SitesBLAST
Comparing SMc00355 FitnessBrowser__Smeli:SMc00355 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)
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)
37% identity, 96% coverage: 7:341/350 of query aligns to 26:358/410 of 2a5hB
- active site: R110 (= R91), Y111 (= Y92), R114 (= R95), C123 (= C104), C127 (= C108), C130 (= C111), R132 (= R113), D291 (= D274), D328 (= D311), K335 (= K318)
- binding lysine: L96 (≠ I77), L116 (= L97), R132 (= R113), L165 (≠ I147), S167 (≠ T149), Y288 (≠ H271), D291 (= D274), D328 (= D311)
- binding pyridoxal-5'-phosphate: T108 (≠ V89), Y111 (= Y92), R114 (= R95), L116 (= L97), R196 (= R178), Y285 (= Y268), Y286 (= Y269), K335 (= K318)
- binding s-adenosylmethionine: H129 (≠ F110), T131 (≠ F112), R132 (= R113), S167 (≠ T149), G169 (= G151), G198 (≠ H180), H228 (= H211), Q256 (= Q239), V258 (= V241), Y288 (≠ H271), C290 (≠ P273), D291 (= D274)
- binding iron/sulfur cluster: C123 (= C104), C127 (= C108), C130 (= C111), G169 (= G151), R200 (= R182), H228 (= H211)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
37% identity, 96% coverage: 7:341/350 of query aligns to 28:360/416 of Q9XBQ8
- E86 (= E65) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D75) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R109) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R113) 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 (= R114) 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 (≠ E115) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E145) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D152) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E217) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D274) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (= D311) mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
35% identity, 98% coverage: 6:347/350 of query aligns to 36:375/471 of O34676
- K290 (≠ E262) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K318) mutation to Q: No activity and no bound PLP.
- K361 (≠ C333) mutation to Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>SMc00355 FitnessBrowser__Smeli:SMc00355
MTAERAIRTARELADAGLVGREQEEAISRVASRYAVAISPTIARLVDRDDPNDPIARQFV
PDMAELTLMPEERADPIGDGAHSPVAGIVHRYPDRVLLKAVHVCPVYCRFCFRREMVGPE
GLGTLTPAELDAALAYIAGRPEIWEVILTGGDPLVLSPRRLGDIMVRLAEIDHVKVVRFH
TRVPVVEPDRVDAGLIAALKSSGKATYVALHANHPRELTAEARAAAARLIDAGIVMVSQS
VLLKGVNDDPDVLAALMRAFVETRIKPYYLHHPDLAPGTGHFRLSIEEGQALVASLRGRV
SGLCQPAYILDIPGGHGKAVVSAGAIEAEGGGCYTVTDFRGNRHDYPPKG
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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