HMM Summary Page: TIGR03458

AccessionTIGR03458
NameYgfH_subfam
Functionsuccinate CoA transferase
Trusted Cutoff658.70
Domain Trusted Cutoff658.70
Noise Cutoff610.30
Domain Noise Cutoff610.30
Isology Typesubfamily
EC Number2.8.3.-
HMM Length489
AuthorSelengut J
Entry DateJul 23 2007 11:12AM
Last ModifiedFeb 21 2012 12:19PM
CommentThis family of CoA transferases includes enzymes catalyzing at least two related but distinct activities. The E. coli YgfH protein has been characterized as a propionyl-CoA:succinate CoA transferase [1] where it appears to be involved in a pathway for the decarboxylation of succinate to propionate. The Clostridium kluyveri CAT1 protein has been characterized as a acetyl-CoA:succinate CoA transferase [2] and is believed to be involved in anaerobic succinate degradation. The propionate:succinate transferase activity has been reported in the propionic acid fermentation of propionibacterium species [3] where it is distinct from the coupled activities of distinct nucleotide-triphosphate dependent succinate and propionate/acetate CoA transferases (as inferred from activity in the absence of NTPs). The family represented by this model includes a member from Propionibacterium acnes KPA171202 which is likely to be responsible for this activity. A closely related clade not included in this family are the Ach1p proteins of fungi which are acetyl-CoA hydrolases [4]. This name has been applied to many of the proteins modeled by this HMM, possibly erroneously.
ReferencesRN [1] RM PMID:10769117 RT Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli. RA Haller T, Buckel T, Retey J, Gerlt JA RL Biochemistry. 2000 Apr 25;39(16):4622-9. RN [2] RM PMID:8550525 RT Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri. RA Sohling B, Gottschalk G RL J Bacteriol. 1996 Feb;178(3):871-80. RN [3] RM PMID:14102852 RT PURIFICATION AND PROPERTIES OF ENZYMES INVOLVED IN THE PROPIONIC ACID FERMENTATION. RA ALLEN SH, KELLERMEYER RW, STJERNHOLM RL, WOOD HG RL J Bacteriol. 1964 Jan;87:171-87. RN [4] RM PMID:12606555 RT Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae. RA Buu LM, Chen YC, Lee FJ RL J Biol Chem. 2003 May 9;278(19):17203-9. Epub 2003 Feb 26.
Genome PropertyGenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)
GenProp0755: pyruvate conversion to propionate, anaerobic, FAD/NAD-regenerating (HMM)