SitesBLAST
Comparing WP_035629568.1 NCBI__GCF_000711315.1:WP_035629568.1 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)
33% identity, 91% coverage: 28:315/318 of query aligns to 53:341/410 of 2a5hB
- active site: R110 (≠ K85), Y111 (= Y86), R114 (= R89), C123 (= C98), C127 (= C102), C130 (= C105), R132 (= R107), D291 (= D265), D328 (≠ E302), K335 (= K309)
- binding lysine: L96 (≠ V71), L116 (= L91), R132 (= R107), L165 (≠ I137), S167 (= S139), Y288 (≠ H262), D291 (= D265), D328 (≠ E302)
- binding pyridoxal-5'-phosphate: T108 (≠ L83), Y111 (= Y86), R114 (= R89), L116 (= L91), R196 (= R168), Y285 (= Y259), Y286 (= Y260), K335 (= K309)
- binding s-adenosylmethionine: H129 (≠ Y104), T131 (≠ F106), R132 (= R107), S167 (= S139), G169 (= G141), G198 (≠ H170), H228 (= H202), Q256 (= Q230), V258 (= V232), Y288 (≠ H262), C290 (≠ L264), D291 (= D265)
- binding iron/sulfur cluster: C123 (= C98), C127 (= C102), C130 (= C105), G169 (= G141), R200 (= R172), H228 (= H202)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
34% identity, 91% coverage: 28:315/318 of query aligns to 55:343/416 of Q9XBQ8
- E86 (= E59) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D69) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R103) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R107) 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 (= R108) 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 (≠ H109) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E135) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D142) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E208) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D265) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ E302) 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)
31% identity, 87% coverage: 30:305/318 of query aligns to 66:342/471 of O34676
- K290 (≠ S253) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
Sites not aligning to the query:
- 346 K→Q: No activity and no bound PLP.
- 361 K→Q: 95% loss of activity, normal PLP binding capacity.
Query Sequence
>WP_035629568.1 NCBI__GCF_000711315.1:WP_035629568.1
MIQRLDELAAQIDIPLEILQRKTLNSDFKLKVPMHFAQQIEKGNLDDPLLRQILPSIEEA
QTAVGFSQDPVGDLKANPTESLLHKYEGRALLITSPQCDIHCRYCFRRHFPYEQAKKRHW
QQALELLATDSSIHEIILSGGDPLTLSEAGLIDLLHQLEQIPHLETLRIHSRTPVVAPNR
ANMKNWLAVLNASRFNKVLVVHCNHPNELSDETHQTFQLYRDVGVTLLNQCVLLKGVNDS
AGTLKRLSKKLFSQGVLPYYCHLLDRVEGAAHFEVDTTPTWQIFETLRKELPGYLVPKLV
REIAGEPYKTPIYENADT
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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