SitesBLAST
Comparing GFF2570 FitnessBrowser__Marino:GFF2570 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, 95% coverage: 13:342/346 of query aligns to 10:338/410 of 2a5hB
- active site: R110 (≠ K114), Y111 (= Y115), R114 (= R118), C123 (= C127), C127 (= C131), C130 (= C134), R132 (= R136), D291 (= D295), D328 (≠ E332), K335 (= K339)
- binding lysine: L96 (= L100), L116 (= L120), R132 (= R136), L165 (≠ I168), S167 (= S170), Y288 (≠ H292), D291 (= D295), D328 (≠ E332)
- binding pyridoxal-5'-phosphate: T108 (≠ I112), Y111 (= Y115), R114 (= R118), L116 (= L120), R196 (= R199), Y285 (= Y289), Y286 (= Y290), K335 (= K339)
- binding s-adenosylmethionine: H129 (≠ Y133), T131 (≠ F135), R132 (= R136), S167 (= S170), G169 (= G172), G198 (≠ H201), H228 (= H232), Q256 (= Q260), V258 (= V262), Y288 (≠ H292), C290 (≠ F294), D291 (= D295)
- binding iron/sulfur cluster: C123 (= C127), C127 (= C131), C130 (= C134), G169 (= G172), R200 (= R203), H228 (= H232)
Sites not aligning to the query:
Q9XBQ8 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Clostridium subterminale (see paper)
33% identity, 95% coverage: 13:342/346 of query aligns to 12:340/416 of Q9XBQ8
- E86 (= E88) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
- D96 (= D98) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
- R130 (= R132) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
- R134 (= R136) 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 (= R137) 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 (≠ H138) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
- D165 (≠ E166) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D172 (= D173) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
- E236 (= E238) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
- D293 (= D295) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
- D330 (≠ E332) 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, 92% coverage: 20:339/346 of query aligns to 28:346/471 of O34676
- K290 (≠ D283) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
- K346 (= K339) 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
>GFF2570 FitnessBrowser__Marino:GFF2570
MIQRTPARIEAHLSDHEQRSWQQLLSGAVTSPKELLRRLELPEEPWLAGAEQGHRLFQIR
VPEPFLNRMEKGNPADPLLRQVLPLADEAGHAPGFVSDPLEESGAIATTGLIRKYRSRAL
LMVTGQCAINCRYCFRRHFPYDEQRLSPHDRQRVIDVLGASPEINEVIFSGGDPLAVNDR
LLSQWASAISGIPHIRRLRLHTRLPVVIPQRVCDELLKWLSTTPLQVVIVLHINHPAEID
GPTRRALGYLRAAGATLLNQSVILRGVNDRTAVLEELSETLFDAGVLPYYLHAFDPVTGA
HHFDVSDDEARNLVRELLARLPGFLVPKLVREEPGKESKTPINLLP
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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