SitesBLAST
Comparing CCNA_03640 FitnessBrowser__Caulo:CCNA_03640 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)
44% identity, 99% coverage: 5:412/412 of query aligns to 1:413/422 of P16640
- A15 (= A19) binding
- D37 (= D41) binding
- K50 (= K54) binding
- V83 (≠ A87) binding
- R134 (= R135) binding
- D284 (= D283) binding
- V302 (= V301) binding
1q1wA Crystal structure of putidaredoxin reductase from pseudomonas putida (see paper)
44% identity, 99% coverage: 6:412/412 of query aligns to 1:412/422 of 1q1wA
- active site: L13 (≠ H18), L44 (≠ R49), P45 (= P50), L305 (= L305)
- binding flavin-adenine dinucleotide: G10 (= G15), G12 (= G17), L13 (≠ H18), A14 (= A19), G35 (= G40), D36 (= D41), L44 (≠ R49), P45 (= P50), K49 (= K54), V82 (≠ A87), A108 (= A113), T109 (= T114), G110 (= G115), R133 (= R135), I159 (≠ V161), D283 (= D283), S300 (= S300), V301 (= V301), W329 (= W329)
3lxdA Crystal structure of ferredoxin reductase arr from novosphingobium aromaticivorans (see paper)
44% identity, 99% coverage: 7:412/412 of query aligns to 2:409/409 of 3lxdA
- active site: H13 (= H18), R44 (= R49), P45 (= P50), N302 (≠ L305)
- binding flavin-adenine dinucleotide: V9 (= V14), G10 (= G15), G12 (= G17), H13 (= H18), G14 (≠ A19), R36 (≠ D41), E37 (= E42), R44 (= R49), P45 (= P50), S48 (= S53), K49 (= K54), E81 (≠ V86), V82 (≠ A87), T109 (= T114), I157 (≠ V161), G278 (= G282), D279 (= D283), S297 (= S300), V298 (= V301), F325 (= F328), W326 (= W329)
3fg2P Crystal structure of ferredoxin reductase for the cyp199a2 system from rhodopseudomonas palustris (see paper)
42% identity, 98% coverage: 8:412/412 of query aligns to 1:404/404 of 3fg2P
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), H11 (= H18), A12 (= A19), D34 (= D41), E35 (= E42), R42 (= R49), P43 (= P50), S46 (= S53), K47 (= K54), R78 (= R89), M79 (vs. gap), T106 (= T114), R127 (= R135), I153 (≠ V161), D275 (= D283), S292 (= S300), V293 (= V301), W321 (= W329)
4h4uA Crystal structure of ferredoxin reductase, bpha4 t176r mutant (reduced form)
39% identity, 98% coverage: 8:412/412 of query aligns to 3:400/401 of 4h4uA
- active site: L13 (≠ H18), R44 (= R49), P45 (= P50), Q291 (≠ L305)
- binding flavin-adenine dinucleotide: G12 (= G17), A14 (= A19), D36 (= D41), R44 (= R49), P45 (= P50), A78 (= A87), T105 (= T114), G106 (= G115), L125 (= L134), R126 (= R135), I152 (≠ V161), E155 (= E164), G268 (= G282), D269 (= D283), E285 (= E299), T286 (≠ S300), W287 (≠ V301), A290 (= A304), W316 (= W329)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V151 (≠ Y160), I152 (≠ V161), E171 (= E180), R172 (= R181), Q173 (≠ E182), G230 (= G244), I231 (≠ V245), G232 (= G246), I284 (≠ L298), E285 (= E299), Y315 (≠ F328)
2yvjA Crystal structure of the ferredoxin-ferredoxin reductase (bpha3-bpha4)complex (see paper)
39% identity, 98% coverage: 8:412/412 of query aligns to 3:400/402 of 2yvjA
- active site: L13 (≠ H18), R44 (= R49), P45 (= P50), Q291 (≠ L305)
- binding flavin-adenine dinucleotide: G10 (= G15), G12 (= G17), G35 (= G40), D36 (= D41), E37 (= E42), R44 (= R49), P45 (= P50), A78 (= A87), T105 (= T114), G106 (= G115), R126 (= R135), G268 (= G282), D269 (= D283), T286 (≠ S300), W287 (≠ V301), A290 (= A304), W316 (= W329)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (= V156), G148 (= G157), G149 (= G158), G150 (= G159), I152 (≠ V161), V170 (≠ I179), E171 (= E180), T172 (≠ R181), R179 (= R188), G230 (= G244), I231 (≠ V245), G232 (= G246), V233 (≠ A247), E285 (= E299)
1f3pA Ferredoxin reductase (bpha4)-nadh complex (see paper)
39% identity, 98% coverage: 8:412/412 of query aligns to 3:400/401 of 1f3pA
- active site: L13 (≠ H18), R44 (= R49), P45 (= P50), Q291 (≠ L305)
- binding flavin-adenine dinucleotide: A14 (= A19), V34 (≠ I39), D36 (= D41), E37 (= E42), R44 (= R49), P45 (= P50), A78 (= A87), T105 (= T114), G106 (= G115), R126 (= R135), G268 (= G282), D269 (= D283), E285 (= E299), T286 (≠ S300), W287 (≠ V301), A290 (= A304), W316 (= W329)
- binding nicotinamide-adenine-dinucleotide: V147 (= V156), G148 (= G157), G150 (= G159), V151 (≠ Y160), I152 (≠ V161), E155 (= E164), E171 (= E180), T172 (≠ R181), R179 (= R188), G230 (= G244), I231 (≠ V245), G232 (= G246), V233 (≠ A247), E285 (= E299), W316 (= W329), S317 (= S330)
8pxkA Structure of nadh-dependent ferredoxin reductase, bpha4, solved at wavelength 5.76 a (see paper)
39% identity, 98% coverage: 8:412/412 of query aligns to 4:401/403 of 8pxkA
- binding flavin-adenine dinucleotide: G13 (= G17), A15 (= A19), D37 (= D41), E38 (= E42), R45 (= R49), P46 (= P50), K50 (= K54), A79 (= A87), T106 (= T114), G107 (= G115), R127 (= R135), I153 (≠ V161), G269 (= G282), D270 (= D283), E286 (= E299), T287 (≠ S300), W288 (≠ V301), A291 (= A304), W317 (= W329)
2gr2A Crystal structure of ferredoxin reductase, bpha4 (oxidized form)
39% identity, 98% coverage: 8:412/412 of query aligns to 2:399/401 of 2gr2A
- active site: L12 (≠ H18), R43 (= R49), P44 (= P50), Q290 (≠ L305)
- binding adenosine-5-diphosphoribose: R109 (= R119), V146 (= V156), G147 (= G157), G149 (= G159), V150 (≠ Y160), I151 (≠ V161), E170 (= E180), T171 (≠ R181), R178 (= R188), G229 (= G244), I230 (≠ V245), G231 (= G246), E284 (= E299)
- binding flavin-adenine dinucleotide: G11 (= G17), A13 (= A19), D35 (= D41), E36 (= E42), R43 (= R49), P44 (= P50), K48 (= K54), A77 (= A87), T104 (= T114), G105 (= G115), R125 (= R135), G267 (= G282), D268 (= D283), T285 (≠ S300), W286 (≠ V301), A289 (= A304), W315 (= W329)
2gr0A Crystal structure of ferredoxin reductase, bpha4 (oxidized form, NAD+ complex) (see paper)
39% identity, 98% coverage: 8:412/412 of query aligns to 2:399/401 of 2gr0A
- active site: L12 (≠ H18), R43 (= R49), P44 (= P50), Q290 (≠ L305)
- binding adenosine-5'-diphosphate: V146 (= V156), G147 (= G157), G149 (= G159), I151 (≠ V161), E170 (= E180), T171 (≠ R181), R178 (= R188), G229 (= G244), I230 (≠ V245), G231 (= G246)
- binding flavin-adenine dinucleotide: G11 (= G17), A13 (= A19), D35 (= D41), E36 (= E42), R43 (= R49), P44 (= P50), K48 (= K54), T76 (≠ V86), A77 (= A87), T104 (= T114), G105 (= G115), R125 (= R135), I151 (≠ V161), G267 (= G282), D268 (= D283), E284 (= E299), T285 (≠ S300), W286 (≠ V301), A289 (= A304), W315 (= W329)
4h4wA Crystal structure of ferredoxin reductase, bpha4 e175c/t176r/q177g mutant (reduced form)
39% identity, 98% coverage: 8:412/412 of query aligns to 2:399/399 of 4h4wA
- active site: L12 (≠ H18), R43 (= R49), P44 (= P50), Q290 (≠ L305)
- binding flavin-adenine dinucleotide: G11 (= G17), A13 (= A19), D35 (= D41), R43 (= R49), P44 (= P50), A77 (= A87), T104 (= T114), G105 (= G115), R125 (= R135), I151 (≠ V161), E154 (= E164), G267 (= G282), D268 (= D283), T285 (≠ S300), W286 (≠ V301), A289 (= A304), W315 (= W329)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G148 (= G158), I151 (≠ V161), R171 (= R181), S177 (≠ A187), R178 (= R188), G229 (= G244), I230 (≠ V245), G231 (= G246)
4emjA Complex between the reductase and ferredoxin components of toluene dioxygenase (see paper)
38% identity, 97% coverage: 11:409/412 of query aligns to 5:400/406 of 4emjA
- binding flavin-adenine dinucleotide: G11 (= G17), V12 (≠ H18), G13 (≠ A19), D35 (= D41), E36 (= E42), R43 (= R49), P44 (= P50), S47 (= S53), K48 (= K54), V80 (≠ A87), T107 (= T114), G108 (= G115), R128 (= R135), G274 (= G282), D275 (= D283), T291 (≠ S300), Y292 (≠ V301), S319 (≠ F328), W320 (= W329)
4emiA Toluene dioxygenase reductase in reduced state in complex with NAD+ (see paper)
38% identity, 97% coverage: 11:409/412 of query aligns to 4:399/402 of 4emiA
- binding flavin-adenine dinucleotide: G10 (= G17), V11 (≠ H18), G12 (≠ A19), D34 (= D41), E35 (= E42), R42 (= R49), P43 (= P50), K47 (= K54), E78 (≠ V86), V79 (≠ A87), T106 (= T114), G107 (= G115), G273 (= G282), D274 (= D283), T290 (≠ S300), Y291 (≠ V301), W319 (= W329)
- binding nicotinamide-adenine-dinucleotide: R111 (= R119), G149 (= G157), L152 (≠ Y160), I153 (≠ V161), E156 (= E164), E172 (= E180), A173 (≠ R181), R180 (= R188), V236 (= V245), G237 (= G246), A238 (= A247), E289 (= E299), W319 (= W329), T320 (≠ S330)
Q9LK94 Monodehydroascorbate reductase 4, peroxisomal; AtMDAR4; EC 1.6.5.4 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
32% identity, 77% coverage: 26:343/412 of query aligns to 23:358/488 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.
6tukB Crystal structure of fdr9 (see paper)
33% identity, 96% coverage: 11:407/412 of query aligns to 4:390/393 of 6tukB
- binding flavin-adenine dinucleotide: V7 (= V14), G8 (= G15), G9 (≠ A16), G10 (= G17), A12 (= A19), A34 (≠ D41), E35 (= E42), R42 (= R49), P43 (= P50), K47 (= K54), A75 (≠ V86), A76 (= A87), T102 (= T114), G103 (= G115), V118 (≠ L134), R119 (= R135), G259 (= G282), D260 (= D283), H277 (≠ S300), W278 (≠ V301), F311 (= F328), W312 (= W329)
Q652L6 Monodehydroascorbate reductase 3, cytosolic; OsMDAR3; OsMDHAR3; EC 1.6.5.4 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 77% coverage: 26:341/412 of query aligns to 25:361/435 of Q652L6
- E41 (= E42) binding
- R48 (= R49) binding
- K53 (= K54) binding
- C70 (≠ S67) mutation to A: No effect on catalytic activity.; mutation to S: Slight reduction of catalytic activity.
- G72 (≠ K69) mutation to N: Slight reduction of catalytic activity.
- I96 (≠ A87) binding
- RE 147:148 (≠ RT 135:136) binding
- 172:178 (vs. 158:164, 86% identical) binding
- YIGLE 174:178 (≠ YVGLE 160:164) binding
- E196 (= E182) binding ; mutation to A: Reduces catalytic activity 2-fold.
- R202 (= R188) binding ; binding
- G261 (= G246) binding ; binding
- D298 (= D283) binding
- EH 314:315 (≠ ES 299:300) binding ; binding
- V316 (= V301) binding
- R320 (≠ L305) binding ; mutation to A: Reduces catalytic activity 5-fold.
- Y349 (≠ W329) binding ; binding ; binding ; mutation Y->A,F,W: Abolishes catalytic activity.
- R351 (≠ D331) 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)
29% identity, 77% coverage: 26:341/412 of query aligns to 22:358/432 of 5jciA
- active site: R45 (= R49), P46 (= P50), L61 (vs. gap), H65 (≠ S65), S70 (≠ P70), R317 (≠ L305)
- binding flavin-adenine dinucleotide: S36 (≠ G40), K37 (≠ D41), E38 (= E42), R45 (= R49), P46 (= P50), K50 (= K54), I93 (≠ A87), A119 (= A113), T120 (= T114), G121 (= G115), R144 (= R135), E145 (≠ T136), Y171 (= Y160), I172 (≠ V161), L262 (≠ N250), D295 (= D283), H312 (≠ S300), V313 (= V301), A316 (= A304), F345 (= F328), Y346 (≠ W329)
Sites not aligning to the query:
5jcnA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
28% identity, 91% coverage: 26:399/412 of query aligns to 22:419/429 of 5jcnA
- active site: R45 (= R49), P46 (= P50), L61 (vs. gap), H65 (≠ S65), S70 (≠ P70), R317 (≠ L305)
- binding ascorbic acid: P46 (= P50), G69 (≠ K69), R317 (≠ L305), F346 (≠ W329)
- binding flavin-adenine dinucleotide: K37 (≠ D41), E38 (= E42), R45 (= R49), P46 (= P50), K50 (= K54), I93 (≠ A87), A119 (= A113), T120 (= T114), R144 (= R135), E145 (≠ T136), L262 (≠ N250), D295 (= D283), E311 (= E299), H312 (≠ S300), V313 (= V301), F346 (≠ W329)
- binding nicotinamide-adenine-dinucleotide: G170 (= G159), Y171 (= Y160), I172 (≠ V161), P192 (≠ R181), G256 (= G244), V257 (= V245), G258 (= G246), E311 (= E299), H312 (≠ S300), F346 (≠ W329)
Sites not aligning to the query:
5jcmA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
28% identity, 91% coverage: 26:399/412 of query aligns to 22:419/429 of 5jcmA
- active site: R45 (= R49), P46 (= P50), L61 (vs. gap), H65 (≠ S65), S70 (≠ P70), R317 (≠ L305)
- binding flavin-adenine dinucleotide: S36 (≠ G40), K37 (≠ D41), E38 (= E42), R45 (= R49), P46 (= P50), K50 (= K54), I93 (≠ A87), A119 (= A113), T120 (= T114), G121 (= G115), R144 (= R135), E145 (≠ T136), D295 (= D283), E311 (= E299), H312 (≠ S300), V313 (= V301), A316 (= A304), F346 (≠ W329)
- binding isoascorbic acid: E44 (≠ Q48), P46 (= P50), K50 (= K54), G69 (≠ K69), R317 (≠ L305), F346 (≠ W329)
- binding nicotinamide-adenine-dinucleotide: G170 (= G159), Y171 (= Y160), I172 (≠ V161), E175 (= E164), P192 (≠ R181), G256 (= G244), V257 (= V245), G258 (= G246), E311 (= E299), H312 (≠ S300), F346 (≠ W329)
Sites not aligning to the query:
5jclA Structure and catalytic mechanism of monodehydroascorbate reductase, mdhar, from oryza sativa l. Japonica (see paper)
28% identity, 91% coverage: 26:399/412 of query aligns to 22:419/429 of 5jclA
- active site: R45 (= R49), P46 (= P50), L61 (vs. gap), H65 (≠ S65), S70 (≠ P70), R317 (≠ L305)
- binding flavin-adenine dinucleotide: S36 (≠ G40), K37 (≠ D41), E38 (= E42), R45 (= R49), P46 (= P50), K50 (= K54), I93 (≠ A87), A119 (= A113), T120 (= T114), G121 (= G115), R144 (= R135), E145 (≠ T136), D295 (= D283), E311 (= E299), H312 (≠ S300), V313 (= V301), A316 (= A304), Y346 (≠ W329)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G170 (= G159), Y171 (= Y160), I172 (≠ V161), E175 (= E164), P192 (≠ R181), R199 (= R188), G256 (= G244), V257 (= V245), G258 (= G246), E311 (= E299), H312 (≠ S300), Y346 (≠ W329)
Sites not aligning to the query:
Query Sequence
>CCNA_03640 FitnessBrowser__Caulo:CCNA_03640
MSAEVNQNACVVIVGAGHAGGSVAAFLRQYGHEGRIVLIGDEPLLPYQRPPLSKAWLKGE
ADADSLSLKPAGWYADNNVMLRLGGVAERINRSDKTVALASGEVIPYDFLVLATGARARE
LPIPGADLAGVLALRTAADAELLKNALGPDKRLAVVGGGYVGLEAAASARALGSHAMVIE
RESRVLARVACETLSHFFQDYHGKHGVAFELNAGVAAFEGHDGHVTGVRFNDGRVVACDV
ALVGVGAVPNDELAKDAGLSTANGVVVDLEARTDDPSIFAIGDVTHRPLPLYDRQFRLES
VPNALEQAKQAASAILGRPGPAPETPWFWSDQYDLKLQIAGLPFDADRQVVRGDVAAAKF
AVFHLKGDLVQAVEAVNAPPEFMAGKQLIAKRTPVDANKLADPSVSMKEVAA
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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