metC

metC
168

cystathionine beta-lyase

Locus
BSU_11880
Molecular weight
42.33 kDa
Isoelectric point
5.76
Protein length
390 aaSequenceBlast
Gene length
1170 bpSequenceBlast
Function
biosynthesis of methionine
Product
cystathionine beta-lyase
Essential
no
E.C.
4.4.1.8
Synonyms
metC, yjcJ
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0626 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,259,606 → 1,260,778
The protein
Catalyzed reaction/ biological activity
H2O + L,L-cystathionine --> L-homocysteine + NH4+ + pyruvate (according to UniProt)
S-substituted L-cysteine + H2O --> thiol + NH4+ + pyruvate (according to UniProt)
Protein family
trans-sulfuration enzymes family (with MccB and MetI, according to UniProt)
Cofactors
PLP (according to UniProt)
Structure
4L0O (PDB) (from Helicobacter pylori, 51% identity)
O31632 (AlphaFold)
Paralogous protein(s)
MccB, MetI
Localization
cytoplasm (according to Swiss-Prot)
Expression and Regulation
Operons
Genes
metI-metC
Description
PubMed
Regulation
induced by methionine starvation (S-box) PubMed
the S-box RNA is degraded by RNase Y PubMed
Regulatory mechanism
S-box: RNA switch, the S-box riboswitch binds S-adenosylmethionine resulting in termination, in S-box
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
Open in new tab

metI→metC

2025-03-15 00:00:28

Jstuelk

84

e7bcabc481203e5715faf59d0740a493d058794d

A78F2908B4A6A8C859B2C706984458FF45D08793

Biological materials
Mutant
MGNA-B299 (yjcJ::erm), available at the NBRP B. subtilis, Japan
1A944 ( metC::kan), PubMed, available at BGSC
1A940 ( metC::spec), PubMed, available at BGSC
BKE11880 (ΔmetC::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CTGGGTTTCCAGCGTCCAAT,  downstream forward: _UP4_TAAAAAAGAAGCCGGGGATA
BKK11880 (ΔmetC::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CTGGGTTTCCAGCGTCCAAT,  downstream forward: _UP4_TAAAAAAGAAGCCGGGGATA
References
Gutiérrez-Preciado A, Henkin TM, Grundy FJ, Yanofsky C, Merino E Biochemical features and functional implications of the RNA-based T-box regulatory mechanism. Microbiology and molecular biology reviews : MMBR. 2009 Mar; 73(1):36-61. doi:10.1128/MMBR.00026-08. PMID:19258532
Tomsic J, McDaniel BA, Grundy FJ, Henkin TM Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro. Journal of bacteriology. 2008 Feb; 190(3):823-33. . PMID:18039762
Mäder U, Homuth G, Scharf C, Büttner K, Bode R, Hecker M Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability. Journal of bacteriology. 2002 Aug; 184(15):4288-95. . PMID:12107147
Auger S, Yuen WH, Danchin A, Martin-Verstraete I The metIC operon involved in methionine biosynthesis in Bacillus subtilis is controlled by transcription antitermination. Microbiology (Reading, England). 2002 Feb; 148(Pt 2):507-18. . PMID:11832514

1C0D38F23D3A2CAA1EB057A92D6F571D0D2AA724

Page visits: 5371

Time of last update: 2025-03-15 19:48:02

Author of last update: Melvin.boenninger