| Comment | This subset of the radical-SAM family (PF04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA, [1]), benzylsuccinate synthase (BssD, [2]), gycerol dehydratase (DhaB2, [3]) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines. |
| References | RN [1]
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RT Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity.
RA Andrei PI, Pierik AJ, Zauner S, Andrei-Selmer LC, Selmer T.
RL Eur J Biochem. 2004 Jun;271(11):2225-30.
RN [2]
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RT Genes involved in the anaerobic degradation of toluene in a denitrifying bacterium, strain EbN1.
RA Kube M, Heider J, Amann J, Hufnagel P, Kuhner S, Beck A, Reinhardt R, Rabus R.
RL Arch Microbiol. 2004 Mar;181(3):182-94. Epub 2004 Jan 21.
RN [3]
RM PMID: 12704244
RT Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum.
RA Raynaud C, Sarcabal P, Meynial-Salles I, Croux C, Soucaille P.
RL Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5010-5. Epub 2003 Apr 18. |
