Sites on a Tree

 

Searching for up to 100 curated homologs for Pf6N2E2_2914 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2914 (396 a.a.)

Found high-coverage hits (≥70%) to 34 curated proteins.

Removed hits that are identical to the query, leaving 33

You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.

Hits with ≥ 30% identity

pobA / P00438 p-hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas fluorescens (see 2 papers)
PHHY_PSEFL / P00438 p-hydroxybenzoate hydroxylase; PHBH; PHBHase; 4-hydroxybenzoate 3-monooxygenase; EC 1.14.13.2 from Pseudomonas fluorescens (see 13 papers)
    76% identity, 99% coverage of query (623 bits)

PHHY_PSEAE / 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)
1d7lA / P20586 Structure-function correlations of the reaction of reduced nicotinamide analogs with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins (see paper)
    76% identity, 99% coverage of query (623 bits)

1iusA P-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate at ph 5.0
    76% identity, 99% coverage of query (623 bits)

1dodA The mobil flavin of 4-oh benzoate hydroxylase: motion of a prosthetic group regulates catalysis
    76% identity, 99% coverage of query (623 bits)

1k0lA Pseudomonas aeruginosa phbh r220q free of p-ohb
    75% identity, 99% coverage of query (621 bits)

1k0jA Pseudomonas aeruginosa phbh r220q in complex with NADPH and free of p- ohb
    75% identity, 99% coverage of query (621 bits)

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
    76% identity, 98% coverage of query (620 bits)

2phhA The coenzyme analogue adenosine 5-diphosphoribose displaces fad in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation
    76% identity, 98% coverage of query (620 bits)

1pdhA Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified fad present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin
    76% identity, 98% coverage of query (620 bits)

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
    76% identity, 98% coverage of query (619 bits)

8y2sA 4-hydroxybenzoate 3-monooxygenase
    76% identity, 98% coverage of query (618 bits)

1ykjB A45g p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound
    75% identity, 99% coverage of query (613 bits)

pobA / Q9R9T1 p-hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas putida (see paper)
Q9R9T1 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) from Pseudomonas putida (see paper)
    71% identity, 99% coverage of query (588 bits)

6dllB / Q88H28 2.2 angstrom resolution crystal structure of p-hydroxybenzoate hydroxylase from pseudomonas putida in complex with fad. (see paper)
    69% identity, 99% coverage of query (582 bits)

pobA / F2JUE7 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) from Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1) (see paper)
    65% identity, 99% coverage of query (550 bits)

pobA / AAA73519.1 4-hydroxybenzoate hydroxylase from Rhizobium leguminosarum (see paper)
    61% identity, 98% coverage of query (504 bits)

RR42_RS21940 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) from Cupriavidus basilensis FW507-4G11
    63% identity, 98% coverage of query (471 bits)

7on9A / C4TP09 Crystal structure of para-hydroxybenzoate-3-hydroxylase prai (see paper)
    51% identity, 98% coverage of query (393 bits)

PRAI_PAESP / C4TP09 4-hydroxybenzoate 3-monooxygenase (NAD(P)H); 4-hydroxybenzoate 3-hydroxylase; 4HB 3-hydroxylase; EC 1.14.13.33 from Paenibacillus sp. (see paper)
praI / BAH79107.1 4-hydroxybenzoate 3-hydroxylase from Paenibacillus sp. JJ-1b (see paper)
    51% identity, 98% coverage of query (393 bits)

8jqoA Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
    46% identity, 98% coverage of query (360 bits)

8jqoD Protocatecuate hydroxylase from xylophilus ampelinus complexed with imidazole (see paper)
    38% identity, 98% coverage of query (254 bits)

Build an alignment

Build an alignment for Pf6N2E2_2914 and 21 homologs with ≥ 30% identity

Select sequences

Add sequences from UniProt, PDB, RefSeq, or MicrobesOnline (separate identifiers with commas or spaces):

Or download the sequences

Change minimum %identity:

Additional hits (identity < 30%)

nat2 / F8QPH2 ansamycin ring hydroxylase from Streptomyces sp. CS (see 5 papers)
    26% identity, 83% coverage of query (64.3 bits)

tsdB / Q0SFL5 resorcinol 4-hydroxylase (NADH) (EC 1.14.13.220) from Rhodococcus jostii (strain RHA1) (see 2 papers)
TSDB_RHOJR / Q0SFL5 Probable NADH-specific resorcinol 4-hydroxylase; EC 1.14.13.220 from Rhodococcus jostii (strain RHA1) (see paper)
    26% identity, 82% coverage of query (60.8 bits)

rif19 / Q9AE02 rifamycin ring hydroxylase from Amycolatopsis mediterranei (see 4 papers)
    24% identity, 78% coverage of query (58.9 bits)

hspB / F8G0M4 6-hydroxy-3-succinoyl-pyridine hydroxylase monomer (EC 1.14.13.163) from Pseudomonas putida (strain DSM 28022 / S16) (see paper)
HSPB_PSEP6 / F8G0M4 6-hydroxy-3-succinoylpyridine 3-monooxygenase HspB; 6-hydroxy-3-succinoylpyridine hydroxylase; HSP hydroxylase; EC 1.14.13.163 from Pseudomonas putida (strain DSM 28022 / S16) (see 2 papers)
F8G0M4 6-hydroxy-3-succinoylpyridine 3-monooxygenase (EC 1.14.13.163) from Pseudomonas putida (see paper)
    25% identity, 84% coverage of query (56.6 bits)

PHZS_LYSAN / A0A172J1S0 Phenazine 1,6-dicarboxylic acid hydroxylase PhzS; Flavin-containing monooxygenase; Phenazine 1-carboxylic acid hydroxylase; EC 1.14.13.-; EC 1.14.13.218 from Lysobacter antibioticus (see 2 papers)
    27% identity, 83% coverage of query (54.7 bits)

PYRE3_STRRG / K7QRJ5 Dialkyldecalin synthase; FAD-dependent [4+2] cyclase; EC 5.5.1.- from Streptomyces rugosporus (see 2 papers)
    27% identity, 78% coverage of query (53.1 bits)

5xgvA / K7QRJ5 The structure of diels-alderase pyre3 in the biosynthetic pathway of pyrroindomycins (see paper)
    28% identity, 77% coverage of query (53.1 bits)

4k2xB / L8EUQ6 Oxys anhydrotetracycline hydroxylase from streptomyces rimosus (see paper)
    25% identity, 83% coverage of query (53.1 bits)

oxyS / L8EUQ6 anhydrotetracycline monooxygenase monomer (EC 1.14.13.234; EC 1.14.13.38) from Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM 4667 / NRRL 2234) (see 6 papers)
OXYS_STRR1 / L8EUQ6 12-dehydrotetracycline 5-monooxygenase/anhydrotetracycline 6-monooxygenase; EC 1.14.13.234; EC 1.14.13.38 from Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM 4667 / NRRL 2234) (see paper)
L8EUQ6 5a,11a-dehydrotetracycline 5-monooxygenase (EC 1.14.13.234) from Streptomyces rimosus subsp. rimosus (see paper)
    24% identity, 83% coverage of query (52.8 bits)

MhpA / b0347 3-(3-hydroxyphenyl)propanoate hydroxylase (EC 1.14.13.127) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
mhpA / P77397 3-(3-hydroxyphenyl)propanoate hydroxylase (EC 1.14.13.127) from Escherichia coli (strain K12) (see 4 papers)
MHPA_ECOLI / P77397 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; 3-HCI hydroxylase; 3-HPP hydroxylase; EC 1.14.13.127 from Escherichia coli (strain K12) (see paper)
    21% identity, 83% coverage of query (51.6 bits)

7oujAAA / Q8KY42 7oujAAA (see paper)
    27% identity, 77% coverage of query (50.8 bits)

8fhjC Crystal structure of a fad monooxygenease from methylocystis sp. Strain sb2 (see paper)
    25% identity, 83% coverage of query (48.1 bits)

Or start over

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory