SitesBLAST
Comparing WP_084197976.1 NCBI__GCF_002869505.1:WP_084197976.1 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)
35% identity, 96% coverage: 11:331/334 of query aligns to 17:336/410 of 2a5hB
- active site: R110 (≠ K105), Y111 (= Y106), R114 (= R109), C123 (= C118), C127 (= C122), C130 (= C125), R132 (= R127), D291 (= D286), D328 (≠ E323), K335 (= K330)
- binding lysine: L96 (≠ V90), L116 (= L111), R132 (= R127), L165 (≠ I159), S167 (= S161), Y288 (≠ H283), D291 (= D286), D328 (≠ E323)
- binding pyridoxal-5'-phosphate: T108 (≠ I103), Y111 (= Y106), R114 (= R109), L116 (= L111), R196 (= R190), Y285 (= Y280), Y286 (= Y281), K335 (= K330)
- binding s-adenosylmethionine: H129 (≠ Y124), T131 (≠ F126), R132 (= R127), S167 (= S161), G169 (= G163), G198 (≠ H192), H228 (= H223), Q256 (= Q251), V258 (= V253), Y288 (≠ H283), C290 (≠ L285), D291 (= D286)
- binding iron/sulfur cluster: C123 (= C118), C127 (= C122), C130 (= C125), G169 (= G163), R200 (= R194), H228 (= H223)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
35% identity, 96% coverage: 11:331/334 of query aligns to 19:338/416 of Q9XBQ8
- E86 (= E78) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D88) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R123) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R127) 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 (= R128) 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 (≠ H129) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E157) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D164) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E229) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D286) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ E323) 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)
30% identity, 96% coverage: 11:330/334 of query aligns to 28:346/471 of O34676
- K290 (≠ E274) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K330) 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_084197976.1 NCBI__GCF_002869505.1:WP_084197976.1
MIPQTELHICDWRSELRHAVSDGETLLARLQLNPEQLGYSALAARDFPVLVPRPYLQRIT
PGDPDDPLLRQVLATGQETLVEPGYSDDPVGETGATIQRPGVIQKYRGRVLLILAGGCAI
NCRYCFRRHFPYQENRNSRQEWLQALEHVAADTSITEVILSGGDPLLVADAALAELVATI
AAIPHVRRLRVHTRLPVVIPQRVTDGLLQALTGSRLRCVMVIHSNHARELDASVAQAMQR
LREADVELLNQSVLLAGVNNHAATLVNLSERLFEIGVRPYYLHLLDKVRGAAHFDVPQAE
GIALIDAMATELPGYLVPRLVHEEAGQPGKTRIA
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