F2LUG1 (F2LUG1_HIPMA) 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
Ordered Locus Names:	Hipma_0516 EMBL AEA33487.1

Organism

Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2) [Complete proteome] [HAMAP] EMBL AEA33487.1

Taxonomic identifier

760142 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfurellales › Desulfurellaceae › Hippea › Hippea maritima

Protein attributes

Sequence length	475 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 SAAS004413
Catalytic activity	ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP-Rule MF_00121 SAAS SAAS004413 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. HAMAP-Rule MF_00121 SAAS SAAS004413
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 Transferase EMBL AEA33487.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	F2LUG1 [UniParc]. Last modified May 31, 2011. Version 1. Checksum: EBDF39D4958734F8	FASTA	475	54,165
	10 20 30 40 50 60 MEFEAVIGLE VHIQLLTNTK IFCSCSTDFG APPNTHICPV CMGMPGVLPV LNKKVLDYAI 70 80 90 100 110 120 KLGLALNCKI NKFSRFARKN YFYPDLPKGY QISQYELPIL EGGHVEIFVN GEYKKIGLER 130 140 150 160 170 180 IHMEEDAGKT IHRPDGSYVD FNRAGVPLLE IVSLPVMHSP QEAGEYLRSL RRIVRYLGIC 190 200 210 220 230 240 DGNMEEGSLR CDANVSIRPK GQTKLGTKTE LKNMNSFRHV EKALEYEIQR QIEVVEDGGK 250 260 270 280 290 300 IIQQTRLWDE KTGMTKPMRS KEEAYEYRYF PDPDLVPIFI DDEWIERIKD EVPELPRQKL 310 320 330 340 350 360 ERFVEEYGLK EEDARVLVEE KSLADYFEEA AKGYKKPQSI ANWILSELLG YLNKENKNIE 370 380 390 400 410 420 DTLIKPNHIR ELVELIDSGL ISGKIAKTVF GKMYETAKSP KQIVEEEGLV QITDRSQIEG 430 440 450 460 470 IVDEVIKANP KAVEQYKSGK KNTIGFFVGQ VMKKTKGKAN PKLVNEILAS KLEEL

References

[1]

"The complete genome of Hippea maritima DSM 10411." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L. , Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A. Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700847 / DSM 10411 / MH2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002606 Genomic DNA. Translation: AEA33487.1.
RefSeq	YP_004339546.1. NC_015318.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEA33487; AEA33487; Hipma_0516.
GeneID	10391843.
KEGG	hmr:Hipma_0516.
PATRIC	54411698. VBIHipMar155866_0523.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K02434.
Enzyme and pathway databases
BioCyc	HMAR760142:GHVE-535-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

F2LUG1_HIPMA

Accession

Primary (citable) accession number: F2LUG1

Entry history

Integrated into UniProtKB/TrEMBL:	May 31, 2011
Last sequence update:	May 31, 2011
Last modified:	May 29, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)