C8NL48 (C8NL48_COREF) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
Short name=Asp/Glu-ADT subunit B HAMAP-Rule MF_00121
EC=6.3.5.- HAMAP-Rule MF_00121

Gene names

Name:	gatB HAMAP-Rule MF_00121 EMBL EEW50635.1
ORF Names:	HMPREF0290_0723 EMBL EEW50635.1

Organism

Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) EMBL EEW50635.1

Taxonomic identifier

196164 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium efficiens

Protein attributes

Sequence length	501 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_00121 SAAS SAAS018027
Catalytic activity	ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP-Rule MF_00121 SAAS SAAS018027 ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP-Rule MF_00121
Subunit structure	Heterotrimer of A, B and C subunits By similarity. SAAS SAAS018027 HAMAP-Rule MF_00121
Sequence similarities	Belongs to the gatB/gatE family. GatB subfamily. HAMAP-Rule MF_00121

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00121
Ligand	ATP-binding HAMAP-Rule MF_00121 Nucleotide-binding
Molecular function	Ligase HAMAP-Rule MF_00121 EMBL EEW50635.1 Transferase EMBL EEW50635.1
Gene Ontology (GO)
Biological_process	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)
	C8NL48 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: 8FE00DAFCE208253	FASTA	501	54,549
	10 20 30 40 50 60 MTAAFYDLMD FDEVLEKYDP VMGLEVHVEL ATETKMFSAS SAHFGAAPNS NVDPVSLGLP 70 80 90 100 110 120 GALPVVNAKG VEWAIKIGLA LNCSIAESSR FARKNYFYPD QPKNYQISQY DEPIAYDGYL 130 140 150 160 170 180 DVMLEDGTEW RIEIERAHME EDTGKLTHLG GTSGRIHGAT ASLVDCNRAG VPLIEIVTKP 190 200 210 220 230 240 IEGAGARAPE IAKAYVSALR DLVKALGVSD GRLDQGSMRV DANLSLRPIG QEEFGTRTET 250 260 270 280 290 300 KNINSLKSVE QAITFEMQRQ AHVLDNGGTI DQETRHYQET DGTTSKGRPK ETAEDYRYFN 310 320 330 340 350 360 DPDLPPVIAP AEWVEEIRAT LPELPWVRRA RIQEEWKLSD AEMRDLVNAN ALDLIIETVE 370 380 390 400 410 420 AGTTPDEARA WWVSYLSQKA NETGVELEAL PVTPAHVARV VALIKEGKLT NKLGRQAIDG 430 440 450 460 470 480 VLAGEGDVDA VVASRGLEVV RDDGAIEAAV DEALAANPDI VEKYRAGNTK VTGAIVGAVM 490 500 KATRGKADPA QVNKLIAEKL A

References

[1]

Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R. , Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., Petrosino J., Highlander S., Gibbs R. Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: YS-314 EMBL EEW50635.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACLI01000045 Genomic DNA. Translation: EEW50635.1.
RefSeq	NP_737961.1. NC_004369.1.
3D structure databases
ProteinModelPortal	C8NL48.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1033716.
KEGG	cef:CE1351.
PATRIC	21488834. VBICorEff9312_1350.
Phylogenomic databases
eggNOG	COG0064.
KO	K02434.
OMA	KNYFYAD.
ProtClustDB	PRK05477.
Enzyme and pathway databases
BioCyc	CEFF196164:GJW8-1371-MONOMER.
Family and domain databases
Gene3D	1.10.10.410. 1 hit.
HAMAP	MF_00121. GatB.
InterPro	IPR004413. Apn/Gln-ADT_bsu. IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E. IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat. IPR018027. Asn/Gln_amidotransferase. IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel. IPR023168. GatB_Yqey_C. IPR017958. Gln-tRNA_amidoTrfase_suB_CS. [Graphical view]
PANTHER	PTHR11659. PTHR11659. 1 hit.
Pfam	PF02934. GatB_N. 1 hit. PF02637. GatB_Yqey. 1 hit. [Graphical view]
SMART	SM00845. GatB_Yqey. 1 hit. [Graphical view]
SUPFAM	SSF89095. GatB_Yqey. 1 hit.
TIGRFAMs	TIGR00133. gatB. 1 hit.
PROSITE	PS01234. GATB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C8NL48_COREF

Accession

Primary (citable) accession number: C8NL48

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)