Home  |  Contact

A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.21.4.2

Accepted Name
Glycine reductase.
Reaction catalysed
Acetyl phosphate + NH(3) + thioredoxin disulfide + H(2)O <=> glycine + phosphate + thioredoxin
Comment(s)
  • The reaction is observed only in the direction of glycine reduction.
  • The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C.
  • Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release.
  • Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate.
  • Only subunit B distinguishes this enzyme from EC 1.21.4.3 and EC 1.21.4.4.
Cross-references
BRENDA1.21.4.2
EC2PDB1.21.4.2
ExplorEnz1.21.4.2
PRIAM enzyme-specific profiles1.21.4.2
KEGG Ligand Database for Enzyme Nomenclature1.21.4.2
IUBMB Enzyme Nomenclature1.21.4.2
IntEnz1.21.4.2
MEDLINEFind literature relating to 1.21.4.2
MetaCyc1.21.4.2
UniProtKB/Swiss-Prot
P50972, GRDA1_PEPAC;  Q6LH20, GRDA1_PHOPR;  O32518, GRDA2_PEPAC;  
Q6LH19, GRDA2_PHOPR;  P26971, GRDA_ACESD;  A6TU46, GRDA_ALKMQ;  
Q3A9J5, GRDA_CARHZ;  A7FTE0, GRDA_CLOB1;  A7GCV1, GRDA_CLOBL;  
P26970, GRDA_CLOPU;  P52216, GRDA_PEPLI;  Q67KE6, GRDA_SYMTH;  
Q73PQ2, GRDA_TREDE;  Q3A9J4, GRDB_CARHZ;  P55793, GRDB_CLOPU;  
Q9R4G8, GRDB_PEPAC;  P52217, GRDB_PEPLI;  Q67KE7, GRDB_SYMTH;  
P54935, GRDC_PEPAC;  Q47878, GRDD_PEPAC;  Q9EV94, GRDE_ACESD;  
Q9R4G7, GRDE_PEPAC;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.21.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.21.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-