SitesBLAST
Comparing CCNA_02487 FitnessBrowser__Caulo:CCNA_02487 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, 96% coverage: 16:404/406 of query aligns to 1:389/391 of 1pbcA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding 2-hydroxy-4-aminobenzoic acid: V47 (= V62), W185 (= W200), L199 (= L214), Y201 (= Y216), L210 (= L225), S212 (= S227), R214 (= R229), Y222 (= Y237), P293 (= P308), T294 (= T309)
- binding flavin-adenine dinucleotide: G9 (= G24), P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), Q102 (= Q117), D159 (= D174), I164 (≠ V179), G285 (= G300), D286 (= D301), G298 (= G313)
1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0 (see paper)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of 1iusA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding flavin-adenine dinucleotide: G11 (= G26), P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), V47 (= V62), Q102 (= Q117), D159 (= D174), D286 (= D301), A296 (= A311), K297 (= K312), G298 (= G313), L299 (≠ M314), N300 (= N315)
- binding 4-aminobenzoic acid: Y201 (= Y216), L210 (= L225), S212 (= S227), R214 (= R229), Y222 (= Y237), P293 (= P308)
1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis (see paper)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of 1dodA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding 2,4-dihydroxybenzoic acid: V47 (= V62), Y201 (= Y216), S212 (= S227), R214 (= R229), Y222 (= Y237), P293 (= P308), T294 (= T309), A296 (= A311)
- binding flavin-adenine dinucleotide: P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), Q102 (= Q117), D159 (= D174), Y222 (= Y237), D286 (= D301), P293 (= P308), G298 (= G313)
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)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of 1d7lA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide: G9 (= G24), G11 (= G26), P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), G46 (= G61), V47 (= V62), Q102 (= Q117), D159 (= D174), I164 (≠ V179), D286 (= D301), A296 (= A311), K297 (= K312), G298 (= G313), L299 (≠ M314), N300 (= N315)
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)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of P20586
- S13 (≠ A28) binding
- E32 (= E47) binding
- RIRAGV 42:47 (≠ RVRAGV 57:62) binding
- A45 (= A60) mutation to G: The positions of the substrate and the flavin are not altered.
- Q102 (= Q117) binding
- Y201 (= Y216) Important for catalytic activity; binding ; mutation to F: Reduction of hydroxylase activity.
- SQR 212:214 (≠ SMR 227:229) binding
- R220 (= R235) mutation to Q: Lower affinity for p-OHB than the wild-type.
- Y222 (= Y237) binding
- D286 (= D301) binding
- P293 (= P308) binding
- LN 299:300 (≠ MN 314:315) binding
- N300 (= N315) 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 (= Y400) 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)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/391 of 1bf3A
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding flavin-adenine dinucleotide: P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R44 (= R59), A45 (= A60), G46 (= G61), V47 (= V62), Q102 (= Q117), D159 (= D174), D286 (= D301), A296 (= A311), G298 (= G313), L299 (≠ M314), N300 (= N315)
P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 11 papers)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of P00438
- S13 (≠ A28) binding
- E32 (= E47) binding
- R33 (= R48) 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 (≠ K49) 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 (= Y53) 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 (= R57) 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 57:62) binding
- R44 (= R59) 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 (= Q117) binding
- C116 (≠ R131) mutation to S: Slight decrease of affinity for NADPH and p-OHB are observed.
- F161 (≠ Y176) mutation to A: Decrease of affinity for NADPH.; mutation to G: Decrease of affinity for NADPH.
- H162 (= H177) 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 (= R181) 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 (= Y216) binding
- SQR 212:214 (≠ SMR 227:229) binding
- R214 (= R229) mutation to K: Strong decrease of affinity for NADPH and 4-fold decrease of affinity for p-OHB are observed.
- Y222 (= Y237) 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 (= R284) 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 (= D301) binding
- P293 (= P308) binding
- LN 299:300 (≠ MN 314:315) 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, 96% coverage: 16:404/406 of query aligns to 1:389/391 of 2phhA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding adenosine-5-diphosphoribose: I8 (≠ V23), P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), Q102 (= Q117), D159 (= D174), I164 (≠ V179), G285 (= G300), D286 (= D301), G298 (= G313), L299 (≠ M314)
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, 96% coverage: 16:404/406 of query aligns to 1:389/391 of 1pdhA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding arabino-flavin-adenine dinucleotide: P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), Q102 (= Q117), D159 (= D174), Y222 (= Y237), D286 (= D301), P293 (= P308), G298 (= G313)
1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb (see paper)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of 1k0lA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding flavin-adenine dinucleotide: P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), A45 (= A60), Q102 (= Q117), V127 (= V142), D159 (= D174), G160 (= G175), D286 (= D301), A296 (= A311), G298 (= G313), L299 (≠ M314)
- binding sulfite ion: D131 (= D146), Q133 (≠ E148)
1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb (see paper)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:389/394 of 1k0jA
- active site: H72 (= H87), Y201 (= Y216), P293 (= P308), K297 (= K312), Y385 (= Y400)
- binding flavin-adenine dinucleotide: P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), G46 (= G61), V47 (= V62), Q102 (= Q117), D159 (= D174), D286 (= D301), P293 (= P308), G298 (= G313), L299 (≠ M314), N300 (= N315)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R44 (= R59), F161 (≠ Y176), H162 (= H177), R269 (= R284)
1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound (see paper)
61% identity, 96% coverage: 16:404/406 of query aligns to 1:387/392 of 1ykjB
- active site: H70 (= H87), Y199 (= Y216), P291 (= P308), K295 (= K312), Y383 (= Y400)
- binding flavin-adenine dinucleotide: I8 (≠ V23), G9 (= G24), P12 (= P27), S13 (≠ A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), G45 (≠ A60), V47 (= V62), Q100 (= Q117), D157 (= D174), G158 (= G175), D284 (= D301), P291 (= P308), G296 (= G313), L297 (≠ M314), N298 (= N315)
- binding pyrosulfate: R33 (= R48), A123 (≠ D140), E124 (≠ A141), R126 (= R143), H160 (= H177), P265 (= P282), R267 (= R284)
6dllB 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
59% identity, 97% coverage: 13:405/406 of query aligns to 1:394/398 of 6dllB
- active site: H75 (= H87), Y204 (= Y216), P296 (= P308), K300 (= K312), Y389 (= Y400)
- binding flavin-adenine dinucleotide: P15 (= P27), S16 (≠ A28), E35 (= E47), R36 (= R48), R45 (= R57), R47 (= R59), A48 (= A60), Q105 (= Q117), C161 (= C173), D162 (= D174), I167 (≠ V179), Y225 (= Y237), D289 (= D301), P296 (= P308), G301 (= G313)
7on9A Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
51% identity, 96% coverage: 16:405/406 of query aligns to 1:392/393 of 7on9A
- binding flavin-adenine dinucleotide: I8 (≠ V23), G11 (= G26), P12 (= P27), A13 (= A28), E32 (= E47), N33 (≠ R48), R34 (≠ K49), R44 (= R59), A45 (= A60), G46 (= G61), V47 (= V62), Q102 (= Q117), D161 (= D174), P166 (≠ V179), V268 (≠ A281), G287 (= G300), D288 (= D301), P295 (= P308), A298 (= A311), G300 (= G313), L301 (≠ M314), N302 (= N315)
8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
46% identity, 96% coverage: 16:405/406 of query aligns to 1:390/391 of 8jqoA
- binding flavin-adenine dinucleotide: G11 (= G26), P12 (= P27), A13 (= A28), E32 (= E47), R33 (= R48), R42 (= R57), R44 (= R59), V47 (= V62), Q102 (= Q117), V126 (≠ A141), D159 (= D174), G160 (= G175), G285 (= G300), D286 (= D301), A296 (= A311), K297 (= K312), G298 (= G313), L299 (≠ M314), N300 (= N315)
8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
40% identity, 96% coverage: 18:405/406 of query aligns to 1:308/309 of 8jqoD
- binding flavin-adenine dinucleotide: G7 (= G24), P10 (= P27), V19 (= V62), D78 (= D174), G79 (= G175), T184 (≠ A281), G203 (= G300), D204 (= D301), A214 (= A311), G216 (= G313), L217 (≠ M314), N218 (= N315)
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: 20:356/406 of query aligns to 4:324/476 of F2R776
- T12 (≠ A28) binding
- E31 (= E47) binding
- K32 (≠ R48) binding
- Q98 (≠ M113) binding
- L122 (≠ V136) binding
- T156 (= T183) binding
- R196 (= R229) binding
- R213 (≠ Y237) binding
- D277 (= D301) binding
- L290 (≠ M314) binding
- N291 (= N315) binding
6brdA Crystal structure of rifampin monooxygenase from streptomyces venezuelae, complexed with rifampin and fad (see paper)
27% identity, 83% coverage: 20:356/406 of query aligns to 4:324/474 of 6brdA
- active site: Q43 (≠ R59), L207 (vs. gap), V215 (≠ Q239), P284 (= P308), Q288 (≠ K312)
- binding flavin-adenine dinucleotide: V7 (= V23), G10 (= G26), P11 (= P27), T12 (≠ A28), E31 (= E47), K32 (≠ R48), R41 (= R57), A42 (≠ V58), Q98 (≠ M113), L122 (≠ V136), D151 (= D174), G152 (= G175), T156 (= T183), D277 (= D301), P284 (= P308), G287 (≠ A311), G289 (= G313), L290 (≠ M314)
- binding rifampicin: H46 (≠ E64), F74 (≠ N91), R196 (= R229), R201 (= R235), M205 (vs. gap), V215 (≠ Q239), T285 (= T309), G286 (= G310)
Sites not aligning to the query:
7yj0D Structural basis of oxepinone formation by a flavin-monooxygenase vibo
25% identity, 77% coverage: 17:328/406 of query aligns to 52:376/622 of 7yj0D
- binding flavin-adenine dinucleotide: I58 (≠ V23), G59 (= G24), G61 (= G26), P62 (= P27), V63 (≠ A28), D82 (≠ E47), R83 (= R48), R92 (= R59), A93 (= A60), Q155 (= Q130), A179 (vs. gap), D218 (= D174), G219 (= G175), D349 (= D301), A356 (≠ P308), G361 (= G313)
4k2xB Oxys anhydrotetracycline hydroxylase from streptomyces rimosus (see paper)
27% identity, 84% coverage: 16:356/406 of query aligns to 1:323/490 of 4k2xB
- active site: L44 (≠ A60), L210 (≠ R229), T218 (≠ Q239), P283 (= P308)
- binding flavin-adenine dinucleotide: G9 (= G24), G11 (= G26), P12 (= P27), T13 (≠ A28), L31 (= L46), E32 (= E47), R33 (= R48), K42 (≠ V58), A43 (≠ R59), Q99 (= Q118), V123 (= V147), D155 (= D174), G156 (= G175), T160 (≠ V179), G275 (= G300), D276 (= D301), P283 (= P308), G286 (≠ A311), Q287 (≠ K312), G288 (= G313), L289 (≠ M314), N290 (= N315)
Query Sequence
>CCNA_02487 FitnessBrowser__Caulo:CCNA_02487
MMQVVSGGVRAESSIVRTQVAIVGAGPAGLFLGHLLRQAGVDVVILERKDRAYVEGRVRA
GVLERITVELMERLGVDERMRREGLVHAGANLASDGEMFRIDMAELTGGSTVMVYGQQEV
MKDLFDAAEQRDLRIVFDADAVRLHDVEGERPHITWRKDGAEHRLDCDFIAGCDGYHGVS
RATIPDKVLKTFERVYPFGWLGILAEAPPCDHELIYSNHDRGFALASMRSPTRSRYYVQC
SLDDRLEDWSDERFWDEVSVRLGPEAAARIVRAPSFEKSIAPLRSFVSEPMRYGRLFLAG
DAAHIVPPTGAKGMNLAVSDVIMLSEALVEHYHERSSAGIDGYSARALARVWKAERFSWW
FTSLTHRFPDQDGFDRKMQVAELAYIKGSRAAQVTLAENYVGLPLV
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