SitesBLAST
Comparing AO356_05295 FitnessBrowser__pseudo5_N2C3_1:AO356_05295 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)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
77% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of 1iusA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding flavin-adenine dinucleotide: G11 (= G14), P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), V47 (= V50), Q102 (= Q105), D159 (= D162), D286 (= D289), A296 (= A299), K297 (= K300), G298 (= G301), L299 (= L302), N300 (= N303)
- binding 4-aminobenzoic acid: Y201 (= Y204), L210 (= L213), S212 (= S215), R214 (= R217), Y222 (= Y225), P293 (= P296)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
77% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of 1dodA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding 2,4-dihydroxybenzoic acid: V47 (= V50), Y201 (= Y204), S212 (= S215), R214 (= R217), Y222 (= Y225), P293 (= P296), T294 (= T297), A296 (= A299)
- binding flavin-adenine dinucleotide: P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), Q102 (= Q105), D159 (= D162), Y222 (= Y225), D286 (= D289), P293 (= P296), G298 (= G301)
1d7lA Structure-function correlations of the reaction of reduced nicotinamide analogs with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins (see paper)
77% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of 1d7lA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G12), G11 (= G14), P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), G46 (= G49), V47 (= V50), Q102 (= Q105), D159 (= D162), I164 (≠ V167), D286 (= D289), A296 (= A299), K297 (= K300), G298 (= G301), L299 (= L302), N300 (= N303)
P20586 p-hydroxybenzoate hydroxylase; PHBH; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 7 papers)
77% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of P20586
- S13 (= S16) binding FAD
- E32 (= E35) binding FAD
- RIRAGV 42:47 (= RIRAGV 45:50) binding FAD
- A45 (= A48) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q105) binding FAD
- Y201 (= Y204) Important for catalytic activity; binding substrate; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SMR 215:217) binding substrate
- R220 (= R223) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y225) binding substrate
- D286 (= D289) binding FAD
- P293 (= P296) binding substrate
- LN 299:300 (= LN 302:303) binding FAD
- N300 (= N303) mutation to D: The side chain of Asp300 moves away from the flavin, disrupting the interactions of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interactions with the flavin ring.
- Y385 (= Y387) Important for catalytic activity; mutation to F: The positions of the substrate and the flavin are not altered.
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
77% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of P00438
- S13 (= S16) binding FAD
- E32 (= E35) binding FAD
- R33 (= R36) mutation to E: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH.; mutation to K: Slight decrease of affinity for p-OHB and NADPH.; mutation to S: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH.
- Q34 (= Q37) mutation to K: Slight decrease of affinity for p-OHB and NADPH.; mutation to R: Slight decrease of affinity for p-OHB and NADPH.; mutation to T: Slight decrease of affinity for p-OHB and NADPH.
- Y38 (= Y41) mutation to E: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH.; mutation to F: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH.; mutation to K: Slight decrease of affinity for p-OHB and strong decrease of affinity for NADPH.
- R42 (= R45) mutation to K: 4-fold and 10-fold decrease of affinity for p-OHB and NADPH, respectively. The turnover rate of p-hydroxybenzoate hydroxylase results from impaired binding of NADPH.; mutation to S: 3-fold and 10-fold decrease of affinity for p-OHB and NADPH, respectively. The turnover rate of p-hydroxybenzoate hydroxylase results from impaired binding of NADPH. Hardly disturbs the binding of FAD.
- RIRAGV 42:47 (= RIRAGV 45:50) binding FAD
- R44 (= R47) mutation to K: Decrease of affinity for the flavin prosthetic group. It affects NADPH binding, resulting in a low yield of the charge-transfer species between reduced flavin and NADP.
- Q102 (= Q105) binding FAD
- C116 (≠ A119) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (= F164) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H165) mutation to D: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to K: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly.; mutation to N: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to R: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly.; mutation to S: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to T: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to Y: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly.
- R166 (= R169) mutation to E: Loses the ability to bind NADPH and FAD.; mutation to K: Loses the ability to bind NADPH.; mutation to S: Loses the ability to bind NADPH.
- Y201 (= Y204) binding substrate
- SQR 212:214 (≠ SMR 215:217) binding substrate
- R214 (= R217) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y225) binding substrate; mutation to A: Results in the removal of a large side chain involving in the binding of the carboxyl group of the substrate.
- R269 (= R272) mutation to D: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to K: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly.; mutation to N: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to S: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases slightly.; mutation to T: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.; mutation to Y: No significant changes in affinity for p-OHB are observed. However, the affinity for NADPH decreases strongly.
- D286 (= D289) binding FAD
- P293 (= P296) binding substrate
- LN 299:300 (= LN 302:303) binding FAD
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
76% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of 1k0lA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding flavin-adenine dinucleotide: P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), Q102 (= Q105), V127 (≠ A130), D159 (= D162), G160 (= G163), D286 (= D289), A296 (= A299), G298 (= G301), L299 (= L302)
- binding sulfite ion: D131 (= D134), Q133 (= Q136)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
76% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of 1k0jA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding flavin-adenine dinucleotide: P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), G46 (= G49), V47 (= V50), Q102 (= Q105), D159 (= D162), D286 (= D289), P293 (= P296), G298 (= G301), L299 (= L302), N300 (= N303)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R47), F161 (= F164), H162 (= H165), R269 (= R272)
1pbcA Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate and 2-hydroxy- 4-aminobenzoate and of the try222ala mutant, complexed with 2- hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring (see paper)
77% identity, 98% coverage: 4:393/396 of query aligns to 1:391/391 of 1pbcA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V50), W185 (= W188), L199 (= L202), Y201 (= Y204), L210 (= L213), S212 (= S215), R214 (= R217), Y222 (= Y225), P293 (= P296), T294 (= T297)
- binding flavin-adenine dinucleotide: G9 (= G12), P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), Q102 (= Q105), D159 (= D162), I164 (≠ V167), G285 (= G288), D286 (= D289), G298 (= G301)
2phhA The coenzyme analogue adenosine 5-diphosphoribose displaces fad in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation (see paper)
77% identity, 98% coverage: 4:393/396 of query aligns to 1:391/391 of 2phhA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding adenosine-5-diphosphoribose: I8 (= I11), P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), Q102 (= Q105), D159 (= D162), I164 (≠ V167), G285 (= G288), D286 (= D289), G298 (= G301), L299 (= L302)
1pdhA Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified fad present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin (see paper)
77% identity, 98% coverage: 4:393/396 of query aligns to 1:391/391 of 1pdhA
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding arabino-flavin-adenine dinucleotide: P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), A45 (= A48), Q102 (= Q105), D159 (= D162), Y222 (= Y225), D286 (= D289), P293 (= P296), G298 (= G301)
1bf3A P-hydroxybenzoate hydroxylase (phbh) mutant with cys 116 replaced by ser (c116s) and arg 42 replaced by lys (r42k), in complex with fad and 4-hydroxybenzoic acid (see paper)
76% identity, 98% coverage: 4:393/396 of query aligns to 1:391/391 of 1bf3A