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B6db families: 2.5.1.49

2.5.1.49
Activity 2.5.1.49
Description O-acetylhomoserine (thiol)-lyase
Notes Family of enzymes occurring in bacteria, fungi and archaea. THe prototype is the T. thermophilus enzyme, whose structure has been solved.
The sequences are strictly related to those of methionine gamma-lyases (family 4.4.1.11).
PDB 2CTZ;4KAM;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences
30
Sequences in seed alignment
ArchaeaAAM06094 (Methanosarcina acetivorans str. C2A); WP_094228163 (Methanolobus psychrotolerans); WP_048122994 (Methanosarcina barkeri CM1);
BacteriaBAB68505 (Thermus thermophilus); CAA71732 (Leptospira meyeri); NP_540083 (Brucella melitensis); NP_349387 (Clostridium acetobutylicum); WP_074567952 (Bacillus cereus); ACC39643 (Mycobacterium marinum M); WP_061859240 (Clostridium colicanis); WP_024621399 (Clostridioides mangenotii); NP_464123 (Listeria monocytogenes EGD-e); APU51341 (Clostridioides difficile); WP_049624723 (Geobacillus stearothermophilus); ZP_00107219 (Nostoc punctiforme); NP_623710 (Thermoanaerobacter tengcongensis); NP_531944 (Agrobacterium tumefaciens str. C58 (U. Washington)); NP_228690 (Thermotoga maritima); ZP_00119048 (Cytophaga hutchinsonii); ZP_00121486 (Bifidobacterium longum DJO10A); NP_661504 (Chlorobium tepidum TLS); ZP_00115203 (Synechococcus sp. WH 8102); NP_385354 (Sinorhizobium meliloti); ZP_00082400 (Geobacter metallireducens);
FungiMT17_YEAST (Saccharomyces cerevisiae); CYSD_SCHPO (Schizosaccharomyces pombe); AAF01452 (Candida albicans); MT17_KLULA (Kluyveromyces lactis); CYSD_EMENI (Emericella nidulans); CAB99179 (Neurospora crassa);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence BAB68505
Domain interval 4-421
Catalytic site 206 K
 
References
 Kulikova VV, Revtovich SV, Bazhulina NP, Anufrieva NV, Kotlov MI, Koval VS, Morozova EA, Hayashi H, Belyi YF, Demidkina TV (2019) Identification of O-acetylhomoserine sulfhydrylase, a putative enzyme responsible for methionine biosynthesis in Clostridioides difficile: Gene cloning and biochemical characterizations IUBMB Life 71 1815-1823.

 Allen KD, Miller DV, Rauch BJ, Perona JJ, White RH (2015) Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea Biochemistry 54 3129-32.

 Omura H, Ikemoto M, Kobayashi M, Shimizu S, Yoshida T, Nagasawa T (2003) Purification, characterization and gene cloning of thermostable O-acetyl-L-homoserine sulfhydrylase forming gamma-cyano-alpha-aminobutyric acid J Biosci Bioeng 96 53-8.

 Shimizu H, Yamagata S, Masui R, Inoue Y, Shibata T, Yokoyama S, Kuramitsu S, Iwama T. (2001) Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product Biochim Biophys Acta 1549 1-72.

 Yamagata, S.; Ichioka, K.; Goto, K.; Mizuno, Y; Iwama, T. (2001) Occurrence of transsulfuration in synthesis of L-homocysteine in an extremely thermophilic bacterium, Thermus thermophilus HB8 J Bacteriol 183 2086-92.

 Bourhy, P.; Martel, A.; Margarita, D.; Saint Girons, I.; Belfaiza, J. (1997) Homoserine O-acetyltransferase, involved in the Leptospira meyeri methionine biosynthetic pathway, is not feedback inhibited J Bacteriol 179 4396-4398.

 Yamagata, S.; Isaji, M.; Nakamura, K.; Fujisaki, S.; Doi, K.; Bawden, S.; D'Andrea, R. (1994) Overexpression of the Saccharomyces cerevisiae MET17/MET25 gene in Escherichia coli and comparative characterization of the product with O-acetylserine.O-acetylhomoserine sulfhydrylase of the yeast Appl Microbiol Biotechnol 42 92-99.

 Brzywczy, J.; Yamagata, S.; Paszewski, A. (1993) Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme Acta Biochim Pol 40 421-8.

Articles on 2.5.1.49
last changed 2019/08/28 12:15

B6db families