SitesBLAST
Comparing HSERO_RS06550 FitnessBrowser__HerbieS:HSERO_RS06550 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)
45% identity, 95% coverage: 12:448/462 of query aligns to 8:453/471 of O85673
- M43 (= M47) mutation to K: Prevents anthranilate degradation.
- D217 (= D223) 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.
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
31% identity, 79% coverage: 31:397/462 of query aligns to 17:398/435 of 8h2tB
- binding fe (iii) ion: N208 (= N220), H214 (= H226), H219 (= H231), D375 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), K86 (= K100), C104 (= C117), H107 (= H120), W109 (= W122)
- binding 1h-indol-3-ylacetic acid: N208 (= N220), L209 (≠ G221), D211 (= D223), H214 (= H226), P215 (≠ V227), F249 (≠ A257), K320 (≠ M318), Y360 (= Y360)
7ylsB Structure of a bacteria protein complex
31% identity, 79% coverage: 31:397/462 of query aligns to 18:399/436 of 7ylsB
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
29% identity, 79% coverage: 24:387/462 of query aligns to 12:374/432 of 2xrxA
- active site: H106 (= H120), D203 (= D223), H206 (vs. gap), H212 (= H226), D361 (= D374)
- binding biphenyl: Q199 (≠ N220), F200 (≠ G221), D203 (= D223), H206 (vs. gap), H296 (≠ N308), L306 (≠ M318), F309 (= F321), F357 (≠ G370)
- binding fe (ii) ion: Q199 (≠ N220), H206 (vs. gap), H212 (= H226), D361 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
30% identity, 79% coverage: 24:387/462 of query aligns to 12:375/433 of 2yflA
- active site: H106 (= H120), D204 (= D223), H207 (= H226), H213 (= H231), D362 (= D374)
- binding 2-chlorodibenzofuran: Q200 (≠ N220), D204 (= D223), M205 (≠ G224), H207 (= H226), S257 (≠ H268), H297 (≠ N308), L307 (≠ M318), F352 (= F364)
- binding fe (ii) ion: Q200 (≠ N220), H207 (= H226), H213 (= H231), D362 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
30% identity, 79% coverage: 24:387/462 of query aligns to 12:375/433 of 2yfjA
- active site: H106 (= H120), D204 (= D223), H207 (= H226), H213 (= H231), D362 (= D374)
- binding dibenzofuran: Q200 (≠ N220), F201 (≠ G221), D204 (= D223), M205 (≠ G224), H207 (= H226), A208 (≠ V227), H297 (≠ N308), L307 (≠ M318), F358 (≠ G370)
- binding fe (ii) ion: Q200 (≠ N220), H207 (= H226), H213 (= H231), D362 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
29% identity, 80% coverage: 21:391/462 of query aligns to 6:367/425 of 1uliC
- active site: H105 (= H120), D205 (= D223), H208 (= H226), H214 (≠ N233), D350 (= D374)
- binding fe (ii) ion: H208 (= H226), H214 (≠ N233), D350 (= D374)
- binding fe2/s2 (inorganic) cluster: C82 (= C97), H84 (= H99), R85 (≠ K100), C102 (= C117), Y104 (≠ F119), H105 (= H120), W107 (= W122)
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, 80% coverage: 21:391/462 of query aligns to 22:395/460 of Q53122
- C98 (= C97) binding
- H100 (= H99) binding
- C118 (= C117) binding
- H121 (= H120) binding
- 217:230 (vs. 220:237, 21% identical) binding
- H224 (= H226) binding
- H230 (≠ T237) binding
- D378 (= D374) binding
3en1A Crystal structure of toluene 2,3-dioxygenase (see paper)
29% identity, 77% coverage: 36:391/462 of query aligns to 21:377/424 of 3en1A
- active site: H105 (= H120), D205 (= D223), H208 (= H226), H214 (≠ W232), D360 (= D374)
- binding fe (ii) ion: Q201 (≠ N220), H208 (= H226), H214 (≠ W232), D360 (= D374)
- binding fe2/s2 (inorganic) cluster: C82 (= C97), H84 (= H99), R85 (≠ K100), C102 (= C117), Y104 (≠ F119), H105 (= H120), W107 (= W122)
- binding toluene: Q201 (≠ N220), F202 (≠ G221), D205 (= D223), H208 (= H226), H295 (≠ N308)
1uljA Biphenyl dioxygenase (bpha1a2) in complex with the substrate (see paper)
28% identity, 80% coverage: 21:391/462 of query aligns to 6:369/425 of 1uljA
- active site: H105 (= H120), D205 (= D223), H208 (= H226), H214 (≠ N233), D352 (= D374)
- binding biphenyl: Q201 (≠ N220), F202 (≠ G221), D205 (= D223), M206 (≠ G224), H208 (= H226), A209 (≠ V227), H214 (≠ N233), I252 (≠ T275), H287 (≠ N308), L297 (≠ M318), F342 (= F364)
- binding fe (ii) ion: Q201 (≠ N220), H208 (= H226), H214 (≠ N233), D352 (= D374)
- binding fe2/s2 (inorganic) cluster: C82 (= C97), H84 (= H99), R85 (≠ K100), M87 (≠ A102), C102 (= C117), Y104 (≠ F119), H105 (= H120), W107 (= W122)
5aeuA Crystal structure of ii9 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 (see paper)
29% identity, 79% coverage: 24:387/462 of query aligns to 12:375/433 of 5aeuA
- active site: H106 (= H120), D204 (= D223), H207 (= H226), H213 (= H231), D362 (= D374)
- binding fe (ii) ion: H207 (= H226), H213 (= H231), D362 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), M88 (≠ A102), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
2xshA Crystal structure of p4 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 in complex with 2,6 di chlorobiphenyl (see paper)
29% identity, 79% coverage: 24:387/462 of query aligns to 12:375/433 of 2xshA
- active site: H106 (= H120), D204 (= D223), H207 (= H226), H213 (= H231), D362 (= D374)
- binding 2,6-dichlorobiphenyl: F201 (≠ G221), M205 (≠ G224), H207 (= H226), Q296 (≠ R307), H297 (≠ N308), L307 (≠ M318), F358 (≠ G370)
- binding fe (ii) ion: Q200 (≠ N220), H207 (= H226), H213 (= H231), D362 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
2b1xA Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. (see paper)
29% identity, 86% coverage: 11:408/462 of query aligns to 4:413/441 of 2b1xA
- active site: H111 (= H120), D213 (= D223), H216 (= H226), H221 (= H231), D372 (= D374)
- binding fe (iii) ion: H216 (= H226), H221 (= H231), D372 (= D374)
- binding fe2/s2 (inorganic) cluster: C88 (= C97), H90 (= H99), R91 (≠ K100), C108 (= C117), Y110 (≠ F119), H111 (= H120), W113 (= W122)
2b24A Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. Bound to indole (see paper)
29% identity, 86% coverage: 11:408/462 of query aligns to 4:413/440 of 2b24A
- active site: H111 (= H120), D213 (= D223), H216 (= H226), H221 (= H231), D372 (= D374)
- binding fe (iii) ion: H216 (= H226), H221 (= H231), D372 (= D374)
- binding fe2/s2 (inorganic) cluster: C88 (= C97), H90 (= H99), R91 (≠ K100), C108 (= C117), Y110 (≠ F119), H111 (= H120), W113 (= W122)
- binding indole: D213 (= D223), H295 (vs. gap), F307 (= F316)
1wqlA Cumene dioxygenase (cuma1a2) from pseudomonas fluorescens ip01 (see paper)
29% identity, 80% coverage: 24:391/462 of query aligns to 12:382/436 of 1wqlA
- active site: H106 (= H120), D208 (= D223), H211 (= H226), H217 (≠ W232), D365 (= D374)
- binding fe (ii) ion: H211 (= H226), H217 (≠ W232), D365 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
- binding oxygen molecule: H211 (= H226), F355 (= F364)
3gzxA Crystal structure of the biphenyl dioxygenase in complex with biphenyl from comamonas testosteroni sp. Strain b-356 (see paper)
28% identity, 78% coverage: 24:382/462 of query aligns to 12:377/440 of 3gzxA
- active site: H106 (= H120), D213 (= D223), H216 (= H226), H222 (≠ S229), D369 (= D374)
- binding biphenyl: Q209 (≠ N220), F210 (≠ G221), H216 (= H226), G302 (≠ A304), H304 (≠ N308), L314 (≠ M318)
- binding fe (ii) ion: Q209 (≠ N220), H216 (= H226), H222 (≠ S229), D369 (= D374)
- binding fe2/s2 (inorganic) cluster: C83 (= C97), H85 (= H99), R86 (≠ K100), C103 (= C117), Y105 (≠ F119), H106 (= H120), W108 (= W122)
2gbxA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 bound to biphenyl (see paper)
27% identity, 88% coverage: 34:441/462 of query aligns to 12:416/449 of 2gbxA
- active site: H98 (= H120), D199 (= D223), H202 (= H226), H207 (≠ Y234), D355 (= D374)
- binding biphenyl: D199 (= D223), V203 (= V227), L255 (≠ V261), H288 (≠ Q305), N290 (= N308), L300 (≠ M318)
- binding fe (iii) ion: H202 (= H226), H207 (≠ Y234), D355 (= D374)
- binding fe2/s2 (inorganic) cluster: C75 (= C97), H77 (= H99), R78 (≠ K100), C95 (= C117), Y97 (≠ F119), H98 (= H120), W100 (= W122)
2gbwA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 (see paper)
27% identity, 88% coverage: 34:441/462 of query aligns to 12:416/449 of 2gbwA
- active site: H98 (= H120), D199 (= D223), H202 (= H226), H207 (≠ Y234), D355 (= D374)
- binding fe (iii) ion: H202 (= H226), H207 (≠ Y234), D355 (= D374)
- binding fe2/s2 (inorganic) cluster: C75 (= C97), H77 (= H99), R78 (≠ K100), C95 (= C117), Y97 (≠ F119), H98 (= H120), W100 (= W122)
- binding oxygen molecule: H202 (= H226), F345 (= F364), D355 (= D374)
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)
29% identity, 73% coverage: 36:374/462 of query aligns to 20:362/449 of P0A111
- C81 (= C97) binding
- H83 (= H99) binding
- C101 (= C117) binding
- H104 (= H120) binding
- H208 (= H226) binding
- H213 (≠ Y234) binding
- F352 (= F364) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D374) 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)
29% identity, 73% coverage: 36:374/462 of query aligns to 20:362/449 of P0A110
- C81 (= C97) binding
- H83 (= H99) binding
- C101 (= C117) binding
- H104 (= H120) binding
- N201 (= N220) mutation to A: Unable to catalyze the cis-dihydroxylation of biphenyl.
- F202 (≠ G221) mutation to L: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
- H208 (= H226) binding
- H213 (≠ Y234) binding
- F352 (= F364) 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 (≠ G370) 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 (= D374) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
Query Sequence
>HSERO_RS06550 FitnessBrowser__HerbieS:HSERO_RS06550
MNTTAAADRYDELDTLLQSALQEDKDNGVFRCRRDIFTNPDLFELEMKHLFESNWVYLAH
ESQIPEINDYYTTWIGRQPVVITRDKSGQLNAVINACSHKGAMLCRRKHGNKSSFTCPFH
GWTFSNSGKLLKVKDEKTTEYPVSFNKNGSHDLTRVARFQSYRGFLFGSLSEDVLPLEEY
LGETRVIIDQIVDQAPNGLEVLRGNSSYLYDGNWKMQMENGCDGYHVSSVHWNYAATMSR
RKEGGTKATDANNWSKAVAGVYGFENGHILLWTNTLNPEVRPIWNQREELAARVGQARAD
TIVAQTRNLCLYPNVFLMDQFGTQIRVARPISVDKTEISIFCFAPKGESEEDRRVRIRQY
EDFFNVSGMGTADDLEEFRACQAGYAGSAVRWNDMSRGAPLWKEGPDENARKMGMHPKLS
GERSEDEGLFVCQHHYWTEQMRKAVKKERAAAQQGSQQGAQA
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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