SitesBLAST
Comparing PP_3161 FitnessBrowser__Putida:PP_3161 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)
47% identity, 93% coverage: 19:439/452 of query aligns to 24:450/471 of O85673
- M43 (= M38) mutation to K: Prevents anthranilate degradation.
- D217 (= D214) 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
29% identity, 85% coverage: 6:391/452 of query aligns to 8:399/436 of 7ylsB
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
29% identity, 85% coverage: 6:391/452 of query aligns to 7:398/435 of 8h2tB
- binding fe (iii) ion: N208 (= N211), H214 (= H217), H219 (= H222), D375 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), K86 (≠ R91), C104 (= C108), H107 (= H111), W109 (= W113)
- binding 1h-indol-3-ylacetic acid: N208 (= N211), L209 (≠ G212), D211 (= D214), H214 (= H217), P215 (≠ V218), F249 (vs. gap), K320 (≠ M313), Y360 (= Y355)
2yflA Crystal structure of biphenyl dioxygenase variant rr41 with 2-chloro dibenzofuran (see paper)
27% identity, 81% coverage: 15:382/452 of query aligns to 12:375/433 of 2yflA
- active site: H106 (= H111), D204 (= D214), H207 (= H217), H213 (= H222), D362 (= D369)
- binding 2-chlorodibenzofuran: Q200 (≠ N211), D204 (= D214), M205 (≠ G215), H207 (= H217), S257 (≠ H263), H297 (≠ N303), L307 (≠ M313), F352 (= F359)
- binding fe (ii) ion: Q200 (≠ N211), H207 (= H217), H213 (= H222), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (≠ F110), H106 (= H111), W108 (= W113)
2yfjA Crystal structure of biphenyl dioxygenase variant rr41 with dibenzofuran (see paper)
27% identity, 81% coverage: 15:382/452 of query aligns to 12:375/433 of 2yfjA
- active site: H106 (= H111), D204 (= D214), H207 (= H217), H213 (= H222), D362 (= D369)
- binding dibenzofuran: Q200 (≠ N211), F201 (vs. gap), D204 (= D214), M205 (≠ G215), H207 (= H217), A208 (≠ V218), H297 (≠ N303), L307 (≠ M313), F358 (≠ A365)
- binding fe (ii) ion: Q200 (≠ N211), H207 (= H217), H213 (= H222), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (≠ F110), H106 (= H111), W108 (= W113)
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, 77% coverage: 24:369/452 of query aligns to 17:362/449 of P0A111
- C81 (= C88) binding
- H83 (= H90) binding
- C101 (= C108) binding
- H104 (= H111) binding
- H208 (= H217) binding
- H213 (≠ Y225) binding
- F352 (= F359) mutation to V: Changes the regioselectivity of the product for naphthalene, phenanthrene and biphenyl.
- D362 (= D369) 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, 77% coverage: 24:369/452 of query aligns to 17:362/449 of P0A110
- C81 (= C88) binding
- H83 (= H90) binding
- C101 (= C108) binding
- H104 (= H111) binding
- N201 (= N211) 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 (= H217) binding
- H213 (≠ Y225) binding
- F352 (= F359) 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 (≠ A365) 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 (= D369) binding ; mutation to A: Unable to catalyze the cis-dihydroxylation of naphthalene, biphenyl and phenanthrene.
4hm8A Naphthalene 1,2-dioxygenase bound to thioanisole
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm8A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding (methylsulfanyl)benzene: N201 (= N211), H295 (≠ S301)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
4hm7A Naphthalene 1,2-dioxygenase bound to styrene
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm7A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
- binding ethenylbenzene: N201 (= N211), H208 (= H217), H295 (≠ S301), N297 (= N303)
4hm6A Naphthalene 1,2-dioxygenase bound to phenetole
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm6A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding ethoxybenzene: N201 (= N211), H208 (= H217), H295 (≠ S301)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
4hm4A Naphthalene 1,2-dioxygenase bound to indan
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm4A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding 2,3-dihydro-1H-indene: H208 (= H217), H295 (≠ S301), N297 (= N303)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
4hm3A Naphthalene 1,2-dioxygenase bound to ethylbenzene
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm3A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
- binding phenylethane: N201 (= N211), D205 (= D214), H208 (= H217), N297 (= N303)
4hm2A Naphthalene 1,2-dioxygenase bound to ethylphenylsulfide
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm2A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding (ethylsulfanyl)benzene: N201 (= N211), D205 (= D214), V209 (= V218), H295 (≠ S301), N297 (= N303)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
4hm1A Naphthalene 1,2-dioxygenase bound to 1-indanone
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hm1A
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding 2,3-dihydro-1H-inden-1-one: N201 (= N211), V209 (= V218), N297 (= N303)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
4hkvA Naphthalene 1,2-dioxygenase bound to benzamide
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hkvA
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
- binding benzamide: N201 (= N211), H208 (= H217), H295 (≠ S301), N297 (= N303)
4hjlA Naphthalene 1,2-dioxygenase bound to 1-chloronaphthalene
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 4hjlA
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding 1-chloronaphthalene: N201 (= N211), D205 (= D214), H208 (= H217), H295 (≠ S301), N297 (= N303), L307 (≠ M313)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
2hmoA Crystal structure of naphthalene 1,2-dioxygenase bound to 3- nitrotoluene. (see paper)
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 2hmoA
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding 3-nitrotoluene: N201 (= N211), N297 (= N303), W358 (≠ A365)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
2hmmA Crystal structure of naphthalene 1,2-dioxygenase bound to anthracene (see paper)
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 2hmmA
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding anthracene: N201 (= N211), D205 (= D214), H208 (= H217), V209 (= V218), F224 (≠ K242), N297 (= N303)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
2hmkA Crystal structure of naphthalene 1,2-dioxygenase bound to phenanthrene (see paper)
30% identity, 77% coverage: 24:369/452 of query aligns to 17:362/446 of 2hmkA
- active site: H104 (= H111), D205 (= D214), H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe (iii) ion: H208 (= H217), H213 (≠ Y225), D362 (= D369)
- binding fe2/s2 (inorganic) cluster: C81 (= C88), H83 (= H90), R84 (= R91), C101 (= C108), Y103 (≠ F110), H104 (= H111), W106 (= W113)
- binding phenanthrene: N201 (= N211), D205 (= D214), H208 (= H217), V209 (= V218), F224 (≠ K242), N297 (= N303)
2xrxA Crystal structure of biphenyl dioxygenase in complex with biphenyl from burkholderia xenovorans lb400 (see paper)
27% identity, 81% coverage: 15:382/452 of query aligns to 12:374/432 of 2xrxA
- active site: H106 (= H111), D203 (= D214), H206 (= H217), H212 (= H222), D361 (= D369)
- binding biphenyl: Q199 (≠ N211), F200 (vs. gap), D203 (= D214), H206 (= H217), H296 (≠ N303), L306 (≠ M313), F309 (= F316), F357 (≠ A365)
- binding fe (ii) ion: Q199 (≠ N211), H206 (= H217), H212 (= H222), D361 (= D369)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (≠ F110), H106 (= H111), W108 (= W113)
Query Sequence
>PP_3161 FitnessBrowser__Putida:PP_3161
MSLGFDYLNAMLEDDREKGIYRCKREMFTDPRLFDLEMKHIFEGNWIYLAHESQIPEKND
FLTLTMGRQPIFIARNKDGELNAFLNACSHRGAMLCRHKRGNRSSYTCPFHGWTFNNSGK
LLKVKDPSNAGYPDSFNCDGSHDLTKVARFESYRGFLFGSLNADVKPLVEHLGESAKIID
MIVDQSPEGLEVLRGASSYIYEGNWKLTAENGADGYHVSSVHWNYAATQNQRKQREAGDE
IKTMSAGAWAKQGGGFYSFDHGHLLLWTRWANPEDRPAYERRDQLAADFGQARADWMIEN
SRNLCLYPNVYLMDQFSSQIRVARPISVNKTEITIYCIAPKGESADARAKRIRQYEDFFN
VSGMATPDDLEEFRSCQTGYGGGTGWNDMSRGAKHWVEGADEAAKEIELEPLLSGVRTED
EGLFVLQHKYWQDTMIQALKDEQQLIPVEAVQ
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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