|Domain Trusted Cutoff||221.25|
|Domain Noise Cutoff||164.80|
|Mainrole Category||Energy metabolism|
|Subrole Category||Amino acids and amines|
|Gene Ontology Term||GO:0019556: histidine catabolic process to glutamate and formamide biological_process|
| ||GO:0030409: glutamate formimidoyltransferase activity molecular_function|
| ||GO:0030412: formimidoyltetrahydrofolate cyclodeaminase activity molecular_function|
|Entry Date||Oct 16 2003 10:43AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This 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 . The crystal structure of the enzyme has been studied in the context of the catalytic mechanism .|
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.
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 Property||GenProp0145: histidine degradation to glutamate (HMM)|
| ||GenProp0145: histidine degradation to glutamate (HMM)|
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