SitesBLAST
Comparing WP_011383696.1 NCBI__GCF_000009985.1:WP_011383696.1 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)
45% identity, 87% coverage: 23:322/344 of query aligns to 44:342/410 of 2a5hB
- active site: R110 (= R89), Y111 (= Y90), R114 (= R93), C123 (= C102), C127 (= C106), C130 (= C109), R132 (= R111), D291 (= D271), D328 (= D308), K335 (= K315)
- binding lysine: L96 (≠ I75), L116 (= L95), R132 (= R111), L165 (≠ I144), S167 (≠ T146), Y288 (≠ H268), D291 (= D271), D328 (= D308)
- binding pyridoxal-5'-phosphate: T108 (≠ V87), Y111 (= Y90), R114 (= R93), L116 (= L95), R196 (= R175), Y285 (= Y265), Y286 (= Y266), K335 (= K315)
- binding s-adenosylmethionine: H129 (≠ F108), T131 (≠ F110), R132 (= R111), S167 (≠ T146), G169 (= G148), G198 (≠ H177), H228 (= H208), Q256 (= Q236), V258 (= V238), Y288 (≠ H268), C290 (≠ P270), D291 (= D271)
- binding iron/sulfur cluster: C123 (= C102), C127 (= C106), C130 (= C109), G169 (= G148), R200 (= R179), H228 (= H208)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
45% identity, 87% coverage: 23:322/344 of query aligns to 46:344/416 of Q9XBQ8
- E86 (= E63) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D73) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R107) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R111) 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 (= R112) 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 (≠ A113) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E142) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D149) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E214) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D271) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (= D308) 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)
39% identity, 92% coverage: 6:322/344 of query aligns to 36:353/471 of O34676
- K290 (≠ R259) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K315) 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
>WP_011383696.1 NCBI__GCF_000009985.1:WP_011383696.1
MSSRRTLRTAQDLHDAGLIPSVEAVAGVAEAYAVALTPAVVDLIDPADPADPIARQYVPS
AEELVTTPEELADPIGDAAYSPVKGLVHRYPDRVLLTPLLVCPVYCRFCFRRARVGDGDA
TMTEAEIDTALAYVAGRPEIREVILTGGDPLMLPPPRLAALLGRIGAIAHVELIRIHSRV
PVSDPERVTPDLARVLGGGDKPVWLAVHVNHPHELSPLARGGLERLARTGVPLLSQTVLL
KGVNDSVSVLDELFRALVRNRVRPYYLHHPDLAPGTSHFRPTIEEGQALMRSLRGRLSGI
AQPTYVLDIPGGAGKVPVGPQYWDGEAGTVADPGGRLHDYAERA
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