HMM Summary Page: TIGR02024

Functionglutamate formiminotransferase
Gene SymbolftcD
Trusted Cutoff221.25
Domain Trusted Cutoff221.25
Noise Cutoff164.80
Domain Noise Cutoff164.80
Isology Typeequivalog
EC Number2.1.2.5
HMM Length298
Mainrole CategoryEnergy metabolism
Subrole CategoryAmino acids and amines
Gene Ontology TermGO:0019556: histidine catabolic process to glutamate and formamide biological_process
GO:0030409: glutamate formimidoyltransferase activity molecular_function
GO:0030412: formimidoyltetrahydrofolate cyclodeaminase activity molecular_function
AuthorSelengut J
Entry DateOct 16 2003 10:43AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis HMM represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype [1]. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism [2].
ReferencesRN [1] RM PMID: 12815595 RT The molecular basis of glutamate formiminotransferase deficiency. RA Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS. RL Hum Mutat. 2003 Jul;22(1):67-73. RN [2] RM PMID: 10673422 RT The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme. RA Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A. RL Structure Fold Des. 2000 Jan 15;8(1):35-46.
Genome PropertyGenProp0145: histidine degradation to glutamate (HMM)
GenProp0145: histidine degradation to glutamate (HMM)