SitesBLAST
Comparing GFF269 FitnessBrowser__Phaeo:GFF269 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)
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, 95% coverage: 21:408/408 of query aligns to 3:390/391 of 2phhA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding adenosine-5-diphosphoribose: I8 (≠ V26), P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), Q102 (= Q120), D159 (= D177), I164 (≠ V182), G285 (= G303), D286 (= D304), G298 (= G316), L299 (= L317)
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, 95% coverage: 21:408/408 of query aligns to 3:390/391 of 1pdhA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding arabino-flavin-adenine dinucleotide: P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), Q102 (= Q120), D159 (= D177), Y222 (= Y240), D286 (= D304), P293 (= P311), G298 (= G316)
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
64% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of P00438
- S13 (= S31) binding
- E32 (= E50) binding
- R33 (= R51) 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 (= Q52) 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 (= Y56) 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 (= R60) 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 60:65) binding
- R44 (= R62) 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 (= Q120) binding
- C116 (≠ M134) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (= F179) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H180) 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 (= R184) 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 (= Y219) binding
- SQR 212:214 (≠ SMR 230:232) binding
- R214 (= R232) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y240) 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 (= R287) 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 (= D304) binding
- P293 (= P311) binding
- LN 299:300 (= LN 317:318) binding
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, 95% coverage: 21:408/408 of query aligns to 3:390/391 of 1pbcA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V65), W185 (= W203), L199 (= L217), Y201 (= Y219), L210 (= L228), S212 (= S230), R214 (= R232), Y222 (= Y240), P293 (= P311), T294 (= T312)
- binding flavin-adenine dinucleotide: G9 (= G27), P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), Q102 (= Q120), D159 (= D177), I164 (≠ V182), G285 (= G303), D286 (= D304), G298 (= G316)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of 1iusA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding flavin-adenine dinucleotide: G11 (= G29), P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), V47 (= V65), Q102 (= Q120), D159 (= D177), D286 (= D304), A296 (= A314), K297 (= K315), G298 (= G316), L299 (= L317), N300 (= N318)
- binding 4-aminobenzoic acid: Y201 (= Y219), L210 (= L228), S212 (= S230), R214 (= R232), Y222 (= Y240), P293 (= P311)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of 1dodA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding 2,4-dihydroxybenzoic acid: V47 (= V65), Y201 (= Y219), S212 (= S230), R214 (= R232), Y222 (= Y240), P293 (= P311), T294 (= T312), A296 (= A314)
- binding flavin-adenine dinucleotide: P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), Q102 (= Q120), D159 (= D177), Y222 (= Y240), D286 (= D304), P293 (= P311), G298 (= G316)
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)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of 1d7lA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G27), G11 (= G29), P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), G46 (= G64), V47 (= V65), Q102 (= Q120), D159 (= D177), I164 (≠ V182), D286 (= D304), A296 (= A314), K297 (= K315), G298 (= G316), L299 (= L317), N300 (= N318)
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)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of P20586
- S13 (= S31) binding
- E32 (= E50) binding
- RIRAGV 42:47 (= RIRAGV 60:65) binding
- A45 (= A63) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q120) binding
- Y201 (= Y219) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SMR 230:232) binding
- R220 (= R238) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y240) binding
- D286 (= D304) binding
- P293 (= P311) binding
- LN 299:300 (= LN 317:318) binding
- N300 (= N318) 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 (= Y403) 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)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/391 of 1bf3A
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding flavin-adenine dinucleotide: P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R44 (= R62), A45 (= A63), G46 (= G64), V47 (= V65), Q102 (= Q120), D159 (= D177), D286 (= D304), A296 (= A314), G298 (= G316), L299 (= L317), N300 (= N318)
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of 1k0lA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding flavin-adenine dinucleotide: P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), A45 (= A63), Q102 (= Q120), V127 (= V145), D159 (= D177), G160 (= G178), D286 (= D304), A296 (= A314), G298 (= G316), L299 (= L317)
- binding sulfite ion: D131 (= D149), Q133 (≠ T151)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:390/394 of 1k0jA
- active site: H72 (= H90), Y201 (= Y219), P293 (= P311), K297 (= K315), Y385 (= Y403)
- binding flavin-adenine dinucleotide: P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), G46 (= G64), V47 (= V65), Q102 (= Q120), D159 (= D177), D286 (= D304), P293 (= P311), G298 (= G316), L299 (= L317), N300 (= N318)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R62), F161 (= F179), H162 (= H180), R269 (= R287)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
63% identity, 95% coverage: 21:408/408 of query aligns to 3:388/392 of 1ykjB
- active site: H70 (= H90), Y199 (= Y219), P291 (= P311), K295 (= K315), Y383 (= Y403)
- binding flavin-adenine dinucleotide: I8 (≠ V26), G9 (= G27), P12 (= P30), S13 (= S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), G45 (≠ A63), V47 (= V65), Q100 (= Q120), D157 (= D177), G158 (= G178), D284 (= D304), P291 (= P311), G296 (= G316), L297 (= L317), N298 (= N318)
- binding pyrosulfate: R33 (= R51), A123 (= A143), E124 (≠ N144), R126 (≠ A146), H160 (= H180), P265 (= P285), R267 (= R287)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
61% identity, 96% coverage: 17:408/408 of query aligns to 2:394/398 of 6dllB
- active site: H75 (= H90), Y204 (= Y219), P296 (= P311), K300 (= K315), Y389 (= Y403)
- binding flavin-adenine dinucleotide: P15 (= P30), S16 (= S31), E35 (= E50), R36 (= R51), R45 (= R60), R47 (= R62), A48 (= A63), Q105 (= Q120), C161 (≠ A176), D162 (= D177), I167 (≠ V182), Y225 (= Y240), D289 (= D304), P296 (= P311), G301 (= G316)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
50% identity, 95% coverage: 21:407/408 of query aligns to 3:391/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (≠ V26), G11 (= G29), P12 (= P30), A13 (≠ S31), E32 (= E50), N33 (≠ R51), R34 (≠ Q52), R44 (= R62), A45 (= A63), G46 (= G64), V47 (= V65), Q102 (= Q120), D161 (= D177), P166 (≠ V182), V268 (≠ A284), G287 (= G303), D288 (= D304), P295 (= P311), A298 (= A314), G300 (= G316), L301 (= L317), N302 (= N318)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
44% identity, 95% coverage: 21:407/408 of query aligns to 3:389/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G29), P12 (= P30), A13 (≠ S31), E32 (= E50), R33 (= R51), R42 (= R60), R44 (= R62), V47 (= V65), Q102 (= Q120), V126 (≠ N144), D159 (= D177), G160 (= G178), G285 (= G303), D286 (= D304), A296 (= A314), K297 (= K315), G298 (= G316), L299 (= L317), N300 (= N318)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
36% identity, 95% coverage: 21:407/408 of query aligns to 1:307/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G27), P10 (= P30), V19 (= V65), D78 (= D177), G79 (= G178), T184 (≠ A284), G203 (= G303), D204 (= D304), A214 (= A314), G216 (= G316), L217 (= L317), N218 (= N318)
6brdA Crystal structure of rifampin monooxygenase from streptomyces venezuelae, complexed with rifampin and fad (see paper)
27% identity, 83% coverage: 23:359/408 of query aligns to 4:324/474 of 6brdA
- active site: Q43 (≠ G64), L207 (vs. gap), V215 (≠ Q242), P284 (= P311), Q288 (≠ K315)
- binding flavin-adenine dinucleotide: V7 (= V26), G10 (= G29), P11 (= P30), T12 (≠ S31), E31 (= E50), K32 (≠ R51), R41 (= R62), A42 (= A63), Q98 (= Q120), L122 (≠ N144), D151 (= D177), G152 (= G178), T156 (≠ V182), D277 (= D304), P284 (= P311), G287 (≠ A314), G289 (= G316), L290 (= L317)
- binding rifampicin: H46 (≠ E67), F74 (≠ H94), R196 (= R232), R201 (vs. gap), M205 (vs. gap), V215 (≠ Q242), T285 (= T312), G286 (= G313)
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)
27% identity, 83% coverage: 23:359/408 of query aligns to 4:324/476 of F2R776
- T12 (≠ S31) binding
- E31 (= E50) binding
- K32 (≠ R51) binding
- Q98 (= Q120) binding
- L122 (≠ N144) binding
- T156 (≠ V182) binding
- R196 (= R232) binding
- R213 (≠ Y240) binding
- D277 (= D304) binding
- L290 (= L317) binding
- N291 (= N318) binding
6c7sA Structure of rifampicin monooxygenase with product bound (see paper)
28% identity, 75% coverage: 23:327/408 of query aligns to 4:299/473 of 6c7sA
- active site: R43 (= R62), A207 (vs. gap), I215 (≠ Q242), P283 (= P311)
- binding flavin-adenine dinucleotide: G8 (= G27), G10 (= G29), P11 (= P30), T12 (≠ S31), L30 (= L49), E31 (= E50), K32 (≠ R51), R41 (= R60), S42 (≠ I61), Q98 (= Q120), E121 (≠ N144), V122 (= V145), D151 (= D177), G152 (= G178), T156 (≠ V182), D276 (= D304), P283 (= P311), G286 (≠ A314), G288 (= G316), L289 (= L317), N290 (= N318)
- binding (1E,3S,4R,5S,6R,7R,8R,9S,10S,11E,13E)-15-amino-1-{[(2S)-5,7-dihydroxy-2,4-dimethyl-8-{(E)-[(4-methylpiperazin-1-yl)imino]methyl}-1,6,9-trioxo-1,2,6,9-tetrahydronaphtho[2,1-b]furan-2-yl]oxy}-7,9-dihydroxy-3-methoxy-4,6,8,10,14-pentamethyl-15-oxopentadeca-1,11,13-trien-5-yl acetate: R43 (= R62), G72 (≠ Q98), G73 (= G99), F74 (≠ R100), G77 (≠ R103), A95 (≠ V117), R196 (= R232), L200 (= L236), F202 (vs. gap), G203 (vs. gap), I215 (≠ Q242), F256 (≠ L286), P283 (= P311), T284 (= T312), G285 (= G313), G286 (≠ A314)
5koxA Structure of rifampicin monooxygenase complexed with rifampicin (see paper)
28% identity, 75% coverage: 23:327/408 of query aligns to 4:299/473 of 5koxA
- active site: R43 (= R62), Q68 (≠ H94), A207 (vs. gap), I215 (≠ Q242), P283 (= P311)
- binding flavin-adenine dinucleotide: G8 (= G27), G10 (= G29), P11 (= P30), T12 (≠ S31), L30 (= L49), E31 (= E50), K32 (≠ R51), R41 (= R60), S42 (≠ I61), R43 (= R62), Q98 (= Q120), V122 (= V145), D151 (= D177), G152 (= G178), T156 (≠ V182), D276 (= D304), P283 (= P311), G286 (≠ A314), Q287 (≠ K315), G288 (= G316), L289 (= L317), N290 (= N318)
- binding rifampicin: R43 (= R62), G44 (≠ A63), F69 (≠ I95), F74 (≠ R100), G203 (vs. gap), V205 (vs. gap), I215 (≠ Q242), F256 (≠ L286), P283 (= P311), T284 (= T312), G285 (= G313), G286 (≠ A314)
Query Sequence
>GFF269 FitnessBrowser__Phaeo:GFF269
MAKFRHDGRANRRKLMQSQTTQVVIVGGGPSGLLLSQLLHRAGIDTIVLERQTRDYVLGR
IRAGVLEHGFVDLLRRAGASARMDRDGMVHHGFHIAHQGRLDRIDLAGSAKGQTVMVYGQ
TEVTRDLYDARDAMGGQIIHEAANVALHDLTTARPNVTYEQQGETRRIDTKFIVGADGFH
GVSRKSIPSDVLQEYEKVYPFGWLGVLSQTSPAADELIYARHDRGFALCSMRNAQLSRYY
IQVPLTDRVEDWSDAAFWEELKRRLPEDVAKGLQTGVSIEKSIAPLRSFVAEPMRYGALF
LAGDAAHIVPPTGAKGLNLAASDIHYLYEGLSDHFQRNDDTALDSYSERALARIWKAERF
SWWMTNLLHRFPDMSPADLRLQQADLDYLFSSDAAQASLAENYVGLPY
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