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Links from Protein

Items: 8

1.

Amidohydrolase BAB2_0307-like, N-terminal domain

This small domain is found at the N-terminal end of Amidohydrolase from Brucella abortus (BAB2_0307, Swiss:Q2YIL4) and similar proteins predominantly found in proteobacteria. This domain shows an all-beta structure. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046272.1
Method:
HMM
2.

amidohydrolase family protein

This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyse the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit [3]. Dihydroorotases (EC:3.5.2.3) are also included [4-5]. [1]. 9144792. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Holm L, Sander C;. Proteins 1997;28:72-82. [2]. 8550522. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. Nygaard P, Duckert P, Saxild HH;. J Bacteriol 1996;178:846-853. [3]. 7754395. The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA;. Science 1995;268:998-1004. [4]. 9878395. Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi. Gao G, Nara T, Nakajima-Shimada J, Aoki T;. J Mol Biol 1999;285:149-161. [5]. 8590465. As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe. Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL;. Curr Genet 1995;28:138-149. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2024-10-16
Family Accession:
NF014081.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

formimidoylglutamate deiminase

GO Terms:
Molecular Function:
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds (GO:0016810)
Date:
2021-10-04
Family Accession:
NF006683.0
Method:
HMM
6.

formimidoylglutamate deiminase

GO Terms:
Molecular Function:
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds (GO:0016810)
Date:
2021-10-01
Family Accession:
NF006684.0
Method:
HMM
7.

formimidoylglutamate deiminase

In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This HMM describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate.

Gene:
hutF
GO Terms:
Biological Process:
L-histidine catabolic process to glutamate and formate (GO:0019557)
Molecular Function:
formimidoylglutamate deiminase activity (GO:0050416)
Date:
2021-04-27
Family Accession:
TIGR02022.1
Method:
HMM
8.

formimidoylglutamate deiminase

formimidoylglutamate deiminase catalyzes the deimination of N-formimidoyl-L-glutamate to form ammonia and N-formyl-L-glutamate in the histidine degradation pathway

Date:
2016-06-06
Family Accession:
10793171
Method:
Sparcle
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