Accession | TIGR01230 |
Name | agmatinase |
Function | agmatinase |
Gene Symbol | speB |
Trusted Cutoff | 174.30 |
Domain Trusted Cutoff | 174.30 |
Noise Cutoff | 141.00 |
Domain Noise Cutoff | 141.00 |
Isology Type | equivalog |
EC Number | 3.5.3.11 |
HMM Length | 275 |
Gene Ontology Term | GO:0008295: spermidine biosynthetic process biological_process |
| GO:0008783: agmatinase activity molecular_function |
Author | Haft DH |
Entry Date | May 8 2001 11:06AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Members of this family include known and predicted examples of agmatinase (agmatine ureohydrolase). The seed includes members of archaea, for which no definitive agmatinase sequence has yet been made available. However, archaeal sequences are phylogenetically close to the experimentally verified B. subtilis sequence. One species of Halobacterium has been demonstrated in vitro to produce agmatine from arginine, but no putrescine from ornithine, suggesting that arginine decarboxylase and agmatinase, rather than arginase and ornithine decarboxylase, lead from Arg to polyamine biosynthesis.
Note: a history of early misannotation of members of this family is detailed in PUBMED:10931887. |
References | DR EXPERIMENTAL; EGAD|47504; Synechocystis PCC6803
DR EXPERIMENTAL; GP|10184435; Neisseria gonorrhoeae
RM 10931887
RT Phylogeny of related functions: the case of polyamine biosynthetic enzymes.
RA Sekowska A, Danchin A, Risler JL
RL Microbiology 2000 Aug;146 ( Pt 8):1815-28
DR HAMAP; MF_01418; 33 of 34 |
Genome Property | GenProp0642: putrescine biosynthesis from arginine utilizing agmatinase (HMM) |