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Links from Protein

Items: 12

1.

Dihydroorotate dehydrogenase

GO Terms:
Cellular Component:
cytoplasm (GO:0005737)
Molecular Function:
oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627)
Date:
2024-08-14
Family Accession:
NF013355.5
Method:
HMM
2.

HisA/HisF-related TIM barrel protein

Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalysed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel e.g. Swiss:P05325 [2]. This family belong to the common phosphate binding site TIM barrel family [3]. [1]. 9332345. Paralogous histidine biosynthetic genes: evolutionary analysis. of the Saccharomyces cerevisiae HIS6 and HIS7 genes.. Fani R, Tamburini E, Mori E, Lazcano A, Lio P, Barberio C,. Casalone E, Cavalieri D, Perito B, Polsinelli M,. Gene 1997;197:9-17.. [2]. 8028028. The evolution of the histidine biosynthetic genes in. prokaryotes: a common ancestor for the hisA and hisF genes.. Fani R, Lio P, Chiarelli I, Bazzicalupo M;. J Mol Evol 1994;38:489-495.. [3]. 11054297. Homology among (betaalpha)(8) barrels: implications for the. evolution of metabolic pathways.. Copley RR, Bork P;. J Mol Biol 2000;303:627-641. (from Pfam)

GO Terms:
Biological Process:
L-histidine biosynthetic process (GO:0000105)
Date:
2024-08-14
Family Accession:
NF013168.5
Method:
HMM
3.

tRNA-dihydrouridine synthase

Members of this family catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 (Swiss:Q9HGN6) from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 (Swiss:P53720) acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD [1]. Some family members may be targeted to the mitochondria and even have a role in mitochondria [1]. [1]. 12003496. A conserved family of Saccharomyces cerevisiae synthases effects. dihydrouridine modification of tRNA.. Xing F, Martzen MR, Phizicky EM;. RNA 2002;8:370-381. (from Pfam)

GO Terms:
Biological Process:
tRNA processing (GO:0008033)
Molecular Function:
tRNA dihydrouridine synthase activity (GO:0017150)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-08-14
Family Accession:
NF013380.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.

dihydroorotate dehydrogenase

This family includes dihydroorotate dehydrogenases EC 1.3.1.14, which uses NAD(+) as an acceptor, and EC 1.3.98.1, which uses fumarate as an acceptor, as the enzyme converts dihydroorotate to orotate during pyrimidine nucleotide biosynthesis.

Date:
2023-07-14
Family Accession:
TIGR01037.2
Method:
HMM
10.

dihydroorotate dehydrogenase

catalytic subunit of dihydroorotate dehydrogenase 1B (NAD(+)) catalyzes the conversion of (S)-dihydroorotate and NAD(+) to orotate and NADH

Date:
2016-05-13
Family Accession:
10012903
Method:
Sparcle
11.

dihydroorotate dehydrogenase

GO Terms:
Molecular Function:
dihydroorotate dehydrogenase activity (GO:0004152)
Biological Process:
pyrimidine nucleotide biosynthetic process (GO:0006221)
Date:
2021-07-30
Family Accession:
NF005574.0
Method:
HMM
12.
new record, indexing in progress
Family Accession:
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