SitesBLAST
Comparing WP_057506865.1 NCBI__GCF_001431535.1:WP_057506865.1 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)
32% identity, 97% coverage: 12:334/334 of query aligns to 15:340/416 of Q9XBQ8
- E86 (= E80) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D90) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R124) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R128) 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 (= R129) 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 (≠ H130) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E158) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D165) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E230) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D287) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ E324) 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)
32% identity, 97% coverage: 12:334/334 of query aligns to 13:338/410 of 2a5hB
- active site: R110 (≠ K106), Y111 (= Y107), R114 (= R110), C123 (= C119), C127 (= C123), C130 (= C126), R132 (= R128), D291 (= D287), D328 (≠ E324), K335 (= K331)
- binding lysine: L96 (≠ V92), L116 (= L112), R132 (= R128), L165 (≠ I160), S167 (= S162), Y288 (= Y284), D291 (= D287), D328 (≠ E324)
- binding pyridoxal-5'-phosphate: T108 (≠ I104), Y111 (= Y107), R114 (= R110), L116 (= L112), R196 (= R191), Y285 (= Y281), Y286 (= Y282), K335 (= K331)
- binding s-adenosylmethionine: H129 (≠ Y125), T131 (≠ F127), R132 (= R128), S167 (= S162), G169 (= G164), G198 (≠ H193), H228 (= H224), Q256 (= Q252), V258 (= V254), Y288 (= Y284), C290 (≠ L286), D291 (= D287)
- binding iron/sulfur cluster: C123 (= C119), C127 (= C123), C130 (= C126), G169 (= G164), R200 (= R195), H228 (= H224)
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)
33% identity, 81% coverage: 57:327/334 of query aligns to 72:342/471 of O34676
- K290 (≠ A275) 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_057506865.1 NCBI__GCF_001431535.1:WP_057506865.1
MQLSAAHRPVSARWQQLWRQAIRDPGELLARLGLEPAALGVSEAALQQFAQRVPEGFVAR
MRHGDPHDPLLRQVLPIDAEMRQVPGFSLDAVGDGAAKKATGVIQKYRGRALLVTTGSCA
INCRYCFRRHFDYGTENAAKGGWQEAVRAIAEDPGIDEVILSGGDPLSLATHKLVELTDA
LRAIPHLRRLRIHSRLPVVLPERVDDELVAWLGSLPWPLAFVIHANHANEFDASVDAALA
RLRAAGAQLLNQAVLLRGVNDSEDALAALSERSFAAGVMPYYLYQLDRVEGVAHFEVDDA
TAKALIAALTARLSGYLVPKLVRELPGDPSKRPV
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