SitesBLAST
Comparing BWI76_RS13705 FitnessBrowser__Koxy:BWI76_RS13705 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, 91% coverage: 24:442/460 of query aligns to 25:450/471 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
28% identity, 80% coverage: 26:394/460 of query aligns to 18:399/436 of 7ylsB
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
28% identity, 80% coverage: 26:394/460 of query aligns to 17:398/435 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 (≠ R353)
2b24A Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. Bound to indole (see paper)
37% identity, 43% coverage: 30:226/460 of query aligns to 26:221/440 of 2b24A
- active site: H111 (= H115), D213 (= D218), H216 (= H221), H221 (= H226)
- binding fe (iii) ion: H216 (= H221), H221 (= H226)
- binding fe2/s2 (inorganic) cluster: C88 (= C92), H90 (= H94), R91 (= R95), C108 (= C112), Y110 (≠ F114), H111 (= H115), W113 (= W117)
- binding indole: D213 (= D218)
Sites not aligning to the query:
2b1xA Crystal structure of naphthalene 1,2-dioxygenase from rhodococcus sp. (see paper)
37% identity, 43% coverage: 30:226/460 of query aligns to 26:221/441 of 2b1xA
- active site: H111 (= H115), D213 (= D218), H216 (= H221), H221 (= H226)
- binding fe (iii) ion: H216 (= H221), H221 (= H226)
- binding fe2/s2 (inorganic) cluster: C88 (= C92), H90 (= H94), R91 (= R95), C108 (= C112), Y110 (≠ F114), H111 (= H115), W113 (= W117)
Sites not aligning to the query:
2gbxA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 bound to biphenyl (see paper)
29% identity, 78% coverage: 29:386/460 of query aligns to 12:373/449 of 2gbxA
- active site: H98 (= H115), D199 (= D218), H202 (= H221), H207 (≠ Y229), D355 (= D371)
- binding biphenyl: D199 (= D218), V203 (= V222), L255 (= L268), H288 (≠ T303), N290 (= N305), L300 (≠ M315)
- binding fe (iii) ion: H202 (= H221), H207 (≠ Y229), D355 (= D371)
- binding fe2/s2 (inorganic) cluster: C75 (= C92), H77 (= H94), R78 (= R95), C95 (= C112), Y97 (≠ F114), H98 (= H115), W100 (= W117)
2gbwA Crystal structure of biphenyl 2,3-dioxygenase from sphingomonas yanoikuyae b1 (see paper)
29% identity, 78% coverage: 29:386/460 of query aligns to 12:373/449 of 2gbwA
- active site: H98 (= H115), D199 (= D218), H202 (= H221), H207 (≠ Y229), D355 (= D371)
- binding fe (iii) ion: H202 (= H221), H207 (≠ Y229), D355 (= D371)
- binding fe2/s2 (inorganic) cluster: C75 (= C92), H77 (= H94), R78 (= R95), C95 (= C112), Y97 (≠ F114), H98 (= H115), W100 (= W117)
- binding oxygen molecule: H202 (= H221), F345 (= F361), D355 (= D371)
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, 76% coverage: 31:381/460 of query aligns to 20:373/449 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, 76% coverage: 31:381/460 of query aligns to 20:373/449 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.
2bmrA The crystal structure of nitrobenzene dioxygenase in complex with 3- nitrotoluene (see paper)
30% identity, 71% coverage: 31:355/460 of query aligns to 16:339/437 of 2bmrA
- active site: H100 (= H115), D201 (= D218), H204 (= H221), H209 (= H226)
- binding 3-nitrotoluene: F198 (vs. gap), D201 (= D218), H204 (= H221), V205 (= V222), N256 (≠ H265), F291 (≠ T303), N293 (= N305)
- binding fe (iii) ion: H204 (= H221), H209 (= H226)
- binding fe2/s2 (inorganic) cluster: C77 (= C92), H79 (= H94), R80 (= R95), C97 (= C112), Y99 (≠ F114), H100 (= H115), W102 (= W117)
Sites not aligning to the query:
2bmqA The crystal structure of nitrobenzene dioxygenase in complex with nitrobenzene (see paper)
30% identity, 71% coverage: 31:355/460 of query aligns to 16:339/437 of 2bmqA
- active site: H100 (= H115), D201 (= D218), H204 (= H221), H209 (= H226)
- binding fe (iii) ion: H204 (= H221), H209 (= H226)
- binding fe2/s2 (inorganic) cluster: C77 (= C92), H79 (= H94), R80 (= R95), C97 (= C112), Y99 (≠ F114), H100 (= H115), W102 (= W117)
- binding nitrobenzene: N197 (= N215), F198 (vs. gap), H204 (= H221), N256 (≠ H265), F291 (≠ T303), N293 (= N305)
Sites not aligning to the query:
2bmoA The crystal structure of nitrobenzene dioxygenase (see paper)
30% identity, 71% coverage: 31:355/460 of query aligns to 16:339/437 of 2bmoA
- active site: H100 (= H115), D201 (= D218), H204 (= H221), H209 (= H226)
- binding fe (iii) ion: H204 (= H221), H209 (= H226)
- binding fe2/s2 (inorganic) cluster: C77 (= C92), H79 (= H94), R80 (= R95), C97 (= C112), Y99 (≠ F114), H100 (= H115), W102 (= W117)
Sites not aligning to the query:
4hm0A Naphthalene 1,2-dioxygenase bound to indole-3-acetate
31% identity, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/447 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, 76% coverage: 31:381/460 of query aligns to 20:373/446 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, 76% coverage: 31:381/460 of query aligns to 20:373/446 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)
Query Sequence
>BWI76_RS13705 FitnessBrowser__Koxy:BWI76_RS13705
MQKTFARLKDKISNALIVDREKHIYRCHRSIFTDPQLFDFEMKHIFEGNWLFLAHESQIA
QPGDYYTLTLGRQPVIITRDKKNELHALINSCAHRGAMLCRRKTGNKNSLTCPFHGWTFS
NNGKLLKAKDESTGGYPDSFKQEGSHDLTKLPKFQSYRGFLFGSLNADVQPLEEYLGETR
KIIDLIVDQAPQGLEVLKGSSSYVYEGNWKLGAENGADGYHVSVVHWNYASTMSRRNYEA
EGTHAVDANGWSKSVGGGYGFENGHMLLWTRALNPEVRPVYEHRERLRAEFGESRADRMV
NETRNLCLYPNVYLMDQFSTQIRVIRPIAVDKTEVTIWCFAPRGESDQARALRIRQYEDF
FNVSGMGTPDDLEEFSACQRGYLGENLAWSDLSRGALHWVDGPDDHALQAGFSPQLSGVK
SEDEALYIAHHHHWQNVMLAALETERQRYDQSITQRVEVA
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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