O32799 · PFL_LACLM
- ProteinFormate acetyltransferase
- Genepfl
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids787 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Miscellaneous
Several mechanisms have been proposed based on complexes formed with substrate analogs. After activation by the glycine radical, the cysteine radical, Cys-417, can abstract hydrogen atoms from the other active site cysteine, Cys-416, and from coenzyme A, and it can also transfer hydrogen atoms to product radicals. The other active site cysteine can attack the central carbonyl of pyruvate and covalently bind the product acetyl group (By similarity).
Catalytic activity
- acetyl-CoA + formate = CoA + pyruvate
Pathway
Fermentation; pyruvate fermentation; formate from pyruvate: step 1/1.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 416 | S-acetylcysteine intermediate | ||||
Sequence: C | ||||||
Active site | 417 | Cysteine radical intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | formate C-acetyltransferase activity | |
Biological Process | glucose metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormate acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus > Lactococcus cremoris subsp. cremoris
Accessions
- Primary accessionO32799
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166694 | 1-787 | Formate acetyltransferase | |||
Sequence: MKTEVTENIFEQAWDGFKGTNWRDKASVTRFVQENYKPYDGDESFLAGPTERTLKVKKIIEDTKNHYEEVGFPFDTDRVTSIDKIPAGYIDANDKELELIYGMQNSELFRLNFMPRGGLRVAEKILTEHGLSVDPGLHDVLSQTMTSVNDGIFRAYTSAIRKARHAHTVTGLPDAYSRGRIIGVYARLALYGADYLMKEKAKEWDAITEINDDNIRLKEEINMQYQALQEVVNFGALYGLDVSRPAMNVKEAIQWVNIAYMAVCRVINGAATSLGRVPIVLDIFAERDLARGTFTEQEIQEFVDDFILKLRTMKFARAAAYDELYSGDPTFITTSMAGMGNDGRHRVTKMDYRFLNTLDTIGNAPEPNLTVLWDSKLPYSFKRYSMSMSHKHSSIQYEGVETMAKDGYGEMSCISCCVSPLDPENEEGRHNLQYFGARVNVLKAMLTGLNGGYDDVHKDYKVFDIEPVRDEILDYDTVMENFDKSLNWLTDTYVDAMNIIHYMTDKYNYEAVQMAFLPTKVRANMGFGICGFANTVDSLSAIKYAKVKTLRDENGYIYDYEVEGDFPRYGEDDDRADDIAKLVMKMYHEKLASHKLYKNAEATVSLLTITSNVAYSKQTGNSPVHKGVFLNEDGTVNKSKLEFFSPGANPSNKAKGGWLQNLRSLAKLEFKDANDGISLTTQVSPRALGKTRDEQVDNLVQILDGYFTPGALINGTEFAGQHVNLNVMDLKDVYDKIMRGEDVIVRISGYCVNTKYLTPEQKQELTERVFHEVLSNDDEEVMHTSNI | ||||||
Modified residue | 749 | Glycine radical | ||||
Sequence: G |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-629 | PFL | ||||
Sequence: NIFEQAWDGFKGTNWRDKASVTRFVQENYKPYDGDESFLAGPTERTLKVKKIIEDTKNHYEEVGFPFDTDRVTSIDKIPAGYIDANDKELELIYGMQNSELFRLNFMPRGGLRVAEKILTEHGLSVDPGLHDVLSQTMTSVNDGIFRAYTSAIRKARHAHTVTGLPDAYSRGRIIGVYARLALYGADYLMKEKAKEWDAITEINDDNIRLKEEINMQYQALQEVVNFGALYGLDVSRPAMNVKEAIQWVNIAYMAVCRVINGAATSLGRVPIVLDIFAERDLARGTFTEQEIQEFVDDFILKLRTMKFARAAAYDELYSGDPTFITTSMAGMGNDGRHRVTKMDYRFLNTLDTIGNAPEPNLTVLWDSKLPYSFKRYSMSMSHKHSSIQYEGVETMAKDGYGEMSCISCCVSPLDPENEEGRHNLQYFGARVNVLKAMLTGLNGGYDDVHKDYKVFDIEPVRDEILDYDTVMENFDKSLNWLTDTYVDAMNIIHYMTDKYNYEAVQMAFLPTKVRANMGFGICGFANTVDSLSAIKYAKVKTLRDENGYIYDYEVEGDFPRYGEDDDRADDIAKLVMKMYHEKLASHKLYKNAEATVSLLTITSNVAYSKQTGNSPVHKGVF | ||||||
Domain | 645-774 | Glycine radical | ||||
Sequence: SPGANPSNKAKGGWLQNLRSLAKLEFKDANDGISLTTQVSPRALGKTRDEQVDNLVQILDGYFTPGALINGTEFAGQHVNLNVMDLKDVYDKIMRGEDVIVRISGYCVNTKYLTPEQKQELTERVFHEVL |
Sequence similarities
Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length787
- Mass (Da)89,107
- Last updated1998-01-01 v1
- Checksum66537F086BC82E7E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ000325 EMBL· GenBank· DDBJ | CAA03991.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AM406671 EMBL· GenBank· DDBJ | CAL97231.1 EMBL· GenBank· DDBJ | Genomic DNA |