PF17392

Urocanase C-terminal domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameUrocanase_C
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description
Imported from IPR035401

This entry represents the C-terminal domain found in Urocanase.

Urocanase
[2]
(also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyses the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate:

urocanate + H2O = 4,5-dihydro-4-oxo-5-imidazolepropanoate

Urocanase is found in some bacteria (gene hutU)
[1]
, in the liver of many vertebrates, and has also been found in the plant Trifolium repens (white clover). Urocanase is a protein of about 60 Kd, it binds tightly to NAD+and uses it as an electrophil cofactor. A conserved cysteine has been found to be important for the catalytic mechanism and could be involved in the binding of the NAD+.

References
Imported from IPR035401

1.Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. Kaminskas E, Kimhi Y, Magasanik B. J. Biol. Chem. 245, 3536-44, (1970). PMID: 4990470

2.The urocanase story: a novel role of NAD+ as electrophile. Retey J. Arch. Biochem. Biophys. 314, 1-16, (1994). View articlePMID: 7944380

Wikipedia

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