SitesBLAST
Comparing HSERO_RS06720 FitnessBrowser__HerbieS:HSERO_RS06720 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)
O85673 Anthranilate 1,2-dioxygenase large subunit; EC 1.14.12.1 from Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) (see 2 papers)
36% identity, 82% coverage: 29:379/428 of query aligns to 32:389/471 of O85673
- M43 (= M40) mutation to K: Prevents anthranilate degradation.
- D217 (= D212) mutation to A: In ACN476; loss of dioxygenase activity and 2-fold lower redox potential.; mutation to E: Loss of dioxygenase activity and lack of iron at the mononuclear site.; mutation to N: Loss of dioxygenase activity.
2xshA Crystal structure of p4 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 in complex with 2,6 di chlorobiphenyl (see paper)
28% identity, 95% coverage: 21:428/428 of query aligns to 14:425/433 of 2xshA
- active site: H106 (= H113), D204 (= D212), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding 2,6-dichlorobiphenyl: F201 (vs. gap), M205 (≠ G213), H207 (= H215), Q296 (≠ F305), H297 (≠ N306), L307 (vs. gap), F358 (≠ G365)
- binding fe (ii) ion: Q200 (≠ N209), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C90), H85 (= H92), R86 (= R93), C103 (= C110), Y105 (= Y112), H106 (= H113), W108 (= W115)
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
29% identity, 97% coverage: 12:426/428 of query aligns to 2:411/425 of 1uliC
- active site: H105 (= H113), D205 (= D212), H208 (= H215), H214 (≠ F223), D350 (= D369)
- binding fe (ii) ion: H208 (= H215), H214 (≠ F223), D350 (= D369)
- binding fe2/s2 (inorganic) cluster: C82 (= C90), H84 (= H92), R85 (= R93), C102 (= C110), Y104 (= Y112), H105 (= H113), W107 (= W115)
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
28% identity, 95% coverage: 21:428/428 of query aligns to 14:425/433 of 2yflA
- active site: H106 (= H113), D204 (= D212), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding 2-chlorodibenzofuran: Q200 (≠ N209), D204 (= D212), M205 (≠ G213), H207 (= H215), S257 (≠ D263), H297 (≠ N306), L307 (vs. gap), F352 (= F358)
- binding fe (ii) ion: Q200 (≠ N209), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C90), H85 (= H92), R86 (= R93), C103 (= C110), Y105 (= Y112), H106 (= H113), W108 (= W115)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
28% identity, 95% coverage: 21:428/428 of query aligns to 14:425/433 of 2yfjA
- active site: H106 (= H113), D204 (= D212), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding dibenzofuran: Q200 (≠ N209), F201 (vs. gap), D204 (= D212), M205 (≠ G213), H207 (= H215), A208 (≠ F216), H297 (≠ N306), L307 (vs. gap), F358 (≠ G365)
- binding fe (ii) ion: Q200 (≠ N209), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C90), H85 (= H92), R86 (= R93), C103 (= C110), Y105 (= Y112), H106 (= H113), W108 (= W115)
Q53122 Biphenyl 2,3-dioxygenase subunit alpha; Biphenyl dioxygenase system, oxygenase component subunit alpha; BDO, oxygenase component subunit alpha; Rieske dioxygenase; Terminal oxygenase component of biphenyl dioxygenase, large subunit; EC 1.14.12.18 from Rhodococcus jostii (strain RHA1) (see paper)
28% identity, 98% coverage: 9:426/428 of query aligns to 15:439/460 of Q53122
- C98 (= C90) binding
- H100 (= H92) binding
- C118 (= C110) binding
- H121 (= H113) binding
- 217:230 (vs. 209:220, 29% identical) binding
- H224 (= H215) binding
- H230 (= H220) binding
- D378 (= D369) binding
1uljA Biphenyl dioxygenase (bpha1a2) in complex with the substrate (see paper)
29% identity, 97% coverage: 12:426/428 of query aligns to 2:413/425 of 1uljA
- active site: H105 (= H113), D205 (= D212), H208 (= H215), H214 (≠ E230), D352 (= D369)
- binding biphenyl: Q201 (≠ N209), F202 (vs. gap), D205 (= D212), M206 (≠ G213), H208 (= H215), A209 (≠ S225), H214 (≠ E230), I252 (≠ D267), H287 (≠ N306), L297 (vs. gap), F342 (= F358)
- binding fe (ii) ion: Q201 (≠ N209), H208 (= H215), H214 (≠ E230), D352 (= D369)
- binding fe2/s2 (inorganic) cluster: C82 (= C90), H84 (= H92), R85 (= R93), M87 (≠ A95), C102 (= C110), Y104 (= Y112), H105 (= H113), W107 (= W115)
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
28% identity, 95% coverage: 21:428/428 of query aligns to 14:424/432 of 2xrxA
- active site: H106 (= H113), D203 (= D212), H206 (= H215), H212 (vs. gap), D361 (= D369)
- binding biphenyl: Q199 (≠ N209), F200 (vs. gap), D203 (= D212), H206 (= H215), H296 (≠ N306), L306 (≠ S316), F309 (= F319), F357 (≠ G365)
- binding fe (ii) ion: Q199 (≠ N209), H206 (= H215), H212 (vs. gap), D361 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C90), H85 (= H92), R86 (= R93), C103 (= C110), Y105 (= Y112), H106 (= H113), W108 (= W115)
5aeuA Crystal structure of ii9 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 (see paper)
28% identity, 95% coverage: 21:428/428 of query aligns to 14:425/433 of 5aeuA
- active site: H106 (= H113), D204 (= D212), H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding fe (ii) ion: H207 (= H215), H213 (vs. gap), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C90), H85 (= H92), R86 (= R93), M88 (≠ A95), C103 (= C110), Y105 (= Y112), H106 (= H113), W108 (= W115)
P0A111 Naphthalene 1,2-dioxygenase system, large oxygenase component; ISP NAP; Naphthalene 1,2-dioxygenase ISP alpha; Naphthalene 1,2-dioxygenase subunit alpha; ND subunit alpha; NDO subunit alpha; EC 1.14.12.12 from Pseudomonas sp. (strain C18) (see paper)
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/449 of P0A111
- C81 (= C90) binding
- H83 (= H92) binding
- C101 (= C110) binding
- H104 (= H113) binding
- H208 (= H215) binding
- H213 (= H220) binding
- F352 (≠ Q359) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D369) binding
P0A110 Naphthalene 1,2-dioxygenase system, large oxygenase component; ISP NAP; Naphthalene 1,2-dioxygenase ISP alpha; Naphthalene 1,2-dioxygenase subunit alpha; ND subunit alpha; NDO subunit alpha; EC 1.14.12.12 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 5 papers)
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/449 of P0A110
- C81 (= C90) binding
- H83 (= H92) binding
- C101 (= C110) binding
- H104 (= H113) binding
- N201 (= N209) mutation to A: Unable to catalyze the cis-dihydroxylation of biphenyl.
- F202 (vs. gap) mutation to L: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
- H208 (= H215) binding
- H213 (= H220) binding
- F352 (≠ Q359) Important for enantioselectivity; mutation to L: Cis-dihydroxylation of naphthalene results in the formation of cis-naphthalene dihydrodiol with altered stereochemistry. Cis-dihydroxylation of biphenyl results in the formation of cis-biphenyl 3,4-dihydrodiol as the major product.; mutation to V: Cis-dihydroxylation of naphthalene results in the formation of cis-naphthalene dihydrodiol with altered stereochemistry. Cis-dihydroxylation of biphenyl and phenanthrene results in the formation of cis-biphenyl 3,4-dihydrodiol and cis-phenanthrene 1,2-dihydrodiol as the major product, respectively.
- W358 (≠ G365) mutation to A: Unable to catalyze the cis-dihydroxylation of biphenyl. Preferentially oxidizes phenanthrene at the C-3 and C-4 positions, forming almost no cis-phenanthrene 1,2-dihydrodiol.
- D362 (= D369) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm8A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding (methylsulfanyl)benzene: N201 (= N209), H295 (≠ L300)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm7A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
- binding ethenylbenzene: N201 (= N209), H208 (= H215), H295 (≠ L300), N297 (= N306)
4hm6A Naphthalene 1,2-dioxygenase bound to phenetole
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm6A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding ethoxybenzene: N201 (= N209), H208 (= H215), H295 (≠ L300)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
4hm4A Naphthalene 1,2-dioxygenase bound to indan
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm4A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding 2,3-dihydro-1H-indene: H208 (= H215), H295 (≠ L300), N297 (= N306)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
4hm3A Naphthalene 1,2-dioxygenase bound to ethylbenzene
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm3A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
- binding phenylethane: N201 (= N209), D205 (= D212), H208 (= H215), N297 (= N306)
4hm2A Naphthalene 1,2-dioxygenase bound to ethylphenylsulfide
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm2A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding (ethylsulfanyl)benzene: N201 (= N209), D205 (= D212), V209 (≠ F216), H295 (≠ L300), N297 (= N306)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
4hm1A Naphthalene 1,2-dioxygenase bound to 1-indanone
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hm1A
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding 2,3-dihydro-1H-inden-1-one: N201 (= N209), V209 (≠ F216), N297 (= N306)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
4hkvA Naphthalene 1,2-dioxygenase bound to benzamide
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hkvA
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
- binding benzamide: N201 (= N209), H208 (= H215), H295 (≠ L300), N297 (= N306)
4hjlA Naphthalene 1,2-dioxygenase bound to 1-chloronaphthalene
31% identity, 88% coverage: 29:406/428 of query aligns to 20:398/446 of 4hjlA
- active site: H104 (= H113), D205 (= D212), H208 (= H215), H213 (= H220), D362 (= D369)
- binding 1-chloronaphthalene: N201 (= N209), D205 (= D212), H208 (= H215), H295 (≠ L300), N297 (= N306), L307 (vs. gap)
- binding fe (iii) ion: H208 (= H215), H213 (= H220), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C90), H83 (= H92), R84 (= R93), C101 (= C110), Y103 (= Y112), H104 (= H113), W106 (= W115)
Query Sequence
>HSERO_RS06720 FitnessBrowser__HerbieS:HSERO_RS06720
MNAPLRFHPRKTDSSYADLVQDAVVDPSLYTDPALFEAEMDKIFYKTWIWVAHESEIKNP
GDFKTAQIGRQPVIVVRDKTGKINVLENRCRHRGATVCEKHKGNATGFTCPYHSWSYGLD
GKLRGLPYPEGYEDVIEKADLPLQSLRCESYHGMIFASFNQEIEPLSDFLGHAKKWIDLF
MKQGAGFPIKVQGEHKFSFKGNWKIQLENTTDGYHFPVVHKTFLSSVDEETSEMLSFMTD
DQSITRSLGNGHSVMIMVPEHVDLDVDDGSEQLQERFAHVTEELSKTMPPEQVRRIVRSL
HGAGFNLNLFPNVAMSMSFFRVLHPVSVGETQIRHVALGMDGGPEIANRERLRIHEHFQG
PFGFGSPDDAEAWERVQAGSHAGRDAPILVNRGLNREWVDDNGDKVSHSTDETGMREAYA
MWKKMMEK
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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