SitesBLAST
Comparing Ac3H11_3418 FitnessBrowser__acidovorax_3H11:Ac3H11_3418 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)
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)
61% identity, 98% coverage: 11:400/400 of query aligns to 1:390/391 of 1pbcA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V57), W185 (= W195), L199 (= L209), Y201 (= Y211), L210 (= L220), S212 (= S222), R214 (= R224), Y222 (= Y232), P293 (= P303), T294 (= T304)
- binding flavin-adenine dinucleotide: G9 (= G19), P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), Q102 (= Q112), D159 (= D169), I164 (≠ V174), G285 (= G295), D286 (= D296), G298 (= G308)
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
61% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of P00438
- S13 (= S23) binding
- E32 (= E42) binding
- R33 (= R43) 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 (= Q44) 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 (= Y48) 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 (= R52) 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 52:57) binding
- R44 (= R54) 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 (= Q112) binding
- C116 (≠ M126) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (= F171) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H172) 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 (= R176) 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 (= Y211) binding
- SQR 212:214 (≠ SLR 222:224) binding
- R214 (= R224) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y232) 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 (= R279) 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 (= D296) binding
- P293 (= P303) binding
- LN 299:300 (= LN 309:310) binding
2phhA The coenzyme analogue adenosine 5-diphosphoribose displaces fad in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation (see paper)
61% identity, 98% coverage: 11:400/400 of query aligns to 1:390/391 of 2phhA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding adenosine-5-diphosphoribose: I8 (= I18), P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), Q102 (= Q112), D159 (= D169), I164 (≠ V174), G285 (= G295), D286 (= D296), G298 (= G308), L299 (= L309)
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)
61% identity, 98% coverage: 11:400/400 of query aligns to 1:390/391 of 1pdhA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding arabino-flavin-adenine dinucleotide: P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), Q102 (= Q112), D159 (= D169), Y222 (= Y232), D286 (= D296), P293 (= P303), G298 (= G308)
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)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/391 of 1bf3A
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding flavin-adenine dinucleotide: P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R44 (= R54), A45 (= A55), G46 (= G56), V47 (= V57), Q102 (= Q112), D159 (= D169), D286 (= D296), A296 (= A306), G298 (= G308), L299 (= L309), N300 (= N310)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of 1iusA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding flavin-adenine dinucleotide: G11 (= G21), P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), V47 (= V57), Q102 (= Q112), D159 (= D169), D286 (= D296), A296 (= A306), K297 (≠ R307), G298 (= G308), L299 (= L309), N300 (= N310)
- binding 4-aminobenzoic acid: Y201 (= Y211), L210 (= L220), S212 (= S222), R214 (= R224), Y222 (= Y232), P293 (= P303)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of 1dodA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding 2,4-dihydroxybenzoic acid: V47 (= V57), Y201 (= Y211), S212 (= S222), R214 (= R224), Y222 (= Y232), P293 (= P303), T294 (= T304), A296 (= A306)
- binding flavin-adenine dinucleotide: P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), Q102 (= Q112), D159 (= D169), Y222 (= Y232), D286 (= D296), P293 (= P303), G298 (= G308)
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)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of 1d7lA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G19), G11 (= G21), P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), G46 (= G56), V47 (= V57), Q102 (= Q112), D159 (= D169), I164 (≠ V174), D286 (= D296), A296 (= A306), K297 (≠ R307), G298 (= G308), L299 (= L309), N300 (= N310)
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)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of P20586
- S13 (= S23) binding
- E32 (= E42) binding
- RIRAGV 42:47 (= RIRAGV 52:57) binding
- A45 (= A55) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q112) binding
- Y201 (= Y211) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SLR 222:224) binding
- R220 (= R230) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y232) binding
- D286 (= D296) binding
- P293 (= P303) binding
- LN 299:300 (= LN 309:310) binding
- N300 (= N310) 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 (= Y395) 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)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of 1k0lA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding flavin-adenine dinucleotide: P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), A45 (= A55), Q102 (= Q112), V127 (= V137), D159 (= D169), G160 (= G170), D286 (= D296), A296 (= A306), G298 (= G308), L299 (= L309)
- binding sulfite ion: D131 (≠ N141), Q133 (≠ K143)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
60% identity, 98% coverage: 11:400/400 of query aligns to 1:390/394 of 1k0jA
- active site: H72 (= H82), Y201 (= Y211), P293 (= P303), K297 (≠ R307), Y385 (= Y395)
- binding flavin-adenine dinucleotide: P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), G46 (= G56), V47 (= V57), Q102 (= Q112), D159 (= D169), D286 (= D296), P293 (= P303), G298 (= G308), L299 (= L309), N300 (= N310)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R54), F161 (= F171), H162 (= H172), R269 (= R279)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
61% identity, 98% coverage: 9:400/400 of query aligns to 2:394/398 of 6dllB
- active site: H75 (= H82), Y204 (= Y211), P296 (= P303), K300 (≠ R307), Y389 (= Y395)
- binding flavin-adenine dinucleotide: P15 (= P22), S16 (= S23), E35 (= E42), R36 (= R43), R45 (= R52), R47 (= R54), A48 (= A55), Q105 (= Q112), C161 (≠ A168), D162 (= D169), I167 (≠ V174), Y225 (= Y232), D289 (= D296), P296 (= P303), G301 (= G308)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
59% identity, 98% coverage: 11:400/400 of query aligns to 1:388/392 of 1ykjB
- active site: H70 (= H82), Y199 (= Y211), P291 (= P303), K295 (≠ R307), Y383 (= Y395)
- binding flavin-adenine dinucleotide: I8 (= I18), G9 (= G19), P12 (= P22), S13 (= S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), G45 (≠ A55), V47 (= V57), Q100 (= Q112), D157 (= D169), G158 (= G170), D284 (= D296), P291 (= P303), G296 (= G308), L297 (= L309), N298 (= N310)
- binding pyrosulfate: R33 (= R43), A123 (≠ E135), E124 (≠ D136), R126 (≠ Q138), H160 (= H172), P265 (= P277), R267 (= R279)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
49% identity, 98% coverage: 11:400/400 of query aligns to 1:392/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (= I18), G11 (= G21), P12 (= P22), A13 (≠ S23), E32 (= E42), N33 (≠ R43), R34 (≠ Q44), R44 (= R54), A45 (= A55), G46 (= G56), V47 (= V57), Q102 (= Q112), D161 (= D169), P166 (≠ V174), V268 (≠ A276), G287 (= G295), D288 (= D296), P295 (= P303), A298 (= A306), G300 (= G308), L301 (= L309), N302 (= N310)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
43% identity, 98% coverage: 11:400/400 of query aligns to 1:390/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G21), P12 (= P22), A13 (≠ S23), E32 (= E42), R33 (= R43), R42 (= R52), R44 (= R54), V47 (= V57), Q102 (= Q112), V126 (≠ D136), D159 (= D169), G160 (= G170), G285 (= G295), D286 (= D296), A296 (= A306), K297 (≠ R307), G298 (= G308), L299 (= L309), N300 (= N310)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
37% identity, 97% coverage: 13:400/400 of query aligns to 1:308/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G19), P10 (= P22), V19 (= V57), D78 (= D169), G79 (= G170), T184 (≠ A276), G203 (= G295), D204 (= D296), A214 (= A306), G216 (= G308), L217 (= L309), N218 (= N310)
6brdA Crystal structure of rifampin monooxygenase from streptomyces venezuelae, complexed with rifampin and fad (see paper)
26% identity, 81% coverage: 15:338/400 of query aligns to 4:320/474 of 6brdA
- active site: Q43 (≠ G56), L207 (= L223), V215 (≠ Q234), P284 (= P303), Q288 (≠ R307)
- binding flavin-adenine dinucleotide: V7 (≠ I18), G10 (= G21), P11 (= P22), T12 (≠ S23), E31 (= E42), K32 (≠ R43), R41 (= R54), A42 (= A55), Q98 (= Q112), L122 (≠ V137), D151 (= D169), G152 (= G170), T156 (≠ V174), D277 (= D296), P284 (= P303), G287 (≠ A306), G289 (= G308), L290 (= L309)
- binding rifampicin: H46 (≠ E59), F74 (≠ G84), R196 (≠ A212), R201 (≠ G217), M205 (≠ C221), V215 (≠ Q234), T285 (= T304), G286 (= G305)
Sites not aligning to the query:
F2R776 Rifampicin monooxygenase; RIFMO; EC 1.14.13.211 from Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745) (see paper)
26% identity, 81% coverage: 15:338/400 of query aligns to 4:320/476 of F2R776
- T12 (≠ S23) binding
- E31 (= E42) binding
- K32 (≠ R43) binding
- Q98 (= Q112) binding
- L122 (≠ V137) binding
- T156 (≠ V174) binding
- R196 (≠ A212) binding
- R213 (≠ Y232) binding
- D277 (= D296) binding
- L290 (= L309) binding
- N291 (= N310) binding
7vwpB Structure of the flavin-dependent monooxygenase flso1 from the biosynthesis of fluostatinsin
23% identity, 82% coverage: 10:338/400 of query aligns to 1:318/491 of 7vwpB
- binding flavin-adenine dinucleotide: V9 (≠ I18), G10 (= G19), G12 (= G21), P13 (= P22), T14 (≠ S23), D33 (≠ E42), R34 (= R43), L35 (≠ Q44), R43 (= R52), A44 (= A64), Q97 (≠ E121), V121 (= V137), D153 (= D169), T158 (≠ V174), G274 (= G295), D275 (= D296), P282 (= P303), G284 (= G305), Q286 (≠ R307), G287 (= G308), M288 (≠ L309)
6u0pC Crystal structure of piee, the flavin-dependent monooxygenase involved in the biosynthesis of piericidin a1 (see paper)
23% identity, 77% coverage: 11:319/400 of query aligns to 4:332/585 of 6u0pC
- binding flavin-adenine dinucleotide: G14 (= G21), P15 (= P22), A16 (≠ S23), N35 (≠ E42), R36 (= R43), H37 (≠ Q44), R45 (= R54), A46 (= A55), Q119 (= Q112), F144 (≠ D136), D178 (= D169), G179 (= G170), W289 (≠ E272), G308 (= G295), D309 (= D296), P316 (= P303)
Query Sequence
>Ac3H11_3418 FitnessBrowser__acidovorax_3H11:Ac3H11_3418
MNAPTTPGDTMKTQVCIIGGGPSGLMLSQLLHLKGIATIVLERQSREYVLGRIRAGVLEH
GFAALMREAQCGERMDKEGEIHDGFIIAHDGQMDRVDLHKYSGGSSVVVYGQTELTRDLY
EARDRMKGVVIHNAEDVQPHNLKSANPYVTYRNGDEVVRIDCDFVIGADGFHGVSRKSIP
RDVLKEYEKVYPFGWLGVLSRTKPVSPELIYAKHERGFALCSLRSQVLSRYYIQVPLTDN
VEDWSDEAFWAELKRRLPAEVADKLITGASIEKSIAPLRSFVAEPMRYGNLFLAGDAAHI
VPPTGARGLNSAASDIYYLHHAMVAHYQNGDSTGLDKYSEKALARVWKAQRFSWWMTTML
HTFPDSIAYDQKLQDTDLAYLFSSEKALGSLAENYVGLPF
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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