Protein Family Models

These peptidases have gamma-glutamyl hydrolase activity; that is they catalyse the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to Pfam:PF00117, but contain extensions in four loops and at the C terminus [1]. [1]. 11953431. Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. Li H, Ryan TJ, Chave KJ, Van Roey P;. J Biol Chem 2002;277:24522-24529. (from Pfam)

Date:

2024-10-16

This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs [1]. [1]. 3298234. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. Hagervall TG, Edmonds CG, McCloskey JA, Bjork GR;. J Biol Chem 1987;262:8488-8495. Paper describing PDB structure 1gpm. [2]. 8548458. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL;. Nat Struct Biol 1996;3:74-86. Paper describing PDB structure 2der. [3]. 16871210. Snapshots of tRNA sulphuration via an adenylated intermediate. Numata T, Ikeuchi Y, Fukai S, Suzuki T, Nureki O;. Nature. 2006;442:419-424. Paper describing PDB structure 2vxo. [4]. 23816837. Substrate specificity and oligomerization of human GMP synthetase. Welin M, Lehtio L, Johansson A, Flodin S, Nyman T, Tresaugues L, Hammarstrom M, Graslund S, Nordlund P;. J Mol Biol. 2013;425:4323-4333. Paper describing PDB structure 3vrh. [5]. 23444054. Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA. Nakagawa H, Kuratani M, Goto-Ito S, Ito T, Katsura K, Terada T, Shirouzu M, Sekine S, Shigi N, Yokoyama S;. Proteins. 2013;81:1232-1244. Paper describing PDB structure 5mko. [6]. 28655838. Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster. Arragain S, Bimai O, Legrand P, Caillat S, Ravanat JL, T. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. [1]. 8895556. Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A;. EMBO J 1996;15:5125-5134. (from Pfam)

Date:

2024-10-16

Date:

2024-11-04

GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases Swiss:P49915 EC:6.3.5.2. In prokaryotes this domain mediates dimerisation. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains. [1]. 8548458. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL;. Nat Struct Biol 1996;3:74-86. (from Pfam)

Date:

2024-10-16

glutamine-hydrolyzing GMP synthase catalyzes the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP

Date:

2024-07-16

This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit.

Gene:

guaA

Date:

2024-05-30

This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit

Gene:

guaA

Date:

2024-05-30

Contains glutamine-hydrolyzing domain and glutamine amidotransferase; GMP-binding domain; functions to produce GMP from XMP in the IMP pathway

Gene:

guaA

Date:

2021-07-21