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B6db families: 5.4.3.2
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5.4.3.2
Activity 5.4.3.2
Description Lysine 2,3-aminomutase.
Notes Lysine-2,3-aminomutase requires a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal-5'-phosphate as cofactors.
PDB 2A5H;
PLP Fold Type VII
PLP-dependent Domain
Domain alignment
Domain hmm		Fold type VII
Number of sequences
12
Sequences in seed alignment
ArchaeaAAM30630.1 (Methanosarcina mazei Goe1); CAF30417 (Methanococcus maripaludis);
BacteriaZP_00129480 (Desulfovibrio desulfuricans); NP_656164.1 (Bacillus anthracis A2012); NP_243121 (Bacillus halodurans); AAD43134 (Clostridium subterminale); AAB72069.1 (Bacillus subtilis); AAO35482 (Clostridium tetani); AAF12280 (Deinococcus radiodurans); NP_905285 (Porphyromonas gingivalis); AAM23985 (Thermoanaerobacter tengcongensis); NP_602666 (Fusobacterium nucleatum);

DISPLAY: Fasta format, alignment, hmm, hmm_local
Reference sequence AAB72069.1
Domain interval 63-348
Catalytic site 346 K
 
References
 Lepore, B.W.; Ruzicka, F.J.; Frey, P. A.; Ringe, D. (2005) The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale Proc Natl Acad Sci U S A 102 13819-24.

 Chen, D.; Ruzicka, F. J.; Frey, P. A. (2000) A novel lysine 2,3-aminomutase encoded by the yodO gene of bacillus subtilis: characterization and the observation of organic radical intermediates Biochem J 348 539-49.

 Ruzicka, F. J.; Lieder, K. W.; Frey, P. A. (2000) Lysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli J Bacteriol 182 469-76.

Articles on 5.4.3.2
last changed 2008/05/16 14:16

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