SitesBLAST
Comparing PfGW456L13_4924 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4924 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)
O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 77% coverage: 16:357/446 of query aligns to 38:332/471 of O34676
- K290 (≠ R315) 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.
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)
24% identity, 76% coverage: 17:355/446 of query aligns to 28:319/410 of 2a5hB
- active site: R110 (≠ K133), Y111 (= Y134), R114 (≠ T137), C123 (= C148), C127 (= C152), C130 (= C155), R132 (= R157), D291 (≠ E326)
- binding lysine: L96 (≠ I88), L116 (= L139), R132 (= R157), L165 (= L191), S167 (≠ T193), Y288 (≠ F324), D291 (≠ E326)
- binding pyridoxal-5'-phosphate: T108 (≠ Q131), Y111 (= Y134), R114 (≠ T137), L116 (= L139), R196 (= R222), Y285 (= Y321), Y286 (= Y322)
- binding s-adenosylmethionine: H129 (≠ F154), T131 (≠ F156), R132 (= R157), S167 (≠ T193), G169 (= G195), G198 (= G224), H228 (= H263), Q256 (= Q292), V258 (≠ P294), Y288 (≠ F324), C290 (≠ V325), D291 (≠ E326)
- binding iron/sulfur cluster: C123 (= C148), C127 (= C152), C130 (= C155), G169 (= G195), R200 (≠ K226), H228 (= H263)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
24% identity, 76% coverage: 17:355/446 of query aligns to 30:321/416 of Q9XBQ8
- E86 (≠ L76) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (≠ Q86) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (≠ T153) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R157) 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 (≠ A159) 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 (≠ Q160) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (= D189) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D196) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E269) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (≠ E326) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
Sites not aligning to the query:
- 330 mutation D->A,N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
Query Sequence
>PfGW456L13_4924 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4924
MQGLSEHERYKPYNSRTIRDTPYWHKLTPALQEAMTVVARVMPFRTNEYVLGTLIDWNNI
PDDPVLRMTFPHKDMLLAEEYASLKQLIEQDDSAAIKRRIEAIWRRMNPHPAGQLTHNGV
TLNGKVLPGIQHKYRETVLFFPGAGQTCHAYCTFCFRWAQFIGEEELKFNARESQELVSY
LRVHTEVTDVLITGGDPMIMNTRSLAGYIEPLLDLPHLKNIRIGTKSVAYWPQRFVSDKD
APELLELFQRIVAAGKNLSIMGHYNHPVEIRQVIARQAIERIRSTGATVRMQAPVIRHVN
ENPADWAALWTEGVRLGAVPYYMFVERDTGPSHYFEMPLARAFEIFQAAYRTVSGLARTV
RGPSMSTFYGKVLINGIETVAGEKVFVLQFLQARNPQWVLRTFYARFDPQVTWFDDLQPA
FGERAFFFQTELTAVPELIPVLLETA
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