SitesBLAST

E86 (= E65) mutation to Q: Reduction in activity. Decrease in iron and sulfide and PLP content.
D96 (= D75) mutation to N: Reduction in activity. Decrease in iron and sulfide and PLP content.
R130 (= R109) mutation R->Q,K: Complete loss of activity. Decrease in iron and sulfide but not PLP content. Destabilise the iron-sulfur centers.
R134 (= R113) 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 (= R114) 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 (≠ E115) mutation to Q: Reduction in activity. Significant decrease in iron and sulfide and PLP content.
D165 (≠ E145) mutation to N: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D172 (= D152) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content. Destabilise the iron-sulfur centers.
E236 (= E217) mutation to Q: Significant reduction in activity. Decrease in iron and sulfide and PLP content.
D293 (= D274) mutation to N: Complete loss of activity. Decrease in iron and sulfide and PLP content.
D330 (= D311) 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)
44% identity, 84% coverage: 36:326/345 of query aligns to 55:343/410 of 2a5hB

query
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2a5hB

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active site: R110 (= R91), Y111 (= Y92), R114 (= R95), C123 (= C104), C127 (= C108), C130 (= C111), R132 (= R113), D291 (= D274), D328 (= D311), K335 (= K318)
binding lysine: L96 (≠ I77), L116 (= L97), R132 (= R113), L165 (≠ I147), S167 (≠ T149), Y288 (≠ H271), D291 (= D274), D328 (= D311)
binding pyridoxal-5'-phosphate: T108 (≠ V89), Y111 (= Y92), R114 (= R95), L116 (= L97), R196 (= R178), Y285 (= Y268), Y286 (= Y269), K335 (= K318)
binding s-adenosylmethionine: H129 (≠ F110), T131 (≠ F112), R132 (= R113), S167 (≠ T149), G169 (= G151), G198 (≠ H180), H228 (= H211), Q256 (= Q239), V258 (= V241), Y288 (≠ H271), C290 (≠ G273), D291 (= D274)
binding iron/sulfur cluster: C123 (= C104), C127 (= C108), C130 (= C111), G169 (= G151), R200 (= R182), H228 (= H211)

Sites not aligning to the query:

binding zinc ion: 373, 375, 378

O34676 L-lysine 2,3-aminomutase; LAM; KAM; EC 5.4.3.2 from Bacillus subtilis (strain 168) (see paper)
39% identity, 89% coverage: 36:342/345 of query aligns to 66:375/471 of O34676

query
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O34676

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K290 (≠ E262) mutation to Q: More than 95% loss of activity, and half of normal PLP binding capacity.
K346 (= K318) mutation to Q: No activity and no bound PLP.
K361 (vs. gap) mutation to Q: 95% loss of activity, normal PLP binding capacity.

Query Sequence

>CCNA_00753 FitnessBrowser__Caulo:CCNA_00753
MSPVQTLRDARSLTEAGLVPSERLPALEAVAARYAVAITPAMAELIDPDRDDDPIARQFV
PSPEELVSSPGEDGDPIGDAAHSPVEGIVHRYPDRVLLKPTHTCAVYCRFCFRREMVGPE
GLSNLTPAQLDAAFAYIAQRPQIWEVIVTGGDPLVLSPRRLADLMDRLEAIDHVKIVRFH
TRVPAVDPGAVTPELVAALKRSSKTVYVALHANHARELTPAARAACAQIVDAGVPMVSQT
VLLRGVNDNPETLVELMRAFVETRIRPYYLHHGDLAPGTAHLRTTVAEGQAIMRALRGTL
SGLAQPTYVLDIPGGHGKVPVGPNYLSDGAVEDPDGAVRPYPPTA

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