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ENZYME entry: EC 2.5.1.108

Accepted Name
2-(3-amino-3-carboxypropyl)histidine synthase.
Reaction catalysed
L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine <=> 2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
Cofactor(s)
Iron-sulfur.
Comment(s)
  • Modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical.
  • The enzyme is present in archae and eukaryotes but not in eubacteria.
  • Part of diphthamide biosynthesis.
  • Formerly EC 2.5.1.n7.
Cross-references
BRENDA2.5.1.108
EC2PDB2.5.1.108
ExplorEnz2.5.1.108
PRIAM enzyme-specific profiles2.5.1.108
KEGG Ligand Database for Enzyme Nomenclature2.5.1.108
IUBMB Enzyme Nomenclature2.5.1.108
IntEnz2.5.1.108
MEDLINEFind literature relating to 2.5.1.108
MetaCyc2.5.1.108
Rhea expert-curated reactions2.5.1.108
UniProtKB/Swiss-Prot
Q75AZ9, DPH1_ASHGO;  Q4X0S7, DPH1_ASPFU;  Q3SYT1, DPH1_BOVIN;  
P49958, DPH1_CAEEL;  Q59MG1, DPH1_CANAL;  Q6FTG1, DPH1_CANGA;  
Q5ZHX9, DPH1_CHICK;  P0CN19, DPH1_CRYNB;  P0CN18, DPH1_CRYNJ;  
Q567W6, DPH1_DANRE;  Q6BPU5, DPH1_DEBHA;  Q54PW5, DPH1_DICDI;  
Q5AZJ7, DPH1_EMENI;  Q8SUZ5, DPH1_ENCCU;  Q4IQ72, DPH1_GIBZE;  
Q9BZG8, DPH1_HUMAN;  Q6CLC9, DPH1_KLULA;  Q5NCQ5, DPH1_MOUSE;  
A7SLX5, DPH1_NEMVE;  Q7SC98, DPH1_NEUCR;  Q3T7C9, DPH1_PENVA;  
O59713, DPH1_SCHPO;  Q4PA25, DPH1_USTMA;  Q6GPQ5, DPH1_XENLA;  
Q6C0S8, DPH1_YARLI;  P40487, DPH1_YEAST;  Q757B6, DPH2_ASHGO;  
Q4WN99, DPH2_ASPFU;  Q08DM2, DPH2_BOVIN;  Q09454, DPH2_CAEEL;  
Q6FPD9, DPH2_CANGA;  Q5ZKI2, DPH2_CHICK;  Q002B5, DPH2_CRIGR;  
P0CN21, DPH2_CRYNB;  P0CN20, DPH2_CRYNJ;  A4QN59, DPH2_DANRE;  
Q6BMF6, DPH2_DEBHA;  B0G132, DPH2_DICDI;  Q5B2Q1, DPH2_EMENI;  
Q4I5M4, DPH2_GIBZE;  Q9BQC3, DPH2_HUMAN;  Q6CS90, DPH2_KLULA;  
Q57907, DPH2_METJA;  Q9CR25, DPH2_MOUSE;  A7SKJ3, DPH2_NEMVE;  
Q7S5C0, DPH2_NEUCR;  Q5RE82, DPH2_PONAB;  O58832, DPH2_PYRHO;  
Q568Y2, DPH2_RAT;  Q10206, DPH2_SCHPO;  Q6DE00, DPH2_XENLA;  
Q6CGE7, DPH2_YARLI;  P32461, DPH2_YEAST;  

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