D5D9E2 (D5D9E2_BACMD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C HAMAP-Rule MF_00122
Short name=Asp/Glu-ADT subunit C HAMAP-Rule MF_00122
EC=6.3.5.- HAMAP-Rule MF_00122

Gene names

Name:	gatC HAMAP-Rule MF_00122 EMBL ADF37204.1
Ordered Locus Names:	BMD_0292

Organism

Bacillus megaterium (strain DSM 319) [Complete proteome] [HAMAP] EMBL ADF37204.1

Taxonomic identifier

592022 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus megaterium

Protein attributes

Sequence length	96 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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) By similarity. HAMAP-Rule MF_00122 SAAS SAAS003837
Catalytic activity	ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP-Rule MF_00122 SAAS SAAS003837 ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP-Rule MF_00122 SAAS SAAS003837
Subunit structure	Heterotrimer of A, B and C subunits By similarity. HAMAP-Rule MF_00122 SAAS SAAS003837
Sequence similarities	Belongs to the GatC family. HAMAP-Rule MF_00122

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00122 SAAS SAAS003837
Ligand	ATP-binding HAMAP-Rule MF_00122 SAAS SAAS003837 Nucleotide-binding
Molecular function	Ligase HAMAP-Rule MF_00122 SAAS SAAS003837 EMBL ADF37204.1 Transferase EMBL ADF37204.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	regulation of translational fidelity Inferred from electronic annotation. Source: InterPro translation Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	D5D9E2 [UniParc]. Last modified June 15, 2010. Version 1. Checksum: 782824E7F529C0D0	FASTA	96	10,783
	10 20 30 40 50 60 MSRISVDQVK HVANLARLAV TDDEAELFTK QLDAIITYAE QLDELDTTNV KPTSHVLDMK 70 80 90 NVMREDKPAK GLPIEDVVKN APDHKDGYIR VPTILE

References

[1]

"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure." Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S. Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 319.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001982 Genomic DNA. Translation: ADF37204.1.
RefSeq	YP_003595554.1. NC_014103.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADF37204; ADF37204; BMD_0292.
GeneID	9115683.
KEGG	bmd:BMD_0292.
PATRIC	37250531. VBIBacMeg104484_0239.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000017523.
KO	K02435.
Enzyme and pathway databases
BioCyc	BMEG592022:GIVX-292-MONOMER.
Family and domain databases
HAMAP	MF_00122. GatC.
InterPro	IPR003837. Asp/Glu-ADT_csu. [Graphical view]
Pfam	PF02686. Glu-tRNAGln. 1 hit. [Graphical view]
TIGRFAMs	TIGR00135. gatC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

D5D9E2_BACMD

Accession

Primary (citable) accession number: D5D9E2

Entry history

Integrated into UniProtKB/TrEMBL:	June 15, 2010
Last sequence update:	June 15, 2010
Last modified:	May 1, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)