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B6db families: a
Description L-serine ammonia-lyase (family a)
Notes The validated serine ammonia-lyases come from fungi and animals; accordingly, the family is constituted by fungal and metazoan proteins only (although some very similar bacterial sequences can be found in databases).

Note that, in some bacteria, the deamination of L-Ser is carried out by L-threonine ammonia lyase (EC and the corresponding enzymes have been included in that family.

Note also that some bacteria possess PLP-independent L-serine ammonia-lyases.

PLP Fold Type II
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type II

Number of sequences 26
Sequences in seed alignment
FungiEAA55293 (Magnaporthe grisea); XP_387338 (Gibberella zeae); XP_503774 (Yarrowia lipolytica); EAL00695 (Candida albicans); ALX72404 (Rhizomucor miehei); EAK97061 (Candida albicans); SDHL_YEAST (Saccharomyces cerevisiae); CAP92996 (Penicillium rubens Wisconsin 54-1255); XP_001212195 (Aspergillus terreus); STDH_YEAST (Saccharomyces cerevisiae); XP_775525 (Cryptococcus neoformans); ORZ27577 (Lobosporangium transversale); CEG69314 (Rhizopus microsporus);
MetazoaXP_001378476 (Monodelphis domestica); SDHL_HUMAN (Homo sapiens); CAF91636 (Tetraodon nigroviridis); SDSL_HUMAN (Homo sapiens); XP_415319 (Gallus gallus); XP_692090 (Danio rerio); 1PWEA (Rattus norvegicus); AAU05774 (Aplysia californica); NP_001091171 (Xenopus laevis); XP_798802 (Strongylocentrotus purpuratus); NP_001092465 (Bos taurus); AAH60346 (Xenopus laevis); NP_663540 (Mus musculus);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence STDH_YEAST
Domain interval 1-302
Catalytic site 37 K
 Wu M, Crismaru CG, Salo O, Bovenberg RAL, Driessen AJ (2020) Impact of classical strain improvement of Penicillium rubens on amino acid metabolism during -lactam production Appl Environ Microbiol 86 e01561-19.

 Qin Z, Yan Q, Ma Q, Jiang Z (2015) Crystal structure and characterization of a novel L-serine ammonia-lyase from Rhizomucor miehei Biochem Biophys Res Commun 466 431-7.

 Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F. (2008) A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: Crystal structure and site-directed mutagenesis studies Biochim Biophys Acta 1780 809-18.

 Bornaes, C.; Petersen, J.G.; Holmberg, S. (1992) Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases Genetics 131 531-9.

 Ogawa, H.; Fujioka, M.; Date, T.; Mueckler, M.; Su, Y.; Pitot, H.C. (1990) Rat serine dehydratase gene codes for two species of mRNA of which only one is translated into serine dehydratase J Biol Chem 265 14407-13.

 Ogawa, H.; Gomi, T.; Konishi, K.; Date, T.; Nakashima, H.; Nose, K.; Matsuda, Y.; Peraino, C.; Pitot, H.C.; Fujioka, M. (1989) Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources J Biol Chem 264 15818-23.

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last changed 2017/07/25 17:39

B6db families