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Comparing AO353_05950 FitnessBrowser__pseudo3_N2E3:AO353_05950 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)
75% identity, 99% coverage: 5:462/462 of query aligns to 4:460/471 of O85673
- M43 (= M44) mutation to K: Prevents anthranilate degradation.
- D217 (= D218) 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)
28% identity, 82% coverage: 28:404/462 of query aligns to 17:398/435 of 8h2tB
- binding fe (iii) ion: N208 (= N215), H214 (= H221), H219 (= H226), D375 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), K86 (≠ R97), C104 (= C114), H107 (= H117), W109 (= W119)
- binding 1h-indol-3-ylacetic acid: N208 (= N215), L209 (≠ G216), D211 (= D218), H214 (= H221), P215 (≠ V222), F249 (≠ L256), K320 (≠ L325), Y360 (≠ F367)
7ylsB Structure of a bacteria protein complex
28% identity, 82% coverage: 28:404/462 of query aligns to 18:399/436 of 7ylsB
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
28% identity, 79% coverage: 33:395/462 of query aligns to 22:379/433 of 2yflA
- active site: H106 (= H117), D204 (= D218), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding 2-chlorodibenzofuran: Q200 (≠ N215), D204 (= D218), M205 (≠ G219), H207 (= H221), S257 (≠ H274), H297 (≠ N315), L307 (= L325), F352 (= F371)
- binding fe (ii) ion: Q200 (≠ N215), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
28% identity, 79% coverage: 33:395/462 of query aligns to 22:379/433 of 2yfjA
- active site: H106 (= H117), D204 (= D218), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding dibenzofuran: Q200 (≠ N215), F201 (≠ G216), D204 (= D218), M205 (≠ G219), H207 (= H221), A208 (≠ V222), H297 (≠ N315), L307 (= L325), F358 (≠ G377)
- binding fe (ii) ion: Q200 (≠ N215), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
2xshA Crystal structure of p4 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 in complex with 2,6 di chlorobiphenyl (see paper)
28% identity, 79% coverage: 33:395/462 of query aligns to 22:379/433 of 2xshA
- active site: H106 (= H117), D204 (= D218), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding 2,6-dichlorobiphenyl: F201 (≠ G216), M205 (≠ G219), H207 (= H221), Q296 (≠ R314), H297 (≠ N315), L307 (= L325), F358 (≠ G377)
- binding fe (ii) ion: Q200 (≠ N215), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
3en1A Crystal structure of toluene 2,3-dioxygenase (see paper)
29% identity, 80% coverage: 28:395/462 of query aligns to 16:377/424 of 3en1A
- active site: H105 (= H117), D205 (= D218), H208 (= H221), H214 (= H226), D360 (= D381)
- binding fe (ii) ion: Q201 (≠ N215), H208 (= H221), H214 (= H226), D360 (= D381)
- binding fe2/s2 (inorganic) cluster: C82 (= C94), H84 (= H96), R85 (= R97), C102 (= C114), Y104 (≠ F116), H105 (= H117), W107 (= W119)
- binding toluene: Q201 (≠ N215), F202 (≠ G216), D205 (= D218), H208 (= H221), H295 (≠ N315)
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
28% identity, 79% coverage: 33:395/462 of query aligns to 22:378/432 of 2xrxA
- active site: H106 (= H117), D203 (= D218), H206 (= H221), H212 (≠ Y227), D361 (= D381)
- binding biphenyl: Q199 (≠ N215), F200 (≠ G216), D203 (= D218), H206 (= H221), H296 (≠ N315), L306 (= L325), F309 (≠ I328), F357 (≠ G377)
- binding fe (ii) ion: Q199 (≠ N215), H206 (= H221), H212 (≠ Y227), D361 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
5aeuA Crystal structure of ii9 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 (see paper)
28% identity, 79% coverage: 33:395/462 of query aligns to 22:379/433 of 5aeuA
- active site: H106 (= H117), D204 (= D218), H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding fe (ii) ion: H207 (= H221), H213 (≠ Y227), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), M88 (≠ T99), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
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)
27% identity, 80% coverage: 28:395/462 of query aligns to 32:395/460 of Q53122
- C98 (= C94) binding
- H100 (= H96) binding
- C118 (= C114) binding
- H121 (= H117) binding
- 217:230 (vs. 215:227, 29% identical) binding
- H224 (= H221) binding
- H230 (≠ Y227) binding
- D378 (= D381) binding
2b24A Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. Bound to indole (see paper)
36% identity, 44% coverage: 29:230/462 of query aligns to 23:225/440 of 2b24A
- active site: H111 (= H117), D213 (= D218), H216 (= H221), H221 (= H226)
- binding fe (iii) ion: H216 (= H221), H221 (= H226)
- binding fe2/s2 (inorganic) cluster: C88 (= C94), H90 (= H96), R91 (= R97), C108 (= C114), Y110 (≠ F116), H111 (= H117), W113 (= W119)
- binding indole: D213 (= D218)
Sites not aligning to the query:
2b1xA Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. (see paper)
36% identity, 44% coverage: 29:230/462 of query aligns to 23:225/441 of 2b1xA
- active site: H111 (= H117), D213 (= D218), H216 (= H221), H221 (= H226)
- binding fe (iii) ion: H216 (= H221), H221 (= H226)
- binding fe2/s2 (inorganic) cluster: C88 (= C94), H90 (= H96), R91 (= R97), C108 (= C114), Y110 (≠ F116), H111 (= H117), W113 (= W119)
Sites not aligning to the query:
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
27% identity, 80% coverage: 28:395/462 of query aligns to 16:367/425 of 1uliC
- active site: H105 (= H117), D205 (= D218), H208 (= H221), H214 (≠ Y227), D350 (= D381)
- binding fe (ii) ion: H208 (= H221), H214 (≠ Y227), D350 (= D381)
- binding fe2/s2 (inorganic) cluster: C82 (= C94), H84 (= H96), R85 (= R97), C102 (= C114), Y104 (≠ F116), H105 (= H117), W107 (= W119)
1uljA Biphenyl dioxygenase (bpha1a2) in complex with the substrate (see paper)
27% identity, 80% coverage: 28:395/462 of query aligns to 16:369/425 of 1uljA
- active site: H105 (= H117), D205 (= D218), H208 (= H221), H214 (= H235), D352 (= D381)
- binding biphenyl: Q201 (≠ N215), F202 (≠ G216), D205 (= D218), M206 (≠ G219), H208 (= H221), A209 (≠ V230), H214 (= H235), I252 (≠ M281), H287 (≠ N315), L297 (= L325), F342 (= F371)
- binding fe (ii) ion: Q201 (≠ N215), H208 (= H221), H214 (= H235), D352 (= D381)
- binding fe2/s2 (inorganic) cluster: C82 (= C94), H84 (= H96), R85 (= R97), M87 (≠ T99), C102 (= C114), Y104 (≠ F116), H105 (= H117), W107 (= W119)
1wqlA Cumene dioxygenase (cuma1a2) from pseudomonas fluorescens ip01 (see paper)
29% identity, 79% coverage: 33:395/462 of query aligns to 22:382/436 of 1wqlA
- active site: H106 (= H117), D208 (= D218), H211 (= H221), H217 (= H226), D365 (= D381)
- binding fe (ii) ion: H211 (= H221), H217 (= H226), D365 (= D381)
- binding fe2/s2 (inorganic) cluster: C83 (= C94), H85 (= H96), R86 (= R97), C103 (= C114), Y105 (≠ F116), H106 (= H117), W108 (= W119)
- binding oxygen molecule: H211 (= H221), F355 (= F371)
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)
28% identity, 80% coverage: 33:402/462 of query aligns to 20:383/449 of P0A111
- C81 (= C94) binding
- H83 (= H96) binding
- C101 (= C114) binding
- H104 (= H117) binding
- H208 (= H221) binding
- H213 (= H226) binding
- F352 (= F371) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D381) 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)
28% identity, 80% coverage: 33:402/462 of query aligns to 20:383/449 of P0A110
- C81 (= C94) binding
- H83 (= H96) binding
- C101 (= C114) binding
- H104 (= H117) binding
- N201 (= N215) mutation to A: Unable to catalyze the cis-dihydroxylation of biphenyl.
- F202 (≠ G216) mutation to L: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
- H208 (= H221) binding
- H213 (= H226) binding
- F352 (= F371) 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 (≠ G377) 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 (= D381) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
28% identity, 80% coverage: 33:402/462 of query aligns to 20:383/446 of 4hm8A
- active site: H104 (= H117), D205 (= D218), H208 (= H221), H213 (= H226), D362 (= D381)
- binding (methylsulfanyl)benzene: N201 (= N215), H295 (≠ R312)
- binding fe (iii) ion: H208 (= H221), H213 (= H226), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C81 (= C94), H83 (= H96), R84 (= R97), C101 (= C114), Y103 (≠ F116), H104 (= H117), W106 (= W119)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
28% identity, 80% coverage: 33:402/462 of query aligns to 20:383/446 of 4hm7A
- active site: H104 (= H117), D205 (= D218), H208 (= H221), H213 (= H226), D362 (= D381)
- binding fe (iii) ion: H208 (= H221), H213 (= H226), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C81 (= C94), H83 (= H96), R84 (= R97), C101 (= C114), Y103 (≠ F116), H104 (= H117), W106 (= W119)
- binding ethenylbenzene: N201 (= N215), H208 (= H221), H295 (≠ R312), N297 (= N315)
4hm6A Naphthalene 1,2-dioxygenase bound to phenetole
28% identity, 80% coverage: 33:402/462 of query aligns to 20:383/446 of 4hm6A
- active site: H104 (= H117), D205 (= D218), H208 (= H221), H213 (= H226), D362 (= D381)
- binding ethoxybenzene: N201 (= N215), H208 (= H221), H295 (≠ R312)
- binding fe (iii) ion: H208 (= H221), H213 (= H226), D362 (= D381)
- binding fe2/s2 (inorganic) cluster: C81 (= C94), H83 (= H96), R84 (= R97), C101 (= C114), Y103 (≠ F116), H104 (= H117), W106 (= W119)
Query Sequence
>AO353_05950 FitnessBrowser__pseudo3_N2E3:AO353_05950
MSGEKNVEQWKAFIEGCLDFRPAEGVFRIARDIFTEPQLFDLEMELIFEKNWIYACHESE
LANNHDFITMRAGRQPMIITRDGDGQLNALINACQHRGTTLTRVGKGNQSTFTCPFHAWC
YKSDGRLVKVKAPGEYPEGFDKATRGLKKARIQSYKGFVFISLDVHGDNSLEDFLGDAKV
FFDMMVAQSPTGELEVLPGKSAYTYDGNWKLQNENGLDGYHVSTVHYNYVATVQHRQQVD
SKNGTRASGTLDYSKLGAGDANTDDGWFAFNNGHSVLFSDMPNPTVRSGYATIMPRLIEE
HGQEKAEWMMHRLRNLNIYPSLFFLDQISSQLRIIRPVAWNKTEIISQCLGVKNESDADR
ENRIRQFEDFFNVSGLGTPDDLVEFREAQRGFQARLERWSDISRGSHQWATGATPNSEAI
GIAPAMTGTEFTHEGLYVNQHSNWQKFLLDGLDAKSLKLREV
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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