E3HMV5 (E3HMV5_ACHXA) 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 ADP19462.1
Ordered Locus Names:	AXYL_06169 EMBL ADP19462.1

Organism

Achromobacter xylosoxidans (strain A8) [Complete proteome] [HAMAP] EMBL ADP19462.1

Taxonomic identifier

762376 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Achromobacter › Alcaligenes xylosoxydans xylosoxydans

Protein attributes

Sequence length	485 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 EMBL ADP19462.1 Transferase EMBL ADP19462.1
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)
	E3HMV5 [UniParc]. Last modified January 11, 2011. Version 1. Checksum: DABB0C823AAAF923	FASTA	485	52,499
	10 20 30 40 50 60 MNWEIVIGLE THTQLSTDSK IFSGSSTEFG AAPNTHANVV DLALPGSLPV MNRGAAERAI 70 80 90 100 110 120 RFGLAVGATI APRSVFARKN YFYPDLPKGY QISQYELPVV VGGSLSFFVG EEEKTVNLTR 130 140 150 160 170 180 AHLEEDAGKS LHDDFNLANG APASGIDLNR AGTPLLEIVT EPEMRSAAEA VSYARALHSL 190 200 210 220 230 240 VVWLGICDGN MQEGSFRCDA NVSVRPVGQK EFGTRTEIKN VNSFRFLERA IVYEARRQIE 250 260 270 280 290 300 LIEDGGTVVQ ETRLYDADRD ETRSMRSKED AHDYRYFPDP DLPTLVISSA WVDEVRAAMP 310 320 330 340 350 360 ELPAAQRARF ESEYGLPAYD AAQLTVSRDL AAYFEAVAHA LPAGQAKLAA NWVMGEVSAA 370 380 390 400 410 420 LNKDEKSIAD SPVQAPALAA LIGRIIDGTI SNKIAREVFG AMWAGENGGQ ADAIIDARGL 430 440 450 460 470 480 KQISDTGAIG AMIDEVLAAN PAIVEEYRAG KQKAFNSLVG QIMKAARGKA NPQQVNDLLK QKLDS

References

[1]

"Complete genome sequence of the haloaromatic acid-degrading bacterium Achromobacter xylosoxidans A8." Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V. J. Bacteriol. 193:791-792(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: A8 EMBL ADP19462.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002287 Genomic DNA. Translation: ADP19462.1.
RefSeq	YP_003982177.1. NC_014640.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADP19462; ADP19462; AXYL_06169.
GeneID	9900501.
KEGG	axy:AXYL_06169.
PATRIC	42565458. VBIAchXyl160325_6181.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000223742.
KO	K02434.
OMA	KNYFYAD.
Enzyme and pathway databases
BioCyc	AXYL762376:GJUB-6169-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

E3HMV5_ACHXA

Accession

Primary (citable) accession number: E3HMV5

Entry history

Integrated into UniProtKB/TrEMBL:	January 11, 2011
Last sequence update:	January 11, 2011
Last modified:	May 29, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)