glutamyl-tRNA(GLN) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.

Glutaminyl-tRNA synthetase (EC 6.1.1.18) (Glutamine--tRNA ligase) (GlnRS). glnS: glutaminyl-tRNA synthetase; High confidence in function and specificity.

Glutamate-tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.

2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; TREMBLNEW:47357: 69% identity, 80% similarity. 2-hydroxy-6-oxo-6-phenylhexa-24-dienoate hydrolase. The alpha/beta hydrolase fold [1] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices Pfam: Ndr family. TIGR00148: conserved hypothetical protein; High confidence in function and specificity.

AspS protein; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Putative Hydantoin racemase,28% Identity toTrEMBL;Q7NTB3,Q885G0,Q6YNI1. SProt;Q00924. Has PF01177,Asp/Glu/Hydantoin racemase;IPR001920, Asp/Glu_race; This family contains aspartate racemase, glutamate racemase,hydantoin racemase and arylmalonate decarboxylase. Aspartate racemase (EC: 5.1.1.13) and glutamate racemase (EC: 5.1.1.3) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity. Glutamate racemase, which interconverts L-glutamate into D-glutamate, is required for the biosynthesis of peptidoglycan and some peptide-based antibiotics [...]

Glutamate-tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.

Indoleacetamide hydrolase (EC 3.5.1.-) (IAH) (Indole-3-acetamide hydrolase). Hydrolyzes indole-3-acetamide (IAM) into indole-3- acetic acid (IAA); Family membership; Belongs to the amidase family.

Conserved hypothetical urea amidolyase-related protein. Homology to ybgK of E. coli of 36% (sprot|YBGK_ECOLI). InterPro: DUF183 (IPR003778) Uncharacterized domain in proteins of unknown function. This domain is found in a multifunctional enzyme, urea amidolyase, from yeast. Pfam: DFU182, uncharcterized ACR,COG1984 no signal peptide no TMHs; Function unclear.