SitesBLAST
Comparing WP_092483144.1 NCBI__GCF_900115975.1:WP_092483144.1 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)
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
51% identity, 87% coverage: 46:405/413 of query aligns to 4:362/416 of Q9XBQ8
- E86 (= E130) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D139) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R173) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R177) 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 (= R178) 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 (= R179) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (= D208) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D215) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E279) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (≠ K336) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ N373) 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)
51% identity, 87% coverage: 46:405/413 of query aligns to 2:360/410 of 2a5hB
- active site: R110 (= R155), Y111 (= Y156), R114 (= R159), C123 (= C168), C127 (= C172), C130 (= C175), R132 (= R177), D291 (≠ K336), D328 (≠ N373), K335 (= K380)
- binding lysine: L96 (≠ M141), L116 (≠ I161), R132 (= R177), L165 (= L210), S167 (≠ T212), Y288 (≠ F333), D291 (≠ K336), D328 (≠ N373)
- binding pyridoxal-5'-phosphate: T108 (= T153), Y111 (= Y156), R114 (= R159), L116 (≠ I161), R196 (= R241), Y285 (= Y330), Y286 (= Y331), K335 (= K380)
- binding s-adenosylmethionine: H129 (= H174), T131 (≠ Q176), R132 (= R177), S167 (≠ T212), G169 (= G214), G198 (= G243), H228 (= H273), Q256 (= Q301), V258 (= V303), Y288 (≠ F333), C290 (≠ A335), D291 (≠ K336)
- binding iron/sulfur cluster: C123 (= C168), C127 (= C172), C130 (= C175), G169 (= G214), R200 (= R245), H228 (= H273)
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)
47% identity, 87% coverage: 48:405/413 of query aligns to 13:371/471 of O34676
- K290 (= K324) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K380) mutation to Q: No activity and no bound PLP.
- K361 (≠ Y395) mutation to Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>WP_092483144.1 NCBI__GCF_900115975.1:WP_092483144.1
MTVNKHDKRDIALDRTEELKQRIESYLEAAKSIPTGFKMEEEYQARKKELLQFFGATEEN
WQDWHWQMRNRISDVGMLRKLWSLTEEEAEQIESVSEKFRWAVSPYYLSLMEPGNPGCPV
RMQGIPSIRELQDNWGKLDPMAEEYTSPAPRITRRYADRLIINVTNQCAMFCRHCQRRRS
IGEVDKPAPVEEIKAAIDYIRQNPEVRDVLITGGDPLTLSDEWLDWILSELDKIEHVEIK
RIGSRTPVTMPQRITPELCAMLESHHPLYLNTHFNHPREVTQEALRATRMLAKAGISLGN
QAVLLKGINNDPHVMKKLNHELLKIHVRPYYIFHAKPVKGTTHFVTTVQEGLEIMENLRG
YTSGLAIPWYIINAPGGAGKTPLLPQYLLTMGKDYVMIRTWEGKVFRCANGNI
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