SitesBLAST
Comparing BPHYT_RS10690 FitnessBrowser__BFirm:BPHYT_RS10690 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)
31% identity, 94% coverage: 25:426/427 of query aligns to 20:425/433 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, 94% coverage: 25:426/427 of query aligns to 20:425/433 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, 94% coverage: 25:426/427 of query aligns to 20:425/433 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, 94% coverage: 25:426/427 of query aligns to 20:424/432 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)
31% identity, 94% coverage: 25:426/427 of query aligns to 20:425/433 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)
8h2tB Cryo-em structure of iadd/e dioxygenase bound with iaa (see paper)
31% 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 (≠ M237), K320 (≠ S314), Y360 (≠ I352)
7ylsB Structure of a bacteria protein complex
31% identity, 97% coverage: 13:426/427 of query aligns to 9:434/436 of 7ylsB
7c8zA Crystal structure of salicylate 5-hydroxylase naggh (a rieske non-heme iron-dependent monooxgenase) (see paper)
30% identity, 95% coverage: 20:424/427 of query aligns to 14:381/383 of 7c8zA
- active site: H106 (= H111), D213 (= D210), H216 (= H213), H221 (= H218), D330 (= D367)
- binding fe (iii) ion: H216 (= H213), H221 (= H218), D330 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), C103 (= C108), H106 (= H111), W108 (= W113)
1uliC Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. Strain rha1 (see paper)
28% identity, 95% coverage: 19:424/427 of query aligns to 13:411/425 of 1uliC
- active site: H105 (= H111), D205 (= D210), H208 (= H213), H214 (≠ K219), D350 (= D367)
- binding fe (ii) ion: H208 (= H213), H214 (≠ K219), D350 (= D367)
- binding fe2/s2 (inorganic) cluster: C82 (= C88), H84 (= H90), R85 (= R91), C102 (= C108), Y104 (= Y110), H105 (= H111), W107 (= W113)
1uljA Biphenyl dioxygenase (bpha1a2) in complex with the substrate (see paper)
28% identity, 95% coverage: 19:424/427 of query aligns to 13:413/425 of 1uljA
- active site: H105 (= H111), D205 (= D210), H208 (= H213), H214 (≠ E228), D352 (= D367)
- binding biphenyl: Q201 (≠ N207), F202 (vs. gap), D205 (= D210), M206 (≠ L211), H208 (= H213), A209 (≠ K223), H214 (≠ E228), I252 (≠ D266), H287 (≠ N304), L297 (vs. gap), F342 (= F356)
- binding fe (ii) ion: Q201 (≠ N207), H208 (= H213), H214 (≠ E228), D352 (= D367)
- binding fe2/s2 (inorganic) cluster: C82 (= C88), H84 (= H90), R85 (= R91), M87 (≠ A93), C102 (= C108), Y104 (= Y110), H105 (= H111), W107 (= W113)
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)
29% identity, 95% coverage: 19:424/427 of query aligns to 29:439/460 of Q53122
- C98 (= C88) binding
- H100 (= H90) binding
- C118 (= C108) binding
- H121 (= H111) binding
- 217:230 (vs. 207:218, 21% identical) binding
- H224 (= H213) binding
- H230 (vs. gap) binding
- D378 (= D367) binding
3en1A Crystal structure of toluene 2,3-dioxygenase (see paper)
29% identity, 98% coverage: 6:424/427 of query aligns to 1:422/424 of 3en1A
- active site: H105 (= H111), D205 (= D210), H208 (= H213), H214 (= H218), D360 (= D367)
- binding fe (ii) ion: Q201 (≠ N207), H208 (= H213), H214 (= H218), D360 (= D367)
- binding fe2/s2 (inorganic) cluster: C82 (= C88), H84 (= H90), R85 (= R91), C102 (= C108), Y104 (= Y110), H105 (= H111), W107 (= W113)
- binding toluene: Q201 (≠ N207), F202 (vs. gap), D205 (= D210), H208 (= H213), H295 (≠ N304)
1wqlA Cumene dioxygenase (cuma1a2) from pseudomonas fluorescens ip01 (see paper)
28% identity, 94% coverage: 25:426/427 of query aligns to 20:428/436 of 1wqlA
- active site: H106 (= H111), D208 (= D210), H211 (= H213), H217 (= H218), D365 (= D367)
- binding fe (ii) ion: H211 (= H213), H217 (= H218), D365 (= D367)
- binding fe2/s2 (inorganic) cluster: C83 (= C88), H85 (= H90), R86 (= R91), C103 (= C108), Y105 (= Y110), H106 (= H111), W108 (= W113)
- binding oxygen molecule: H211 (= H213), F355 (≠ H355)
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)
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/449 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)
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/449 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
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/447 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 (= H286), N297 (= N304)
1uuvA Naphthalene 1,2-dioxygenase with nitric oxide and indole bound in the active site. (see paper)
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/447 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)
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/447 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 (= H286)
1o7mA Naphthalene 1,2-dioxygenase, binary complex with dioxygen (see paper)
28% identity, 86% coverage: 27:395/427 of query aligns to 20:392/447 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)
Query Sequence
>BPHYT_RS10690 FitnessBrowser__BFirm:BPHYT_RS10690
MSESSYQTVDASALYQRVQSDRVAPSLYYDPAVFEAELERIFYKTWIWVAHESELPNPGD
FRTTTIGRQPVIVVRDKSGAVNVLQNRCRHRGATVCEQHKGNAKGFTCPYHSWTYGLDGT
LRALPYGDGYEGVVDKTELPLASLRVGIYQGLIFASFNQEIEPLEDFLGGAKPWIDLFMK
QGAGYPIKANGEHRFRFNGNWKIQLENTTDLYHFPVVHKSWMKSIDDETAAAITSFMTSD
QAFCRSLGNGHSLAVLVPEIVDLDKDDGAPIPERFEELAASLARDHTPEEVRRIVRSLMG
VGFNLNLFPNLALSMAFFRVLRPISANETEIRHVALAMDGGPEEANRVRLRIHEHFQGPF
GFGSPDDAEAWERVQRGSHAGPDLPILVNRGLNRESTAPNGEKTAHATDETGMREAYAQW
RTMMEQA
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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