SitesBLAST
Comparing Pf6N2E2_2163 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2163 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 3 hits to proteins with known functional sites (download)
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
37% identity, 80% coverage: 31:401/465 of query aligns to 1:337/416 of Q9XBQ8
- E86 (= E132) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D143) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R177) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R181) mutation to K: Complete loss of activity. Significant decrease in iron and sulfide and PLP content.; mutation to Q: Complete loss of activity. Slight decrease in iron and sulfide and PLP content.
- R135 (≠ S182) mutation to K: Reduction in activity. Decrease in iron and sulfide and PLP content.; mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- R136 (≠ Y183) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (= D219) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D226) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E300) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D357) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (= D394) mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
2a5hB 2.1 angstrom x-ray crystal structure of lysine-2,3-aminomutase from clostridium subterminale sb4, with michaelis analog (l-alpha-lysine external aldimine form of pyridoxal-5'-phosphate). (see paper)
38% identity, 77% coverage: 45:401/465 of query aligns to 2:335/410 of 2a5hB
- active site: R110 (= R159), Y111 (= Y160), R114 (= R163), C123 (= C172), C127 (= C176), C130 (= C179), R132 (= R181), D291 (= D357), D328 (= D394), K335 (= K401)
- binding lysine: L96 (≠ M145), L116 (= L165), R132 (= R181), L165 (≠ V221), S167 (= S223), Y288 (≠ F354), D291 (= D357), D328 (= D394)
- binding pyridoxal-5'-phosphate: T108 (= T157), Y111 (= Y160), R114 (= R163), L116 (= L165), R196 (= R252), Y285 (= Y351), Y286 (= Y352), K335 (= K401)
- binding s-adenosylmethionine: H129 (≠ Y178), T131 (= T180), R132 (= R181), S167 (= S223), G169 (= G225), G198 (≠ A254), H228 (= H294), Q256 (= Q322), V258 (= V324), Y288 (≠ F354), C290 (≠ G356), D291 (= D357)
- binding iron/sulfur cluster: C123 (= C172), C127 (= C176), C130 (= C179), G169 (= G225), R200 (≠ K256), H228 (= H294)
Sites not aligning to the query:
O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
36% identity, 78% coverage: 38:401/465 of query aligns to 6:346/471 of O34676
- K290 (≠ Y345) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K401) mutation to Q: No activity and no bound PLP.
Sites not aligning to the query:
- 361 K→Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>Pf6N2E2_2163 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2163
MSSNIVDYDFTDIQLKSLIAHSSQGQRLKPLLSLRYAFRSDEFWRDLDHWKDIDVELFLN
HLWQEKNAITSVGALGALIKNRISAAFLRDLEEGHQMAPMSIRLTPYILSLIDWDNPYLD
PLRRQFLPLASEISIDHPMVKLDPMGEQDDSPAPGLTHRYPDRVLFLATNVCPVYCRYCT
RSYAVGLDTDAVTKKKINAPGERWEPALRYIETNSSVEDVVISGGDAYRLKARQITEIGE
RLLDVPHVRRMRFATKGLAVLPMKIQSDHDWTDAISRLSDRARKVHKSIAIHTHFNHPNE
ITAVTAKALGMLYERGVEVRNQAVILKGVNDNPQTMHRLNECLAYLNVRPYYCFQGDMIR
GVEALRTSLCDSIALEKSTRGLIAGHNTPHFIVDLPGGGGKRDIHSYDYYDQHLGIAAYR
APAVKKDKIFLYCDPLHTLTADAQALWTNPATRTQLLDDVLKSVK
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