P54950 · SCMK_BACSU
- ProteinN-acetyl-S-(2-succino)cysteine monooxygenase
- GenescmK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids441 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidative cleavage of the C-S bond of N-acetyl-S-(2-succino)cysteine, forming oxaloacetate and N-acetylcysteine (NAC) (PubMed:34510734).
Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine (PubMed:29626092).
Shows almost no activity on S-succinylglutathione and 2SC (PubMed:34510734).
Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine (PubMed:29626092).
Shows almost no activity on S-succinylglutathione and 2SC (PubMed:34510734).
Miscellaneous
The substrate N-acetyl-S-(2-succino)-L-cysteine arises from the spontaneous Michael addition of cysteine to the citric acid cycle intermediate fumarate.
Catalytic activity
- H+ + N-acetyl-S-(2-succino)-L-cysteine + NADH + O2 = H2O + N-acetyl-L-cysteine + NAD+ + oxaloacetateThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
92 μM | N-acetyl-S-(2-succino)cysteine |
kcat is 4.4 sec-1 using E.coli Fre as the flavin reductase partner. The enzyme may work more efficiently in vivo when interacting with its native partner flavin reductase.
Pathway
Amino-acid biosynthesis; L-cysteine biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 59 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 96 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 146 | FMN (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 150 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 220 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 221 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
Biological Process | cysteine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetyl-S-(2-succino)cysteine monooxygenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP54950
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene almost lose the ability to grow on 2SC as the sulfur source but are still able to grow on sulfate. Moreover, they show a massive accumulation of N-acetyl-S-(2-succino)cysteine when S2C is added to the medium.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 19 | Shows 36% of wild-type catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 74 | Loss of catalytic activity. | ||||
Sequence: R → M | ||||||
Mutagenesis | 96 | Shows 10% of wild-type catalytic activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 96 | Shows 0.9% of wild-type catalytic activity. | ||||
Sequence: T → V | ||||||
Mutagenesis | 125 | Loss of catalytic activity. | ||||
Sequence: N → L or V | ||||||
Mutagenesis | 127 | Loss of catalytic activity. | ||||
Sequence: V → G |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000050017 | 1-441 | N-acetyl-S-(2-succino)cysteine monooxygenase | |||
Sequence: MTSKKKQIKLGVFLAGTGHHVASWRHPDAPSDASMNLDYFKELAKTAERGKLDMLFLADSLSIDSKSHPNVLTRFEPFTLLSALAQVTSKIGLTATASTTYSEPFHIARQFASLDHLSNGRAGWNVVTSSIESTALNFSGEKHLEHHLRYQRAEEFVEIVKGLWDSWEEDAFIRNKETGEFFDKEKMHELNHKGEYFSVRGPLNVSRTPQGQPVIIQAGSSGDGKALAAKTAEVIFTAQNHLESAQEFYQSIKEQAAEFGRDPEKIAIMPGIFPIIADTEEAAQAKYKELQDLIIPSVGLQILQNYLGGIDLSAYPLDGPLPKLDAEASNAVKSRFKLVQEMAERDNMTIRELYKYVAGSRGHHIFVGTPEQLADKMQEWVDTKACDGFNIMPPLLPEGIEVFVDQVVPILQERGVFRKEYEGTTLREHFGLEKPVNRYAK |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length441
- Mass (Da)49,339
- Last updated1996-10-01 v1
- Checksum4C7FAF8FDF34C906
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D45912 EMBL· GenBank· DDBJ | BAA08327.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB15988.1 EMBL· GenBank· DDBJ | Genomic DNA |