SitesBLAST
Comparing WP_086511961.1 NCBI__GCF_002151265.1:WP_086511961.1 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)
46% identity, 95% coverage: 12:445/455 of query aligns to 13:453/471 of O85673
- M43 (= M42) 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.
7ylsB Structure of a bacteria protein complex
31% identity, 84% coverage: 12:394/455 of query aligns to 10:399/436 of 7ylsB
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
31% identity, 84% coverage: 12:394/455 of query aligns to 9:398/435 of 8h2tB
- binding fe (iii) ion: N208 (= N215), H214 (= H221), H219 (= H226), D375 (= D371)
- binding fe2/s2 (inorganic) cluster: C83 (= C92), H85 (= H94), K86 (≠ R95), C104 (= C112), H107 (= H115), W109 (= W117)
- binding 1h-indol-3-ylacetic acid: N208 (= N215), L209 (≠ G216), D211 (= D218), H214 (= H221), P215 (≠ V222), F249 (≠ S252), K320 (≠ M315), Y360 (= Y357)
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
29% identity, 79% coverage: 26:384/455 of query aligns to 16:363/425 of 1uliC
- active site: H105 (= H115), D205 (= D218), H208 (= H221), H214 (≠ D234), D350 (= D371)
- binding fe (ii) ion: H208 (= H221), H214 (≠ D234), D350 (= D371)
- binding fe2/s2 (inorganic) cluster: C82 (= C92), H84 (= H94), R85 (= R95), C102 (= C112), Y104 (≠ F114), H105 (= H115), W107 (= W117)
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, 77% coverage: 20:371/455 of query aligns to 10:362/449 of P0A111
- C81 (= C92) binding
- H83 (= H94) binding
- C101 (= C112) binding
- H104 (= H115) binding
- H208 (= H221) binding
- H213 (≠ Y229) binding
- F352 (= F361) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D371) 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, 77% coverage: 20:371/455 of query aligns to 10:362/449 of P0A110
- C81 (= C92) binding
- H83 (= H94) binding
- C101 (= C112) binding
- H104 (= H115) binding
- N201 (= N215) 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 (= H221) binding
- H213 (≠ Y229) binding
- F352 (= F361) 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 (≠ G367) 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 (= D371) 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
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 4hm0A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding 1h-indol-3-ylacetic acid: N201 (= N215), D205 (= D218), H208 (= H221), V209 (= V222), H213 (≠ Y229), H295 (≠ T303), N297 (= N305)
1uuvA Naphthalene 1,2-dioxygenase with nitric oxide and indole bound in the active site. (see paper)
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 1uuvA
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding indole: N297 (= N305), L307 (≠ M315)
- binding nitric oxide: H208 (= H221), H213 (≠ Y229)
1o7pA Naphthalene 1,2-dioxygenase, product complex (see paper)
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 1o7pA
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding (1r, 2s)-cis 1,2 dihydroxy-1,2-dihydronaphthalene: N201 (= N215), H208 (= H221), V209 (= V222), H213 (≠ Y229), H295 (≠ T303)
1o7mA Naphthalene 1,2-dioxygenase, binary complex with dioxygen (see paper)
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 1o7mA
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding oxygen molecule: H208 (= H221), H213 (≠ Y229)
1o7gA Naphthalene 1,2-dioxygenase with naphthalene bound in the active site. (see paper)
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 1o7gA
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding naphthalene: N201 (= N215), D205 (= D218), H208 (= H221), H295 (≠ T303), N297 (= N305)
1eg9A Naphthalene 1,2-dioxygenase with indole bound in the active site. (see paper)
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/447 of 1eg9A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding indole: N201 (= N215), H208 (= H221), V209 (= V222), N297 (= N305), L307 (≠ M315)
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm8A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding (methylsulfanyl)benzene: N201 (= N215), H295 (≠ T303)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm7A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding ethenylbenzene: N201 (= N215), H208 (= H221), H295 (≠ T303), N297 (= N305)
4hm6A Naphthalene 1,2-dioxygenase bound to phenetole
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm6A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding ethoxybenzene: N201 (= N215), H208 (= H221), H295 (≠ T303)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
4hm4A Naphthalene 1,2-dioxygenase bound to indan
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm4A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding 2,3-dihydro-1H-indene: H208 (= H221), H295 (≠ T303), N297 (= N305)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
4hm3A Naphthalene 1,2-dioxygenase bound to ethylbenzene
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm3A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding phenylethane: N201 (= N215), D205 (= D218), H208 (= H221), N297 (= N305)
4hm2A Naphthalene 1,2-dioxygenase bound to ethylphenylsulfide
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm2A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding (ethylsulfanyl)benzene: N201 (= N215), D205 (= D218), V209 (= V222), H295 (≠ T303), N297 (= N305)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
4hm1A Naphthalene 1,2-dioxygenase bound to 1-indanone
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hm1A
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding 2,3-dihydro-1H-inden-1-one: N201 (= N215), V209 (= V222), N297 (= N305)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
4hkvA Naphthalene 1,2-dioxygenase bound to benzamide
31% identity, 77% coverage: 20:371/455 of query aligns to 10:362/446 of 4hkvA
- active site: H104 (= H115), D205 (= D218), H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe (iii) ion: H208 (= H221), H213 (≠ Y229), D362 (= D371)
- binding fe2/s2 (inorganic) cluster: C81 (= C92), H83 (= H94), R84 (= R95), C101 (= C112), Y103 (≠ F114), H104 (= H115), W106 (= W117)
- binding benzamide: N201 (= N215), H208 (= H221), H295 (≠ T303), N297 (= N305)
Query Sequence
>WP_086511961.1 NCBI__GCF_002151265.1:WP_086511961.1
MTTQLDQLEARVRGAVVDDAEKGIFRCHRSMFTDPAFFELEMKHVFEGNWLFLAHESQIS
EPGDYMTVTMGRQPVVITRDKSGELHALINACAHRGATLCRRKRGNKGTFTCPFHGWTFK
NDGKLLKAKSEKVGAYPDSFKQDGSHDLKRVPRFESYKGFLFGSLNEDVKPLQEYLGETT
KVIDNIVDQAPEGLEVLRGTSSYTFKGNWKLQAENGADGYHVSTVHWNYASTMDRRNYEA
GGTKAVDADGWSKSQGGFYSYENGHMLLWTRLLNPEVRPVYQNREWIQAQFGEARADSIV
NQTRNLCLYPNVYLMDQFSTQIRVLRPISVDETEVTIYCFAPKGESAENRRVRIRQYEDF
FNVSGMGTPDDLEEFRGCQDGYHGALAEWNDLSRGAKQWIEGADDNAKAIGMQPLLSGAS
PEDEGLYVLHHKHWVEEMLRAIEKERSQFIATQTA
Or try a new SitesBLAST search
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