SitesBLAST
Comparing Pf6N2E2_227 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_227 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)
7oudAAA FAD-dependent monooxygenase GrhO5 (see paper)
33% identity, 60% coverage: 8:336/548 of query aligns to 1:339/527 of 7oudAAA
- binding Collinone: V43 (= V50), R75 (= R84), S204 (≠ C210), H207 (≠ E218), M273 (≠ F270), P298 (= P295)
- binding flavin-adenine dinucleotide: V7 (≠ I14), G8 (= G15), S10 (≠ G17), V12 (≠ T19), E31 (≠ D38), R32 (= R39), H33 (≠ K40), R41 (= R48), Q105 (= Q110), L129 (= L135), D162 (= D168), G163 (= G169), W271 (≠ Y268), G290 (= G287), D291 (= D288), P298 (= P295)
Sites not aligning to the query:
7oucAAA Putative FAD-dependent monooxygenase GrhO5 (see paper)
33% identity, 60% coverage: 8:336/548 of query aligns to 1:339/527 of 7oucAAA
- binding flavin-adenine dinucleotide: V7 (≠ I14), G8 (= G15), S10 (≠ G17), V12 (≠ T19), E31 (≠ D38), R32 (= R39), H33 (≠ K40), R41 (= R48), Q105 (= Q110), E128 (= E134), L129 (= L135), D162 (= D168), G163 (= G169), W271 (≠ Y268), G290 (= G287), D291 (= D288)
7oujAAA RubL (see paper)
32% identity, 59% coverage: 11:336/548 of query aligns to 8:349/540 of 7oujAAA
- binding (2S)-hexane-1,2,6-triol: P44 (= P47), R45 (= R48), T224 (= T225), V228 (vs. gap), G236 (vs. gap), T237 (vs. gap), G241 (≠ E229), E248 (= E236), D252 (≠ Q240), F253 (≠ V241)
- binding flavin-adenine dinucleotide: V11 (≠ I14), S14 (≠ G17), V16 (≠ T19), E35 (≠ D38), R36 (= R39), H37 (≠ K40), R45 (= R48), A46 (= A49), V47 (= V50), G48 (≠ S51), E138 (= E134), L139 (= L135), D172 (= D168), G173 (= G169), T177 (≠ P173), W281 (≠ Y268), G300 (= G287), D301 (= D288), G311 (= G298), G313 (= G300), A314 (≠ M301), N315 (= N302)
Sites not aligning to the query:
Q2PWU9 4-methyl-5-nitrocatechol 5-monooxygenase; 4M5NC monooxygenase; MNC monooxygenase; 4-methyl-5-nitrocatechol oxygenase; EC 1.14.13.210 from Burkholderia sp. (see paper)
32% identity, 60% coverage: 7:336/548 of query aligns to 11:362/548 of Q2PWU9
- M22 (≠ P18) mutation to L: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with I-380.
Sites not aligning to the query:
- 380 L→I: Able to accept the two new substrates 4-nitrophenol (4NP) and 3-methyl-4-nitrophenol (3M4NP); when associated with L-22.
6u0pC Crystal structure of piee, the flavin-dependent monooxygenase involved in the biosynthesis of piericidin a1 (see paper)
30% identity, 60% coverage: 7:336/548 of query aligns to 4:357/585 of 6u0pC
- binding flavin-adenine dinucleotide: G14 (= G17), P15 (= P18), A16 (≠ T19), N35 (≠ D38), R36 (= R39), H37 (≠ K40), R45 (= R48), A46 (= A49), Q119 (= Q110), F144 (≠ L135), D178 (= D168), G179 (= G169), W289 (≠ Y268), G308 (= G287), D309 (= D288), P316 (= P295)
6u0sA Crystal structure of the flavin-dependent monooxygenase piee in complex with fad and substrate (see paper)
30% identity, 60% coverage: 7:336/548 of query aligns to 4:357/579 of 6u0sA
- binding flavin-adenine dinucleotide: G12 (= G15), G14 (= G17), P15 (= P18), A16 (≠ T19), N35 (≠ D38), R36 (= R39), H37 (≠ K40), R45 (= R48), A46 (= A49), H47 (≠ V50), L48 (≠ S51), Q119 (= Q110), E143 (= E134), F144 (≠ L135), A177 (≠ C167), D178 (= D168), G179 (= G169), R183 (≠ P173), G308 (= G287), D309 (= D288), P316 (= P295), G319 (= G298), G321 (= G300), L322 (≠ M301), N323 (= N302)
- binding 2-[(2E,5E,7E,9R,10R,11E)-10-hydroxy-3,7,9,11-tetramethyltrideca-2,5,7,11-tetraen-1-yl]-6-methoxy-3-methylpyridin-4-ol: H47 (≠ V50), L48 (≠ S51), L221 (vs. gap), A232 (≠ H223), F251 (≠ L232), P316 (= P295), T317 (≠ Y296), G319 (= G298)
Sites not aligning to the query:
- binding 2-[(2E,5E,7E,9R,10R,11E)-10-hydroxy-3,7,9,11-tetramethyltrideca-2,5,7,11-tetraen-1-yl]-6-methoxy-3-methylpyridin-4-ol: 371
2dkiA Crystal structure of 3-hydroxybenzoate hydroxylase from comamonas testosteroni, under pressure of xenon gas (12 atm) (see paper)
31% identity, 61% coverage: 11:345/548 of query aligns to 35:396/615 of 2dkiA
- active site: D75 (≠ V50), R262 (vs. gap), Y271 (≠ E229), P346 (= P295)
- binding flavin-adenine dinucleotide: G39 (= G15), P42 (= P18), A43 (≠ T19), E63 (≠ D38), Q64 (≠ R39), Q73 (≠ R48), R165 (≠ E134), V166 (≠ L135), D207 (= D168), G208 (= G169), N212 (≠ P173), R269 (= R226), Y271 (≠ E229), Y307 (= Y268), G338 (= G287), D339 (= D288), S355 (≠ G304)
- binding xenon: W230 (= W191), P346 (= P295)
Sites not aligning to the query:
2dkhA Crystal structure of 3-hydroxybenzoate hydroxylase from comamonas testosteroni, in complex with the substrate (see paper)
31% identity, 61% coverage: 11:345/548 of query aligns to 35:395/614 of 2dkhA
- active site: D75 (≠ V50), R262 (vs. gap), Y271 (≠ L231), P345 (= P295)
- binding 3-hydroxybenzoic acid: D75 (≠ V50), H135 (≠ K104), K247 (≠ R207), I260 (≠ V219), Y271 (≠ L231)
- binding flavin-adenine dinucleotide: P42 (= P18), A43 (≠ T19), E63 (≠ D38), Q64 (≠ R39), Q73 (≠ R48), R165 (≠ E134), V166 (≠ L135), D207 (= D168), G208 (= G169), V232 (= V193), R269 (= R226), Y271 (≠ L231), Y306 (= Y268), G337 (= G287), D338 (= D288)
Q6SSJ6 3-hydroxybenzoate 4-monooxygenase; 3-hydroxybenzoate 4-hydroxylase; M-hydroxybenzoate hydroxylase; EC 1.14.13.23 from Comamonas testosteroni (Pseudomonas testosteroni) (see 2 papers)
30% identity, 61% coverage: 11:345/548 of query aligns to 35:406/639 of Q6SSJ6
- Q73 (≠ R48) binding
- V166 (≠ L135) binding
- N212 (≠ P173) binding
- N227 (≠ S188) mutation to H: In MobA3-1; able to hydroxylate 3-aminophenol; when associated with R-292 and A-416.
- V257 (= V216) mutation to A: Broadens the substrate range rendering it able to transform phenol to catechol.
- RFY 269:271 (≠ RRF 226:228) binding
- Q292 (vs. gap) mutation to R: In MobA3-1; able to hydroxylate 3-aminophenol; when associated with H-227 and A-416.
- Y317 (= Y268) binding
- D349 (= D288) binding
- S365 (≠ G304) binding
- A400 (= A339) mutation to G: In MobA14-1; able to hydroxylate 3-aminophenol; when associated with R-429.
Sites not aligning to the query:
- 34:64 binding
- 416 D→A: In MobA3-1; able to hydroxylate 3-aminophenol; when associated with H-227 and R-292.
- 429 K→R: In MobA14-1; able to hydroxylate 3-aminophenol; when associated with G-400.
3eptA Structure of the rebeccamycin biosynthetic enzyme rebc with reduced flavin (see paper)
30% identity, 60% coverage: 7:336/548 of query aligns to 3:338/516 of 3eptA
- active site: G46 (≠ V50), L227 (vs. gap), T239 (vs. gap), P297 (= P295)
- binding dihydroflavine-adenine dinucleotide: G13 (= G17), P14 (= P18), V15 (≠ T19), E34 (≠ D38), Q35 (≠ R39), R44 (= R48), V45 (≠ A49), G46 (≠ V50), T47 (≠ S51), R135 (≠ E134), L136 (= L135), D170 (= D168), G171 (= G169), W270 (≠ Y268), D290 (= D288), G302 (= G300), M303 (= M301), N304 (= N302)
4k2xB Oxys anhydrotetracycline hydroxylase from streptomyces rimosus (see paper)
32% identity, 64% coverage: 7:355/548 of query aligns to 1:343/490 of 4k2xB
- active site: L44 (≠ V50), L210 (= L232), T218 (vs. gap), P283 (= P295)
- binding flavin-adenine dinucleotide: G9 (= G15), G11 (= G17), P12 (= P18), T13 (= T19), L31 (≠ I37), E32 (≠ D38), R33 (= R39), K42 (≠ R48), A43 (= A49), Q99 (≠ T116), V123 (≠ L135), D155 (= D168), G156 (= G169), T160 (≠ P173), G275 (= G287), D276 (= D288), P283 (= P295), G286 (= G298), Q287 (= Q299), G288 (= G300), L289 (≠ M301), N290 (= N302)
2r0gA Chromopyrrolic acid-soaked rebc with bound 7-carboxy-k252c (see paper)
30% identity, 60% coverage: 7:336/548 of query aligns to 3:337/522 of 2r0gA
- active site: G46 (≠ V50), L227 (≠ E239), T239 (≠ L251), P296 (= P295)
- binding 7-carboxy-5-hydroxy-12,13-dihydro-6H-indolo[2,3-a]pyrrolo[3,4-c]carbazole: F214 (= F228), F225 (vs. gap), P226 (vs. gap), R228 (≠ Q240), R237 (≠ A249), P296 (= P295), S297 (≠ Y296), G298 (≠ A297)
- binding flavin-adenine dinucleotide: L10 (≠ I14), V15 (≠ T19), E34 (≠ D38), Q35 (≠ R39), R44 (= R48), V45 (≠ A49), T47 (≠ S51), R135 (≠ E134), L136 (= L135), D170 (= D168), G171 (= G169), W269 (≠ Y268), D289 (= D288), G301 (= G300), M302 (= M301)
Sites not aligning to the query:
3ihgA Crystal structure of a ternary complex of aklavinone-11 hydroxylase with fad and aklavinone (see paper)
30% identity, 62% coverage: 8:349/548 of query aligns to 5:369/535 of 3ihgA
- active site: A47 (≠ V50), F234 (≠ P220), F246 (≠ L231), P315 (= P295)
- binding flavin-adenine dinucleotide: G12 (= G15), G14 (= G17), E35 (≠ D38), R36 (= R39), R45 (= R48), A46 (= A49), Q119 (≠ E114), R142 (≠ E134), L143 (= L135), D179 (= D168), G180 (= G169), W288 (≠ Y268), G307 (= G287), D308 (= D288)
- binding methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate: A47 (≠ V50), F79 (≠ Y81), M202 (≠ W191), W222 (≠ V208), Y224 (≠ C210), P315 (= P295), T316 (≠ Y296), G317 (≠ A297), G318 (= G298)
Q54530 Aklavinone 12-hydroxylase RdmE; Aklavinone 11-hydroxylase; EC 1.14.13.180 from Streptomyces purpurascens (see 2 papers)
30% identity, 62% coverage: 8:349/548 of query aligns to 5:369/535 of Q54530
- L15 (≠ P18) binding
- G16 (≠ T19) binding
- E35 (≠ D38) binding
- Q119 (≠ E114) binding
- L143 (= L135) binding
- Y224 (≠ C210) active site, Proton acceptor; mutation to F: Loss of hydroxylase activity.
- D308 (= D288) binding
- G317 (≠ A297) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 373 R→A: Hydroxylase activity similar as the wild-type enzyme.; R→M: Hydroxylase activity similar as the wild-type enzyme.; R→Q: Hydroxylase activity similar as the wild-type enzyme.
7vwpB Structure of the flavin-dependent monooxygenase flso1 from the biosynthesis of fluostatinsin
30% identity, 60% coverage: 7:335/548 of query aligns to 2:322/491 of 7vwpB
- binding flavin-adenine dinucleotide: V9 (≠ I14), G10 (= G15), G12 (= G17), P13 (= P18), T14 (= T19), D33 (= D38), R34 (= R39), L35 (≠ K40), R43 (= R48), A44 (= A49), Q97 (≠ T96), V121 (≠ L135), D153 (= D168), T158 (≠ P173), G274 (= G287), D275 (= D288), P282 (= P295), G284 (≠ A297), Q286 (= Q299), G287 (= G300), M288 (= M301)
8fhjC Crystal structure of a fad monooxygenease from methylocystis sp. Strain sb2 (see paper)
30% identity, 59% coverage: 11:336/548 of query aligns to 7:348/532 of 8fhjC
- binding flavin-adenine dinucleotide: V10 (≠ I14), G11 (= G15), G13 (= G17), A15 (≠ T19), E34 (≠ D38), R35 (= R39), R36 (≠ K40), R41 (≠ T45), K44 (≠ R48), A45 (= A49), H46 (≠ V50), Q114 (= Q110), T137 (≠ E134), L138 (= L135), D172 (= D168), G173 (= G169), N239 (≠ R227), W280 (≠ Y268), G299 (= G287), D300 (= D288), P307 (= P295), G310 (= G298), G312 (= G300), G313 (≠ M301), Q314 (≠ N302)
5kowA Structure of rifampicin monooxygenase (see paper)
32% identity, 59% coverage: 10:335/548 of query aligns to 4:324/474 of 5kowA
- active site: R44 (≠ V50), Q69 (≠ H80), A208 (≠ R224), I216 (≠ L232), P284 (= P295)
- binding flavin-adenine dinucleotide: G9 (= G15), G11 (= G17), P12 (= P18), T13 (= T19), L31 (≠ I37), E32 (≠ D38), K33 (≠ R39), R42 (= R48), S43 (≠ A49), Q99 (= Q110), E122 (= E134), V123 (≠ L135), D152 (= D168), G153 (= G169), T157 (≠ P173), D277 (= D288), P284 (= P295), Q288 (= Q299), G289 (= G300), L290 (≠ M301), N291 (= N302)
6c7sA Structure of rifampicin monooxygenase with product bound (see paper)
32% identity, 59% coverage: 10:335/548 of query aligns to 3:323/473 of 6c7sA
- active site: R43 (≠ V50), A207 (≠ R224), I215 (≠ L232), P283 (= P295)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), P11 (= P18), T12 (= T19), L30 (≠ I37), E31 (≠ D38), K32 (≠ R39), R41 (= R48), S42 (≠ A49), Q98 (= Q110), E121 (= E134), V122 (≠ L135), D151 (= D168), G152 (= G169), T156 (≠ P173), D276 (= D288), P283 (= P295), G286 (= G298), G288 (= G300), L289 (≠ M301), N290 (= N302)
- binding (1E,3S,4R,5S,6R,7R,8R,9S,10S,11E,13E)-15-amino-1-{[(2S)-5,7-dihydroxy-2,4-dimethyl-8-{(E)-[(4-methylpiperazin-1-yl)imino]methyl}-1,6,9-trioxo-1,2,6,9-tetrahydronaphtho[2,1-b]furan-2-yl]oxy}-7,9-dihydroxy-3-methoxy-4,6,8,10,14-pentamethyl-15-oxopentadeca-1,11,13-trien-5-yl acetate: R43 (≠ V50), G72 (= G86), G73 (= G87), F74 (≠ R88), G77 (= G91), A95 (= A107), R196 (= R213), L200 (≠ V217), F202 (≠ V219), G203 (≠ P220), I215 (≠ L232), F256 (≠ Y268), P283 (= P295), T284 (≠ Y296), G285 (≠ A297), G286 (= G298)
5koxA Structure of rifampicin monooxygenase complexed with rifampicin (see paper)
32% identity, 59% coverage: 10:335/548 of query aligns to 3:323/473 of 5koxA
- active site: R43 (≠ V50), Q68 (≠ H80), A207 (≠ R224), I215 (≠ L232), P283 (= P295)
- binding flavin-adenine dinucleotide: G8 (= G15), G10 (= G17), P11 (= P18), T12 (= T19), L30 (≠ I37), E31 (≠ D38), K32 (≠ R39), R41 (= R48), S42 (≠ A49), R43 (≠ V50), Q98 (= Q110), V122 (≠ L135), D151 (= D168), G152 (= G169), T156 (≠ P173), D276 (= D288), P283 (= P295), G286 (= G298), Q287 (= Q299), G288 (= G300), L289 (≠ M301), N290 (= N302)
- binding rifampicin: R43 (≠ V50), G44 (≠ S51), F69 (≠ Y81), F74 (≠ R88), G203 (≠ P220), V205 (≠ P222), I215 (≠ L232), F256 (≠ Y268), P283 (= P295), T284 (≠ Y296), G285 (≠ A297), G286 (= G298)
Q5YTV5 Rifampicin monooxygenase; RIFMO; EC 1.14.13.211 from Nocardia farcinica (strain IFM 10152) (see 2 papers)
32% identity, 59% coverage: 10:335/548 of query aligns to 3:323/473 of Q5YTV5
- T12 (= T19) binding
- E31 (≠ D38) binding
- K32 (≠ R39) binding
- R41 (= R48) binding
- R43 (≠ V50) binding
- Q98 (= Q110) binding
- V122 (≠ L135) binding
- T156 (≠ P173) binding
- R196 (= R213) binding
- D276 (= D288) binding
- G285 (≠ A297) binding
- L289 (≠ M301) binding
- N290 (= N302) binding
Query Sequence
>Pf6N2E2_227 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_227
MTTLKRINTQVLIIGAGPTGLTLANLLGQADVDTLIIDRKPGTVTEPRAVSIDDESLRTM
QAIGLDAAVLRDVVPGYGVHYFTRPGGRCFGKVEPTGKLYGFPKRNAFRQPLFENTLRRG
LERFASLTARFSHELVEFTQDPHGVCALVRDAEGQLMEVHAAYLVACDGGRSPVRKQLGI
EMVGSSFSSRWLVVDTDQDDDPFWQTRVYCDARRPVVEVPGPHRTRRFEFLLKPDETDEQ
VLDETCLQALLRPFKSDAPVSIVRKTVYTFHARVAERWQVQRVFLAGDAAHLTPPYAGQG
MNSGVRDAHNLGWKLVGVLKGKMAESALLSYESERRDHAWALIKLALNLGVVMAPATVLR
ARLISGAFALIGLLPPLRDYFLQMRFKPKPRFTRGLVLTEGQAGTLSCGHMFPQPMLTDA
HDQERLLDDAIGAGFALIQYGDPTRQRIDELKHGLWSHLEARRILILPASVQAMPSIPGC
TVLQDREGQLKTLLGDSHPFLLLRPDRYIAAIFDKATEIRAAESLQSLFGIAEAHSSAIE
PSIAPVFH
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