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Comparing H281DRAFT_01653 FitnessBrowser__Burk376:H281DRAFT_01653 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)
33% identity, 89% coverage: 22:399/427 of query aligns to 27:411/471 of O85673
- M43 (≠ L38) mutation to K: Prevents anthranilate degradation.
- D217 (= D210) 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)
30% identity, 96% coverage: 19:426/427 of query aligns to 14:425/433 of 2xshA
- active site: H106 (= H111), D204 (= D210), H207 (= H213), H213 (= H218), D362 (= D367)
- binding 2,6-dichlorobiphenyl: F201 (vs. gap), M205 (≠ L211), H207 (= H213), Q296 (≠ F303), H297 (≠ N304), L307 (vs. gap), F358 (≠ G363)
- binding fe (ii) ion: Q200 (≠ N207), H207 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
31% identity, 96% coverage: 19:426/427 of query aligns to 14:425/433 of 2yflA
- active site: H106 (= H111), D204 (= D210), H207 (= H213), H213 (= H218), D362 (= D367)
- binding 2-chlorodibenzofuran: Q200 (≠ N207), D204 (= D210), M205 (≠ L211), H207 (= H213), S257 (≠ D262), H297 (≠ N304), L307 (vs. gap), F352 (≠ Q357)
- binding fe (ii) ion: Q200 (≠ N207), H207 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
31% identity, 96% coverage: 19:426/427 of query aligns to 14:425/433 of 2yfjA
- active site: H106 (= H111), D204 (= D210), H207 (= H213), H213 (= H218), D362 (= D367)
- binding dibenzofuran: Q200 (≠ N207), F201 (vs. gap), D204 (= D210), M205 (≠ L211), H207 (= H213), A208 (≠ F214), H297 (≠ N304), L307 (vs. gap), F358 (≠ G363)
- binding fe (ii) ion: Q200 (≠ N207), H207 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
31% identity, 96% coverage: 19:426/427 of query aligns to 14:424/432 of 2xrxA
- active site: H106 (= H111), D203 (= D210), H206 (= H213), H212 (= H218), D361 (= D367)
- binding biphenyl: Q199 (≠ N207), F200 (vs. gap), D203 (= D210), H206 (= H213), H296 (≠ N304), L306 (≠ S314), F309 (= F317), F357 (≠ G363)
- binding fe (ii) ion: Q199 (≠ N207), H206 (= H213), H212 (= H218), D361 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
5aeuA Crystal structure of ii9 variant of biphenyl dioxygenase from burkholderia xenovorans lb400 (see paper)
30% identity, 96% coverage: 19:426/427 of query aligns to 14:425/433 of 5aeuA
- active site: H106 (= H111), D204 (= D210), H207 (= H213), H213 (= H218), D362 (= D367)
- binding fe (ii) ion: H207 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), M88 (≠ A93), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
7ylsB Structure of a bacteria protein complex
29% identity, 97% coverage: 13:426/427 of query aligns to 9:434/436 of 7ylsB
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
29% identity, 97% coverage: 13:426/427 of query aligns to 8:433/435 of 8h2tB
- binding fe (iii) ion: N208 (= N207), H214 (= H213), H219 (= H218), D375 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), K86 (≠ R91), C104 (= C108), H107 (= H111), W109 (= W113)
- binding 1h-indol-3-ylacetic acid: N208 (= N207), L209 (≠ T208), D211 (= D210), H214 (= H213), P215 (≠ F214), F249 (≠ V232), K320 (≠ S314), Y360 (≠ I352)
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)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/449 of P0A111
- C81 (= C88) binding
- H83 (= H90) binding
- C101 (= C108) binding
- H104 (= H111) binding
- H208 (= H213) binding
- H213 (= H218) binding
- F352 (≠ Q357) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D367) 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)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/449 of P0A110
- C81 (= C88) binding
- H83 (= H90) binding
- C101 (= C108) binding
- H104 (= H111) binding
- N201 (= N207) 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 (= H213) binding
- H213 (= H218) binding
- F352 (≠ Q357) 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 (≠ G363) 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 (= D367) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
4hm0A Naphthalene 1,2-dioxygenase bound to indole-3-acetate
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 4hm0A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding 1h-indol-3-ylacetic acid: N201 (= N207), D205 (= D210), H208 (= H213), V209 (≠ F214), H213 (= H218), H295 (≠ L298), N297 (= N304)
1uuvA Naphthalene 1,2-dioxygenase with nitric oxide and indole bound in the active site. (see paper)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 1uuvA
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding indole: N297 (= N304), L307 (vs. gap)
- binding nitric oxide: H208 (= H213), H213 (= H218)
1o7pA Naphthalene 1,2-dioxygenase, product complex (see paper)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 1o7pA
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding (1r, 2s)-cis 1,2 dihydroxy-1,2-dihydronaphthalene: N201 (= N207), H208 (= H213), V209 (≠ F214), H213 (= H218), H295 (≠ L298)
1o7mA Naphthalene 1,2-dioxygenase, binary complex with dioxygen (see paper)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 1o7mA
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding oxygen molecule: H208 (= H213), H213 (= H218)
1o7gA Naphthalene 1,2-dioxygenase with naphthalene bound in the active site. (see paper)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 1o7gA
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding naphthalene: N201 (= N207), D205 (= D210), H208 (= H213), H295 (≠ L298), N297 (= N304)
1eg9A Naphthalene 1,2-dioxygenase with indole bound in the active site. (see paper)
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/447 of 1eg9A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding indole: N201 (= N207), H208 (= H213), V209 (≠ F214), N297 (= N304), L307 (vs. gap)
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/446 of 4hm8A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding (methylsulfanyl)benzene: N201 (= N207), H295 (≠ L298)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/446 of 4hm7A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
- binding ethenylbenzene: N201 (= N207), H208 (= H213), H295 (≠ L298), N297 (= N304)
4hm6A Naphthalene 1,2-dioxygenase bound to phenetole
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/446 of 4hm6A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding ethoxybenzene: N201 (= N207), H208 (= H213), H295 (≠ L298)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
4hm4A Naphthalene 1,2-dioxygenase bound to indan
30% identity, 94% coverage: 27:427/427 of query aligns to 20:427/446 of 4hm4A
- active site: H104 (= H111), D205 (= D210), H208 (= H213), H213 (= H218), D362 (= D367)
- binding 2,3-dihydro-1H-indene: H208 (= H213), H295 (≠ L298), N297 (= N304)
- binding fe (iii) ion: H208 (= H213), H213 (= H218), D362 (= D367)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (= Y110), H104 (= H111), W106 (= W113)
Query Sequence
>H281DRAFT_01653 FitnessBrowser__Burk376:H281DRAFT_01653
MSTPTYQTIDTSALAKRAESDRIAPSLYYDPQLFEEELQRIFYRTWVWVAHDSELPKPGD
FVTTTIGRQPVIVVRDKTGAVNVLQNRCRHRGATVCEEHKGNAKGFTCPYHSWSYALDGT
LRALPYGDGYEGVCEKGDLPLKKLRVGVYQGLIFASFNEQIESLEDFLGGAKPWIDLFMK
QGAGYPIKANGEHKFKFKGNWKIQLENTTDLYHFPVVHKSWMKSIDDETAAVITSFMTSE
DAFCRSLGNGHSLAVLVPEIVDLDRDDGAPLPDRFNELAAQLSQKHTPEEVRRIVRSLMG
VGFNLNLFPNLALSMAFFRVLRPISAEETEIRHVALAMDGGPDEANRVRLRIHEHFQGPF
GFGSPDDAEAWERVQRGSYAGPDVPILVNRGLNRETAAPNGEKTAHATDETGMREAYRQW
RAMMEQA
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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