SitesBLAST
Comparing BPHYT_RS07855 FitnessBrowser__BFirm:BPHYT_RS07855 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)
48% identity, 93% coverage: 25:446/452 of query aligns to 23:453/471 of O85673
- M43 (= M45) mutation to K: Prevents anthranilate degradation.
- D217 (= D221) 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)
30% identity, 85% coverage: 13:395/452 of query aligns to 7:398/435 of 8h2tB
- binding fe (iii) ion: N208 (= N218), H214 (= H224), H219 (= H229), D375 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), K86 (= K98), C104 (= C115), H107 (= H118), W109 (= W120)
- binding 1h-indol-3-ylacetic acid: N208 (= N218), L209 (≠ G219), D211 (= D221), H214 (= H224), P215 (≠ V225), F249 (≠ S255), K320 (≠ M316), Y360 (= Y358)
7ylsB Structure of a bacteria protein complex
30% identity, 85% coverage: 13:395/452 of query aligns to 8:399/436 of 7ylsB
2b1xA Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. (see paper)
28% identity, 96% coverage: 8:439/452 of query aligns to 3:435/441 of 2b1xA
- active site: H111 (= H118), D213 (= D221), H216 (= H224), H221 (= H229), D372 (= D372)
- binding fe (iii) ion: H216 (= H224), H221 (= H229), D372 (= D372)
- binding fe2/s2 (inorganic) cluster: C88 (= C95), H90 (= H97), R91 (≠ K98), C108 (= C115), Y110 (≠ F117), H111 (= H118), W113 (= W120)
2b24A Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. Bound to indole (see paper)
28% identity, 96% coverage: 8:439/452 of query aligns to 3:435/440 of 2b24A
- active site: H111 (= H118), D213 (= D221), H216 (= H224), H221 (= H229), D372 (= D372)
- binding fe (iii) ion: H216 (= H224), H221 (= H229), D372 (= D372)
- binding fe2/s2 (inorganic) cluster: C88 (= C95), H90 (= H97), R91 (≠ K98), C108 (= C115), Y110 (≠ F117), H111 (= H118), W113 (= W120)
- binding indole: D213 (= D221), H295 (vs. gap), F307 (= F314)
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
28% identity, 81% coverage: 22:388/452 of query aligns to 12:377/432 of 2xrxA
- active site: H106 (= H118), D203 (= D221), H206 (= H224), H212 (vs. gap), D361 (= D372)
- binding biphenyl: Q199 (≠ N218), F200 (≠ G219), D203 (= D221), H206 (= H224), H296 (≠ N306), L306 (≠ M316), F309 (= F319), F357 (≠ G368)
- binding fe (ii) ion: Q199 (≠ N218), H206 (= H224), H212 (vs. gap), D361 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), R86 (≠ K98), C103 (= C115), Y105 (≠ F117), H106 (= H118), W108 (= W120)
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
28% identity, 81% coverage: 22:388/452 of query aligns to 12:378/433 of 2yflA
- active site: H106 (= H118), D204 (= D221), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding 2-chlorodibenzofuran: Q200 (≠ N218), D204 (= D221), M205 (≠ G222), H207 (= H224), S257 (≠ H266), H297 (≠ N306), L307 (≠ M316), F352 (= F362)
- binding fe (ii) ion: Q200 (≠ N218), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), R86 (≠ K98), C103 (= C115), Y105 (≠ F117), H106 (= H118), W108 (= W120)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
28% identity, 81% coverage: 22:388/452 of query aligns to 12:378/433 of 2yfjA
- active site: H106 (= H118), D204 (= D221), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding dibenzofuran: Q200 (≠ N218), F201 (≠ G219), D204 (= D221), M205 (≠ G222), H207 (= H224), A208 (≠ V225), H297 (≠ N306), L307 (≠ M316), F358 (≠ G368)
- binding fe (ii) ion: Q200 (≠ N218), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), R86 (≠ K98), C103 (= C115), Y105 (≠ F117), H106 (= H118), W108 (= W120)
5aeuA Crystal structure of ii9 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 (see paper)
28% identity, 81% coverage: 22:388/452 of query aligns to 12:378/433 of 5aeuA
- active site: H106 (= H118), D204 (= D221), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding fe (ii) ion: H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), R86 (≠ K98), M88 (≠ A100), C103 (= C115), Y105 (≠ F117), H106 (= H118), W108 (= W120)
2xshA Crystal structure of p4 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 in complex with 2,6 di chlorobiphenyl (see paper)
28% identity, 81% coverage: 22:388/452 of query aligns to 12:378/433 of 2xshA
- active site: H106 (= H118), D204 (= D221), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding 2,6-dichlorobiphenyl: F201 (≠ G219), M205 (≠ G222), H207 (= H224), Q296 (≠ R305), H297 (≠ N306), L307 (≠ M316), F358 (≠ G368)
- binding fe (ii) ion: Q200 (≠ N218), H207 (= H224), H213 (vs. gap), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C83 (= C95), H85 (= H97), R86 (≠ K98), C103 (= C115), Y105 (≠ F117), H106 (= H118), W108 (= W120)
1uljA Biphenyl dioxygenase (bpha1a2) in complex with the substrate (see paper)
28% identity, 79% coverage: 22:380/452 of query aligns to 11:360/425 of 1uljA
- active site: H105 (= H118), D205 (= D221), H208 (= H224), H214 (≠ W230), D352 (= D372)
- binding biphenyl: Q201 (≠ N218), F202 (≠ G219), D205 (= D221), M206 (≠ G222), H208 (= H224), A209 (≠ V225), H214 (≠ W230), I252 (≠ T273), H287 (≠ N306), L297 (≠ M316), F342 (= F362)
- binding fe (ii) ion: Q201 (≠ N218), H208 (= H224), H214 (≠ W230), D352 (= D372)
- binding fe2/s2 (inorganic) cluster: C82 (= C95), H84 (= H97), R85 (≠ K98), M87 (≠ A100), C102 (= C115), Y104 (≠ F117), H105 (= H118), W107 (= W120)
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
28% identity, 79% coverage: 22:380/452 of query aligns to 11:358/425 of 1uliC
- active site: H105 (= H118), D205 (= D221), H208 (= H224), H214 (≠ Y232), D350 (= D372)
- binding fe (ii) ion: H208 (= H224), H214 (≠ Y232), D350 (= D372)
- binding fe2/s2 (inorganic) cluster: C82 (= C95), H84 (= H97), R85 (≠ K98), C102 (= C115), Y104 (≠ F117), H105 (= H118), W107 (= W120)
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)
34% identity, 46% coverage: 22:228/452 of query aligns to 27:228/460 of Q53122
- C98 (= C95) binding
- H100 (= H97) binding
- C118 (= C115) binding
- H121 (= H118) binding
- H224 (= H224) binding
Sites not aligning to the query:
- 217:230 binding
- 230 binding
- 378 binding
2gbxA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 bound to biphenyl (see paper)
27% identity, 77% coverage: 32:379/452 of query aligns to 12:362/449 of 2gbxA
- active site: H98 (= H118), D199 (= D221), H202 (= H224), H207 (≠ Y232), D355 (= D372)
- binding biphenyl: D199 (= D221), V203 (= V225), L255 (vs. gap), H288 (≠ Q303), N290 (= N306), L300 (≠ M316)
- binding fe (iii) ion: H202 (= H224), H207 (≠ Y232), D355 (= D372)
- binding fe2/s2 (inorganic) cluster: C75 (= C95), H77 (= H97), R78 (≠ K98), C95 (= C115), Y97 (≠ F117), H98 (= H118), W100 (= W120)
2gbwA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 (see paper)
27% identity, 77% coverage: 32:379/452 of query aligns to 12:362/449 of 2gbwA
- active site: H98 (= H118), D199 (= D221), H202 (= H224), H207 (≠ Y232), D355 (= D372)
- binding fe (iii) ion: H202 (= H224), H207 (≠ Y232), D355 (= D372)
- binding fe2/s2 (inorganic) cluster: C75 (= C95), H77 (= H97), R78 (≠ K98), C95 (= C115), Y97 (≠ F117), H98 (= H118), W100 (= W120)
- binding oxygen molecule: H202 (= H224), F345 (= F362), D355 (= D372)
3en1A Crystal structure of toluene 2,3-dioxygenase (see paper)
27% identity, 77% coverage: 34:380/452 of query aligns to 21:368/424 of 3en1A
- active site: H105 (= H118), D205 (= D221), H208 (= H224), H214 (≠ W230), D360 (= D372)
- binding fe (ii) ion: Q201 (≠ N218), H208 (= H224), H214 (≠ W230), D360 (= D372)
- binding fe2/s2 (inorganic) cluster: C82 (= C95), H84 (= H97), R85 (≠ K98), C102 (= C115), Y104 (≠ F117), H105 (= H118), W107 (= W120)
- binding toluene: Q201 (≠ N218), F202 (≠ G219), D205 (= D221), H208 (= H224), H295 (≠ N306)
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, 75% coverage: 34:372/452 of query aligns to 20:362/449 of P0A111
- C81 (= C95) binding
- H83 (= H97) binding
- C101 (= C115) binding
- H104 (= H118) binding
- H208 (= H224) binding
- H213 (≠ Y232) binding
- F352 (= F362) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D372) 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, 75% coverage: 34:372/452 of query aligns to 20:362/449 of P0A110
- C81 (= C95) binding
- H83 (= H97) binding
- C101 (= C115) binding
- H104 (= H118) binding
- N201 (= N218) mutation to A: Unable to catalyze the cis-dihydroxylation of biphenyl.
- F202 (≠ G219) mutation to L: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
- H208 (= H224) binding
- H213 (≠ Y232) binding
- F352 (= F362) 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 (≠ G368) 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 (= D372) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
29% identity, 75% coverage: 34:372/452 of query aligns to 20:362/446 of 4hm8A
- active site: H104 (= H118), D205 (= D221), H208 (= H224), H213 (≠ Y232), D362 (= D372)
- binding (methylsulfanyl)benzene: N201 (= N218), H295 (≠ T304)
- binding fe (iii) ion: H208 (= H224), H213 (≠ Y232), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C81 (= C95), H83 (= H97), R84 (≠ K98), C101 (= C115), Y103 (≠ F117), H104 (= H118), W106 (= W120)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
29% identity, 75% coverage: 34:372/452 of query aligns to 20:362/446 of 4hm7A
- active site: H104 (= H118), D205 (= D221), H208 (= H224), H213 (≠ Y232), D362 (= D372)
- binding fe (iii) ion: H208 (= H224), H213 (≠ Y232), D362 (= D372)
- binding fe2/s2 (inorganic) cluster: C81 (= C95), H83 (= H97), R84 (≠ K98), C101 (= C115), Y103 (≠ F117), H104 (= H118), W106 (= W120)
- binding ethenylbenzene: N201 (= N218), H208 (= H224), H295 (≠ T304), N297 (= N306)
Query Sequence
>BPHYT_RS07855 FitnessBrowser__BFirm:BPHYT_RS07855
MSATFDKASQLDELLHTAVQDDKQNGVFRCRRDIFTNAELFELEMKHIFESNWVYLAHES
QIPNNNDYYTTWIGRQPVVVTRDKSGELHAVINACAHKGAMLCRKKHGNKGTFTCPFHGW
SFANTGKLLKVKDVKTTEYPIQFNTNGSHDLKKVARFQSYRGFLFGTLNADAIPLEDYLG
ETRVIIDQIVDQAPDGLEVLRGNSSYIYDGNWKVQMENGCDGYHVSTVHWNYAATMDRRK
VEGTKAVDANSWSKSVAGVYGFEHGHILLWTKTMNPEVRPVYQYRDEIKARVGEVKADFI
VNQTRNLCLYPNVFLMDQFSTQIRVVRPISVDKTEVSIFCFAPKGESASDRATRIRQYED
FFNVSGMGTADDLEEFRACQAGYAGTTAMWNDLSRGAPLWVEGADANAKNMGLKPVISGE
RSEDEGLFVCQHEYWVHVMRDALRKEQGEAVA
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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