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O26803 (GATE_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit E
Short name=Glu-ADT subunit E
EC=6.3.5.-
Gene names
Name:gatE
Ordered Locus Names:MTH_707
OrganismMethanobacterium thermoautotrophicum (strain Delta H)
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. HAMAP MF_00588

Catalytic activity

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP MF_00588

Subunit structure

Heterodimer of GatD and GatE.

Sequence similarities

Belongs to the GatB/GatE family. GatE subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aminoacyl-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

carbon-nitrogen ligase activity, with glutamine as amido-N-donor

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Glutamyl-tRNA(Gln) amidotransferase subunit E HAMAP MF_00588
PRO_0000140075

Secondary structure

1 .............................................................................................. 619
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O26803 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D362944674300A32

FASTA61969,533
        10         20         30         40         50         60 
MDWEKVGLKM GLEIHQQLDT ESKLFCPCRT ELTDSEPDHD IVRNLRPTQS ELGKFDRAAF 

        70         80         90        100        110        120 
EEAMRKLHFH YENYHEETCL VEADEEPPHP LNPEALEIAV TIALLLNMRV VDEFHTMRKQ 

       130        140        150        160        170        180 
VIDGSNTGGF QRTGLVATDG HLETPQGTVK IENLCLEEDA ARRIRETGDG VVFRLDRLGI 

       190        200        210        220        230        240 
PLVEITTDPS MSDPQQLREV AYQIGQILRS TRVKRGLGTI RQDLNISIRD GARVEVKGVQ 

       250        260        270        280        290        300 
DLDLIPEIVE REVKRQLSLV EIRDTLQERG AVVEDKIFDV SEVFADTESR IISSAESVLA 

       310        320        330        340        350        360 
VKLRGFDGLI GVEIQPGRRL GTEMADYAKK RGVSGIFHTD ELPAYGITEE EVRGLRDAVG 

       370        380        390        400        410        420 
ASQGDAVVMV AHERVTAENA LREVIRRAEM AIQGVPEETR KALPDGNTQY LRPLPTSSRM 

       430        440        450        460        470        480 
YLETDIPLFR IEDDLLEGIR RNLPELPSEK KERIMRDYGL SEDLASQLVK RNLVDEFEAL 

       490        500        510        520        530        540 
TEFRVDTTVI ASLLAYTLRE LRREGHDVDG LGLDELRDAI KLLEVGKISK DALRDIVACM 

       550        560        570        580        590        600 
ADEGLAAEDA ARKLNLLLLA EDEIESIIQE IVEGNLDMIS ERGMGAMGPL MGQAMGRLRG 

       610 
RADGKVVNRI LREKIQERL

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.
[2]"Domain-specific recruitment of amide amino acids for protein synthesis."
Tumbula D.L., Becker H.D., Chang W.-Z., Soell D.
Nature 407:106-110(2000) [PubMed: 10993083] [Abstract]
Cited for: CHARACTERIZATION.
Strain: Delta H.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000666 Genomic DNA. Translation: AAB85212.1.
PIRD69194.
RefSeqNP_275850.1. NC_000916.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D6FX-ray3.15C/D1-619[»]
ProteinModelPortalO26803.
SMRO26803. Positions 1-538.
ModBaseSearch...

Protein-protein interaction databases

STRINGO26803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1470668.
GenomeReviewsGene locus MTH_707 in contig AE000666_GR.
KEGGmth:MTH707.
NMPDRfig|187420.1.peg.705.

Phylogenomic databases

eggNOGarNOG04528.
HOGENOMHBG297405.
OMATSGFQRT.
PhylomeDBO26803.
ProtClustDBPRK04028.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14999.
MTHE187420:MTH707-MONOMER.

Family and domain databases

HAMAPMF_00588. GatE.
[Tree]
InterProIPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR004115. GAD_dom.
IPR023168. GatB_Yqey_C.
IPR004414. Gln-tRNA_amidoTrfase_esu.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:1.10.10.410. GatB_Yqey_C. 1 hit.
KOK03330.
PANTHERPTHR11659. GatB. 1 hit.
PfamPF02938. GAD. 1 hit.
PF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMSSF89095. GatB_Yqey. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00134. GatE_arch. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATE_METTH
AccessionPrimary (citable) accession number: O26803
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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