SitesBLAST
Comparing Pf6N2E2_2914 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2914 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)
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
76% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of P00438
- S13 (= S16) binding
- E32 (= E35) binding
- 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
- 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
- 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
- SQR 212:214 (≠ SMR 215:217) binding
- 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 ; 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
- P293 (= P296) binding
- LN 299:300 (= LN 302:303) binding
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
76% 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)
76% 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)
76% 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)
76% identity, 99% coverage: 4:396/396 of query aligns to 1:394/394 of P20586
- S13 (= S16) binding
- E32 (= E35) binding
- RIRAGV 42:47 (= RIRAGV 45:50) binding
- A45 (= A48) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q105) binding
- Y201 (= Y204) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SMR 215:217) binding
- R220 (= R223) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y225) binding
- D286 (= D289) binding
- P293 (= P296) binding
- LN 299:300 (= LN 302:303) binding
- 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.
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
75% 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)
75% 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)
76% 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)
76% 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)
76% 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
- active site: H72 (= H75), Y201 (= Y204), P293 (= P296), K297 (= K300), Y385 (= Y387)
- binding flavin-adenine dinucleotide: P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R44 (= R47), A45 (= A48), G46 (= G49), V47 (= V50), Q102 (= Q105), D159 (= D162), D286 (= D289), A296 (= A299), G298 (= G301), L299 (= L302), N300 (= N303)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
75% identity, 99% coverage: 4:396/396 of query aligns to 1:392/392 of 1ykjB
- active site: H70 (= H75), Y199 (= Y204), P291 (= P296), K295 (= K300), Y383 (= Y387)
- binding flavin-adenine dinucleotide: I8 (= I11), G9 (= G12), P12 (= P15), S13 (= S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), G45 (≠ A48), V47 (= V50), Q100 (= Q105), D157 (= D162), G158 (= G163), D284 (= D289), P291 (= P296), G296 (= G301), L297 (= L302), N298 (= N303)
- binding pyrosulfate: R33 (= R36), A123 (≠ S128), E124 (≠ N129), R126 (≠ Q131), H160 (= H165), P265 (= P270), R267 (= R272)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
69% identity, 99% coverage: 2:395/396 of query aligns to 2:397/398 of 6dllB
- active site: H75 (= H75), Y204 (= Y204), P296 (= P296), K300 (= K300), Y389 (= Y387)
- binding flavin-adenine dinucleotide: P15 (= P15), S16 (= S16), E35 (= E35), R36 (= R36), R45 (= R45), R47 (= R47), A48 (= A48), Q105 (= Q105), C161 (= C161), D162 (= D162), I167 (≠ V167), Y225 (= Y225), D289 (= D289), P296 (= P296), G301 (= G301)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
51% identity, 98% coverage: 4:393/396 of query aligns to 1:393/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (= I11), G11 (= G14), P12 (= P15), A13 (≠ S16), E32 (= E35), N33 (≠ R36), R34 (≠ Q37), R44 (= R47), A45 (= A48), G46 (= G49), V47 (= V50), Q102 (= Q105), D161 (= D162), P166 (≠ V167), V268 (≠ A269), G287 (= G288), D288 (= D289), P295 (= P296), A298 (= A299), G300 (= G301), L301 (= L302), N302 (= N303)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
46% identity, 98% coverage: 4:393/396 of query aligns to 1:391/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G14), P12 (= P15), A13 (≠ S16), E32 (= E35), R33 (= R36), R42 (= R45), R44 (= R47), V47 (= V50), Q102 (= Q105), V126 (≠ N129), D159 (= D162), G160 (= G163), G285 (= G288), D286 (= D289), A296 (= A299), K297 (= K300), G298 (= G301), L299 (= L302), N300 (= N303)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
38% identity, 98% coverage: 6:393/396 of query aligns to 1:309/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G12), P10 (= P15), V19 (= V50), D78 (= D162), G79 (= G163), T184 (≠ A269), G203 (= G288), D204 (= D289), A214 (= A299), G216 (= G301), L217 (= L302), N218 (= N303)
4k2xB Oxys anhydrotetracycline hydroxylase from streptomyces rimosus (see paper)
25% identity, 83% coverage: 4:333/396 of query aligns to 1:321/490 of 4k2xB
- active site: L44 (≠ R47), L210 (≠ A230), T218 (≠ P238), P283 (= P296)
- binding flavin-adenine dinucleotide: G9 (= G12), G11 (= G14), P12 (= P15), T13 (≠ S16), L31 (= L34), E32 (= E35), R33 (= R36), K42 (≠ R45), A43 (≠ I46), Q99 (≠ T106), V123 (≠ A130), D155 (= D162), G156 (= G163), T160 (≠ V167), G275 (= G288), D276 (= D289), P283 (= P296), G286 (≠ A299), Q287 (≠ K300), G288 (= G301), L289 (= L302), N290 (= N303)
K7QRJ5 Dialkyldecalin synthase; FAD-dependent [4+2] cyclase; EC 5.5.1.- from Streptomyces rugosporus (see 2 papers)
27% identity, 78% coverage: 4:312/396 of query aligns to 1:298/463 of K7QRJ5
- V13 (≠ S16) binding
- E32 (= E35) mutation to A: Loss of catalytic activity. Loss of FAD binding.
- ER 32:33 (= ER 35:36) binding
- H74 (≠ R85) mutation to A: 81% loss of catalytic efficiency.
- I121 (≠ Y125) binding
- D275 (= D289) binding ; mutation to A: Loss of catalytic activity. Loss of FAD binding.
5xgvA The structure of diels-alderase pyre3 in the biosynthetic pathway of pyrroindomycins (see paper)
28% identity, 77% coverage: 8:312/396 of query aligns to 4:297/461 of 5xgvA
- binding flavin-adenine dinucleotide: G10 (= G14), P11 (= P15), V12 (≠ S16), E31 (= E35), R32 (= R36), H33 (≠ Q37), R41 (= R47), I120 (≠ Y125), D149 (= D162), G150 (= G163), W174 (≠ L189), G273 (= G288), D274 (= D289), P281 (= P296), G284 (≠ A299), A286 (≠ G301), L287 (= L302)
L8EUQ6 12-dehydrotetracycline 5-monooxygenase/anhydrotetracycline 6-monooxygenase; EC 1.14.13.234; EC 1.14.13.38 from Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM 4667 / NRRL 2234) (see paper)
24% identity, 83% coverage: 4:333/396 of query aligns to 1:333/503 of L8EUQ6
- T13 (≠ S16) binding
- ER 32:33 (= ER 35:36) binding
- L44 (≠ R47) binding
- H47 (≠ E52) mutation to A: Decrease of the ratio between oxytetracycline and tetracycline.
- Q99 (≠ T106) binding
- V123 (≠ A130) binding
- T160 (≠ V167) binding
- F215 (vs. gap) mutation to I: Dramatic change in the product ratio, in which the amount of tetracycline exceeds that of oxytetracycline.
- D288 (= D289) binding
- LN 301:302 (= LN 302:303) binding
Query Sequence
>Pf6N2E2_2914 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2914
MKTLKTQVAIIGAGPSGLLLGQLLHNAGIDTVILERQTPEYVLSRIRAGVLEQGMVELLR
QAGVGQRMDAEGLPHDGFELVLNDRRVHIDLKGLTGGKNVMVYGQTEVTRDLMAAREAAG
ARTLYLASNAQPHDMQTQTPFVTFEHEGETWRLDCDYIAGCDGFHGVARQSIPAEKLKVF
ERVYPFGWLGVLADTPPVHEELVYARHTRGFALCSMRSKTRTRYYLQVPAEEQVADWPDE
RFWGELKNRLPADLAAALVTGPSIEKSIAPLRSFVVEPMQYGRMFLVGDAAHIVPPTGAK
GLNLAASDVSTLFNILLKVYRDGRVELLEKYSAICLRRVWKAERFSWWMTSMLHRFDDDA
FNQRISEAELEYFVDSEAGRKTIAENYVGLPYEAIE
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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