SitesBLAST
Comparing HSERO_RS19905 FitnessBrowser__HerbieS:HSERO_RS19905 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)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
65% identity, 99% coverage: 1:386/388 of query aligns to 1:389/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (= I8), G11 (= G11), P12 (= P12), A13 (= A13), E32 (= E32), N33 (≠ T33), R34 (= R34), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q101), D161 (= D158), P166 (≠ V163), V268 (≠ I265), G287 (= G284), D288 (= D285), P295 (= P292), A298 (= A295), G300 (= G297), L301 (= L298), N302 (= N299)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of 1iusA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding flavin-adenine dinucleotide: G11 (= G11), P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), V47 (= V47), Q102 (= Q101), D159 (= D158), D286 (= D285), A296 (= A295), K297 (= K296), G298 (= G297), L299 (= L298), N300 (= N299)
- binding 4-aminobenzoic acid: Y201 (= Y200), L210 (= L209), S212 (= S211), R214 (= R213), Y222 (= Y221), P293 (= P292)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of 1dodA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding 2,4-dihydroxybenzoic acid: V47 (= V47), Y201 (= Y200), S212 (= S211), R214 (= R213), Y222 (= Y221), P293 (= P292), T294 (= T293), A296 (= A295)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), Q102 (= Q101), D159 (= D158), Y222 (= Y221), D286 (= D285), P293 (= P292), G298 (= G297)
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)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of 1d7lA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G9), G11 (= G11), P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q101), D159 (= D158), I164 (≠ V163), D286 (= D285), A296 (= A295), K297 (= K296), G298 (= G297), L299 (= L298), N300 (= N299)
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)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of P20586
- S13 (≠ A13) binding
- E32 (= E32) binding
- RIRAGV 42:47 (≠ TIRAGV 42:47) binding
- A45 (= A45) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q101) binding
- Y201 (= Y200) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ STR 211:213) binding
- R220 (= R219) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y221) binding
- D286 (= D285) binding
- P293 (= P292) binding
- LN 299:300 (= LN 298:299) binding
- N300 (= N299) 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 (= Y384) 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)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/391 of 1bf3A
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R44 (= R44), A45 (= A45), G46 (= G46), V47 (= V47), Q102 (= Q101), D159 (= D158), D286 (= D285), A296 (= A295), G298 (= G297), L299 (= L298), N300 (= N299)
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)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/391 of 1pbcA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V47), W185 (= W184), L199 (= L198), Y201 (= Y200), L210 (= L209), S212 (= S211), R214 (= R213), Y222 (= Y221), P293 (= P292), T294 (= T293)
- binding flavin-adenine dinucleotide: G9 (= G9), P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), Q102 (= Q101), D159 (= D158), I164 (≠ V163), G285 (= G284), D286 (= D285), G298 (= G297)
2phhA The coenzyme analogue adenosine 5-diphosphoribose displaces fad in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation (see paper)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/391 of 2phhA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding adenosine-5-diphosphoribose: I8 (= I8), P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), Q102 (= Q101), D159 (= D158), I164 (≠ V163), G285 (= G284), D286 (= D285), G298 (= G297), L299 (= L298)
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)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/391 of 1pdhA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding arabino-flavin-adenine dinucleotide: P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), Q102 (= Q101), D159 (= D158), Y222 (= Y221), D286 (= D285), P293 (= P292), G298 (= G297)
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
51% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of P00438
- S13 (≠ A13) binding
- E32 (= E32) binding
- R33 (≠ T33) 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 (≠ R34) 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 (≠ E38) 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 (≠ T42) 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 (≠ TIRAGV 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 (= Q101) binding
- C116 (≠ A115) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (= F160) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H161) 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 (= R165) 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 (= Y200) binding
- SQR 212:214 (≠ STR 211:213) binding
- R214 (= R213) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y221) 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 (= R268) 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 (= D285) binding
- P293 (= P292) binding
- LN 299:300 (= LN 298:299) binding
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
50% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of 1k0lA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), A45 (= A45), Q102 (= Q101), V127 (≠ T126), D159 (= D158), G160 (= G159), D286 (= D285), A296 (= A295), G298 (= G297), L299 (= L298)
- binding sulfite ion: D131 (≠ G130), Q133 (≠ E132)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
50% identity, 99% coverage: 1:386/388 of query aligns to 1:387/394 of 1k0jA
- active site: H72 (= H72), Y201 (= Y200), P293 (= P292), K297 (= K296), Y385 (= Y384)
- binding flavin-adenine dinucleotide: P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), G46 (= G46), V47 (= V47), Q102 (= Q101), D159 (= D158), D286 (= D285), P293 (= P292), G298 (= G297), L299 (= L298), N300 (= N299)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R44), F161 (= F160), H162 (= H161), R269 (= R268)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
50% identity, 99% coverage: 1:386/388 of query aligns to 1:387/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G11), P12 (= P12), A13 (= A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), V47 (= V47), Q102 (= Q101), V126 (≠ G125), D159 (= D158), G160 (= G159), G285 (= G284), D286 (= D285), A296 (= A295), K297 (= K296), G298 (= G297), L299 (= L298), N300 (= N299)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
50% identity, 99% coverage: 1:386/388 of query aligns to 1:385/392 of 1ykjB
- active site: H70 (= H72), Y199 (= Y200), P291 (= P292), K295 (= K296), Y383 (= Y384)
- binding flavin-adenine dinucleotide: I8 (= I8), G9 (= G9), P12 (= P12), S13 (≠ A13), E32 (= E32), R33 (≠ T33), R42 (≠ T42), R44 (= R44), G45 (≠ A45), V47 (= V47), Q100 (= Q101), D157 (= D158), G158 (= G159), D284 (= D285), P291 (= P292), G296 (= G297), L297 (= L298), N298 (= N299)
- binding pyrosulfate: R33 (≠ T33), A123 (≠ S124), E124 (≠ G125), R126 (≠ S127), H160 (= H161), P265 (≠ G266), R267 (= R268)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
48% identity, 99% coverage: 1:386/388 of query aligns to 4:391/398 of 6dllB
- active site: H75 (= H72), Y204 (= Y200), P296 (= P292), K300 (= K296), Y389 (= Y384)
- binding flavin-adenine dinucleotide: P15 (= P12), S16 (≠ A13), E35 (= E32), R36 (≠ T33), R45 (≠ T42), R47 (= R44), A48 (= A45), Q105 (= Q101), C161 (= C157), D162 (= D158), I167 (≠ V163), Y225 (= Y221), D289 (= D285), P296 (= P292), G301 (= G297)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
42% identity, 99% coverage: 3:386/388 of query aligns to 1:305/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G9), P10 (= P12), V19 (= V47), D78 (= D158), G79 (= G159), T184 (≠ I265), G203 (= G284), D204 (= D285), A214 (= A295), G216 (= G297), L217 (= L298), N218 (= N299)
6brdA Crystal structure of rifampin monooxygenase from streptomyces venezuelae, complexed with rifampin and fad (see paper)
26% identity, 78% coverage: 5:308/388 of query aligns to 4:300/474 of 6brdA
- active site: Q43 (≠ G46), L207 (≠ T216), V215 (≠ C224), P284 (= P292), Q288 (≠ K296)
- binding flavin-adenine dinucleotide: V7 (≠ I8), G10 (= G11), P11 (= P12), T12 (≠ A13), E31 (= E32), K32 (≠ T33), R41 (= R44), A42 (= A45), Q98 (≠ H102), L122 (≠ I128), D151 (= D158), G152 (= G159), T156 (vs. gap), D277 (= D285), P284 (= P292), G287 (≠ A295), G289 (= G297), L290 (= L298)
- binding rifampicin: H46 (≠ E49), F74 (≠ R82), R196 (= R213), R201 (vs. gap), M205 (vs. gap), V215 (≠ C224), T285 (= T293), G286 (= G294)
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: 5:308/388 of query aligns to 4:300/476 of F2R776
- T12 (≠ A13) binding
- E31 (= E32) binding
- K32 (≠ T33) binding
- Q98 (≠ H102) binding
- L122 (≠ I128) binding
- T156 (vs. gap) binding
- R196 (= R213) binding
- R213 (≠ F222) binding
- D277 (= D285) binding
- L290 (= L298) binding
- N291 (= N299) binding
6ui5A Tmn9 in complex with cofactor fad
24% identity, 79% coverage: 5:312/388 of query aligns to 3:309/497 of 6ui5A
- binding flavin-adenine dinucleotide: V6 (≠ I8), G7 (= G9), G9 (= G11), A11 (= A13), D30 (≠ E32), I31 (≠ T33), H32 (≠ R34), R36 (≠ E38), P40 (≠ T42), A41 (≠ I43), L119 (≠ G125), D153 (= D158), Y262 (≠ G263), G281 (= G284), D282 (= D285), P289 (= P292), G294 (= G297), L295 (= L298)
4x4jA Structural and functional studies of bexe: insights into oxidation during be-7585a biosynthesis
27% identity, 82% coverage: 5:324/388 of query aligns to 4:310/482 of 4x4jA
- active site: L43 (≠ G46), L200 (≠ R213), I208 (≠ Y221), P278 (= P292)
- binding flavin-adenine dinucleotide: P11 (= P12), A12 (= A13), L30 (= L31), E31 (= E32), R32 (≠ T33), R41 (= R44), G42 (≠ A45), Q95 (= Q101), E118 (≠ S122), L119 (≠ V123), D151 (= D158), D271 (= D285), P278 (= P292), G281 (≠ A295), Q282 (≠ K296), G283 (= G297), M284 (≠ L298), N285 (= N299)
Query Sequence
>HSERO_RS19905 FitnessBrowser__HerbieS:HSERO_RS19905
MRTQVAIIGAGPAGLLLSHLLHLKGIESVVLETRSREEIESTIRAGVLEQGTMDILTETG
VGERMKREGALHHGIELAFGGRRHRIDLTELTGQAITVYAQHEVIKDLVAARLAAQGQLL
FSVSGTSIEGVETDKPRVRFMHEGEQHTLEADFIAGCDGFHGVSRPAIPDSKRQDYQRIY
PFGWFGVLVEAPPSSDELIYAQHERGFVLVSTRSPTVQRLYFQCDPKDSVDNWSDDRIWN
EFHTRLENGDGWRLKEGKIFQKGIIGMRSFVSTPMQHGRLFLAGDAAHIVPPTGAKGLNL
AVGDVKRLAQGIDDFYRSASEAGLASYTEQALKRIWRAEYFSWWMTSMLHTFEDASPFQR
QIQRAELENVVNSRALSTALAENYVGAF
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