation to A: Reduces catalytic activity 5-fold.
- Y349 (≠ W313) binding ; binding ; binding ; mutation Y->A,F,W: Abolishes catalytic activity.
- R351 (≠ D315) binding ; mutation to A: No effect on catalytic activity.
Sites not aligning to the query:
5jcnA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
32% identity, 75% coverage: 28:325/399 of query aligns to 30:358/429 of 5jcnA
- active site: R45 (= R43), P46 (= P44), L61 (= L57), H65 (≠ S61), S70 (≠ A66), R317 (≠ E289)
- binding ascorbic acid: P46 (= P44), G69 (≠ R65), R317 (≠ E289), F346 (≠ W313)
- binding flavin-adenine dinucleotide: K37 (≠ D35), E38 (= E36), R45 (= R43), P46 (= P44), K50 (= K48), I93 (≠ V81), A119 (= A107), T120 (= T108), R144 (= R126), E145 (≠ T127), L262 (≠ N236), D295 (= D269), E311 (= E283), H312 (≠ T284), V313 (≠ W285), F346 (≠ W313)
- binding nicotinamide-adenine-dinucleotide: G170 (= G150), Y171 (≠ F151), I172 (= I152), P192 (≠ A172), G256 (= G230), V257 (≠ I231), G258 (= G232), E311 (= E283), H312 (≠ T284), F346 (≠ W313)
Sites not aligning to the query:
5jcmA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
32% identity, 75% coverage: 28:325/399 of query aligns to 30:358/429 of 5jcmA
- active site: R45 (= R43), P46 (= P44), L61 (= L57), H65 (≠ S61), S70 (≠ A66), R317 (≠ E289)
- binding flavin-adenine dinucleotide: S36 (≠ G34), K37 (≠ D35), E38 (= E36), R45 (= R43), P46 (= P44), K50 (= K48), I93 (≠ V81), A119 (= A107), T120 (= T108), G121 (= G109), R144 (= R126), E145 (≠ T127), D295 (= D269), E311 (= E283), H312 (≠ T284), V313 (≠ W285), A316 (= A288), F346 (≠ W313)
- binding isoascorbic acid: E44 (= E42), P46 (= P44), K50 (= K48), G69 (≠ R65), R317 (≠ E289), F346 (≠ W313)
- binding nicotinamide-adenine-dinucleotide: G170 (= G150), Y171 (≠ F151), I172 (= I152), E175 (= E155), P192 (≠ A172), G256 (= G230), V257 (≠ I231), G258 (= G232), E311 (= E283), H312 (≠ T284), F346 (≠ W313)
Sites not aligning to the query:
Query Sequence
>GFF2177 FitnessBrowser__WCS417:GFF2177
MNAPLIIVGAGHAGGRAALTLREEGYTGRLILIGDEPHLPYERPPLSKGLLQGTADLAGY
SLCDRARLAELGIEHIAGNPVTHLQPQQHRLQLADGQWLPYAGLLLATGGRARRLPQEQA
HVLYLRTHDEALALRSALKAGTRLVVVGGGFIGLEVAATARGLGCEVTLLEAGPRLAGRV
LPPVISEALLTLHRQHGVDVRLNMALESIQADAVWLVDGQRLPCDLVVVGIGMQPNIELA
AAAGLEVGQGIRVDSHLRTSAPGIYAAGDVCEFRLGGEYQRQETWRNAEAQGRHAALNLL
GRELPFEALPGFWSDQYDWGVQTVGVITPLMVSRPLASGGMLLFYLDADQRLQGACGWAP
GNSVAKDIKLCERLISAHLSLAPASLADPELSLKHLLRG
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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