SitesBLAST
Comparing SM_b20583 FitnessBrowser__Smeli:SM_b20583 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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of P00438
- S13 (= S13) binding
- E32 (≠ D32) binding
- R33 (= R33) 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 (≠ A34) 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 (≠ H38) 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 (= R42) 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 (≠ RVRAGV 42:47) binding
- R44 (= R44) 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 (= Q102) binding
- C116 (≠ V116) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (= F161) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H162) 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 (= R166) 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 (= Y201) binding
- SQR 212:214 (≠ SMR 212:214) binding
- R214 (= R214) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y222) 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 (= R269) 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 (= D286) binding
- P293 (= P293) binding
- LN 299:300 (= LN 299:300) 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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/391 of 2phhA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding adenosine-5-diphosphoribose: I8 (= I8), P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), Q102 (= Q102), D159 (= D159), I164 (≠ V164), G285 (= G285), D286 (= D286), G298 (= G298), L299 (= L299)
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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/391 of 1pdhA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding arabino-flavin-adenine dinucleotide: P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), Q102 (= Q102), D159 (= D159), Y222 (= Y222), D286 (= D286), P293 (= P293), G298 (= G298)
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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/391 of 1pbcA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V47), W185 (= W185), L199 (= L199), Y201 (= Y201), L210 (= L210), S212 (= S212), R214 (= R214), Y222 (= Y222), P293 (= P293), T294 (= T294)
- binding flavin-adenine dinucleotide: G9 (= G9), P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), Q102 (= Q102), D159 (= D159), I164 (≠ V164), G285 (= G285), D286 (= D286), G298 (= G298)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of 1iusA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding flavin-adenine dinucleotide: G11 (= G11), P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), V47 (= V47), Q102 (= Q102), D159 (= D159), D286 (= D286), A296 (= A296), K297 (= K297), G298 (= G298), L299 (= L299), N300 (= N300)
- binding 4-aminobenzoic acid: Y201 (= Y201), L210 (= L210), S212 (= S212), R214 (= R214), Y222 (= Y222), P293 (= P293)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of 1dodA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding 2,4-dihydroxybenzoic acid: V47 (= V47), Y201 (= Y201), S212 (= S212), R214 (= R214), Y222 (= Y222), P293 (= P293), T294 (= T294), A296 (= A296)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), Q102 (= Q102), D159 (= D159), Y222 (= Y222), D286 (= D286), P293 (= P293), G298 (= G298)
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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of 1d7lA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G9), G11 (= G11), P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q102), D159 (= D159), I164 (≠ V164), D286 (= D286), A296 (= A296), K297 (= K297), G298 (= G298), L299 (= L299), N300 (= N300)
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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of P20586
- S13 (= S13) binding
- E32 (≠ D32) binding
- RIRAGV 42:47 (≠ RVRAGV 42:47) binding
- A45 (= A45) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q102) binding
- Y201 (= Y201) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SMR 212:214) binding
- R220 (= R220) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y222) binding
- D286 (= D286) binding
- P293 (= P293) binding
- LN 299:300 (= LN 299:300) binding
- N300 (= N300) 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 (= Y385) Important for catalytic activity; mutation to F: The positions of the substrate and the flavin are not altered.
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)
64% identity, 100% coverage: 1:390/390 of query aligns to 1:390/391 of 1bf3A
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q102), D159 (= D159), D286 (= D286), A296 (= A296), G298 (= G298), L299 (= L299), N300 (= N300)
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
63% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of 1k0lA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), A45 (= A45), Q102 (= Q102), V127 (= V127), D159 (= D159), G160 (= G160), D286 (= D286), A296 (= A296), G298 (= G298), L299 (= L299)
- binding sulfite ion: D131 (= D131), Q133 (≠ D133)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
63% identity, 100% coverage: 1:390/390 of query aligns to 1:390/394 of 1k0jA
- active site: H72 (= H72), Y201 (= Y201), P293 (= P293), K297 (= K297), Y385 (= Y385)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), G46 (= G46), V47 (= V47), Q102 (= Q102), D159 (= D159), D286 (= D286), P293 (= P293), G298 (= G298), L299 (= L299), N300 (= N300)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R44), F161 (= F161), H162 (= H162), R269 (= R269)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
63% identity, 100% coverage: 1:390/390 of query aligns to 1:388/392 of 1ykjB
- active site: H70 (= H72), Y199 (= Y201), P291 (= P293), K295 (= K297), Y383 (= Y385)
- binding flavin-adenine dinucleotide: I8 (= I8), G9 (= G9), P12 (= P12), S13 (= S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), G45 (≠ A45), V47 (= V47), Q100 (= Q102), D157 (= D159), G158 (= G160), D284 (= D286), P291 (= P293), G296 (= G298), L297 (= L299), N298 (= N300)
- binding pyrosulfate: R33 (= R33), A123 (= A125), E124 (≠ N126), R126 (≠ M128), H160 (= H162), P265 (= P267), R267 (= R269)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
61% identity, 100% coverage: 1:390/390 of query aligns to 4:394/398 of 6dllB
- active site: H75 (= H72), Y204 (= Y201), P296 (= P293), K300 (= K297), Y389 (= Y385)
- binding flavin-adenine dinucleotide: P15 (= P12), S16 (= S13), E35 (≠ D32), R36 (= R33), R45 (= R42), R47 (= R44), A48 (= A45), Q105 (= Q102), C161 (= C158), D162 (= D159), I167 (≠ V164), Y225 (= Y222), D289 (= D286), P296 (= P293), G301 (= G298)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
52% identity, 100% coverage: 1:390/390 of query aligns to 1:392/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (= I8), G11 (= G11), P12 (= P12), A13 (≠ S13), E32 (≠ D32), N33 (≠ R33), R34 (≠ A34), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q102), D161 (= D159), P166 (≠ V164), V268 (≠ A266), G287 (= G285), D288 (= D286), P295 (= P293), A298 (= A296), G300 (= G298), L301 (= L299), N302 (= N300)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
46% identity, 100% coverage: 1:390/390 of query aligns to 1:390/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G11), P12 (= P12), A13 (≠ S13), E32 (≠ D32), R33 (= R33), R42 (= R42), R44 (= R44), V47 (= V47), Q102 (= Q102), V126 (≠ N126), D159 (= D159), G160 (= G160), G285 (= G285), D286 (= D286), A296 (= A296), K297 (= K297), G298 (= G298), L299 (= L299), N300 (= N300)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
41% identity, 99% coverage: 3:390/390 of query aligns to 1:308/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G9), P10 (= P12), V19 (= V47), D78 (= D159), G79 (= G160), T184 (≠ A266), G203 (= G285), D204 (= D286), A214 (= A296), G216 (= G298), L217 (= L299), N218 (= N300)
7yj0D Structural basis of oxepinone formation by a flavin-monooxygenase vibo
27% identity, 79% coverage: 2:309/390 of query aligns to 52:372/622 of 7yj0D
- binding flavin-adenine dinucleotide: I58 (= I8), G59 (= G9), G61 (= G11), P62 (= P12), V63 (≠ S13), D82 (= D32), R83 (= R33), R92 (= R44), A93 (= A45), Q155 (= Q102), A179 (≠ L119), D218 (= D159), G219 (= G160), D349 (= D286), A356 (≠ P293), G361 (= G298)
6brdA Crystal structure of rifampin monooxygenase from streptomyces venezuelae, complexed with rifampin and fad (see paper)
26% identity, 78% coverage: 5:309/390 of query aligns to 4:300/474 of 6brdA
- active site: Q43 (≠ G46), L207 (vs. gap), V215 (≠ Q224), P284 (= P293), Q288 (≠ K297)
- binding flavin-adenine dinucleotide: V7 (≠ I8), G10 (= G11), P11 (= P12), T12 (≠ S13), E31 (≠ D32), K32 (≠ R33), R41 (= R44), A42 (= A45), Q98 (= Q102), L122 (≠ A125), D151 (= D159), G152 (= G160), T156 (≠ V164), D277 (= D286), P284 (= P293), G287 (≠ A296), G289 (= G298), L290 (= L299)
- binding rifampicin: H46 (≠ E49), F74 (= F75), R196 (≠ S215), R201 (= R220), M205 (vs. gap), V215 (≠ Q224), T285 (= T294), G286 (= G295)
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, 78% coverage: 5:309/390 of query aligns to 4:300/476 of F2R776
- T12 (≠ S13) binding
- E31 (≠ D32) binding
- K32 (≠ R33) binding
- Q98 (= Q102) binding
- L122 (≠ A125) binding
- T156 (≠ V164) binding
- R196 (≠ S215) binding
- R213 (≠ Y222) binding
- D277 (= D286) binding
- L290 (= L299) binding
- N291 (= N300) binding
5kowA Structure of rifampicin monooxygenase (see paper)
28% identity, 78% coverage: 5:309/390 of query aligns to 5:300/474 of 5kowA
- active site: R44 (= R44), Q69 (≠ G69), A208 (≠ H216), I216 (≠ Q224), P284 (= P293)
- binding flavin-adenine dinucleotide: G9 (= G9), G11 (= G11), P12 (= P12), T13 (≠ S13), L31 (= L31), E32 (≠ D32), K33 (≠ R33), R42 (= R42), S43 (≠ V43), Q99 (= Q102), E122 (≠ N126), V123 (= V127), D152 (= D159), G153 (= G160), T157 (≠ V164), D277 (= D286), P284 (= P293), Q288 (≠ K297), G289 (= G298), L290 (= L299), N291 (= N300)
Query Sequence
>SM_b20583 FitnessBrowser__Smeli:SM_b20583
MRTQVVIIGSGPSGLLLGQLLTEAGIANVILDRATKAHILGRVRAGVLEQGTVRLMEEAG
CGARMHAEGLPHDGFSLAFDGRDHRIDLFGLTGGRRVMIYGQTELTRDLMDHRERVGALS
IYEAANVMPRDFDGRTPHVAYEKDGIAQRIDCDFIAGCDGFHGVSRRSLPEKAIRNFEKI
YPFGWLGILADVPPVDHELVYANHPRGFALCSMRSHTRSRYYIQCPLEEKIEDWDDQRFW
DELRRRLPAHHAERVVTGPSFEKSIAPLRSFVAEPMRFNRLFLAGDAAHIVPPTGAKGLN
LAASDVHYLFEGLLEHYQDRSNAGIDAYSARALARVWKAVRFSWWMTTMLHRFPETSDFD
QRIQEAELDYLTHSRAAATALAENYVGLPF
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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