Glutamyl-tRNA(Gln) amidotransferase subunit E - Pyrococcus abyssi (strain GE5 / Orsay)

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Q9V0U0 (GATE_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit E
Short name=Glu-ADT subunit E
EC=6.3.5.-

Gene names

Name:	gatE
Ordered Locus Names:	PYRAB06990
ORF Names:	PAB1902

Organism

Pyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]

Taxonomic identifier

272844 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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 By similarity. HAMAP MF_00588
Sequence similarities	Belongs to the GatB/GatE family. GatE subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 633

633

Glutamyl-tRNA(Gln) amidotransferase subunit E HAMAP MF_00588

PRO_0000140076

Secondary structure

633

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9V0U0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3F1BE701DBA6214A
Show »

FASTA

633

71,876

        10         20         30         40         50         60 
MMVMTDKFNY EELGLKVGLE IHRQLDTKKL FSPVPSELSD KVEFTFQRRL RPTMSELGEI 

        70         80         90        100        110        120 
DPAALEEFKK GRVYVYEGNY ELTDLVYMDE EPPRGPDREA LEVALQIAYL LNAKPVDEVY 

       130        140        150        160        170        180 
YMRKIVIDGS NVSGFQRTAI IATDGKVETP WGAVGIPTIC LEEDAARIIE RKDKEVIYRL 

       190        200        210        220        230        240 
DRLGIPLIEI STTPDIHHPE QAKVVAKFIG DALRATKKVK RGLGTIRQDL NVSIKGGARI 

       250        260        270        280        290        300 
EIKGVQELDM IPIIIEREVE RQLNLLKIRD ELRKRGVKPK DIKEEFYDVT DIFENTKSKI 

       310        320        330        340        350        360 
IARVIKKGGK VLAIKLPKFR GLIGREIQPG RRLGTEFADR AKKYVPGIFH IDELPNYGIS 

       370        380        390        400        410        420 
QEEVNKVIER LNLSEEDAFV LVAAEEEKAK NALREVIKRA REAIEGVPEE TRRALPDGNT 

       430        440        450        460        470        480 
EYMRPLPGKA RMYPETDIPP LRIPDDLKKK IKENLPELPQ AKVERYVKEY KLDRSLAQTL 

       490        500        510        520        530        540 
VDDERDELFE ELVSMGVKPS LAASILVVVL KGLRKEVPIE NVTDEHIREA FQLYLEGKIA 

       550        560        570        580        590        600 
KEAFEEIFKE LARNPSKSAR EVAEEKGLTL LSEEEVTRII EEVIQQNIEV VKAKGMGAMG 

       610        620        630 
LIMGRVMAKV RGKADGKLVS QIVRRKLQEI SGG

« Hide

References

[1]

"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ248285 Genomic DNA. Translation: CAB49613.1.

PIR

D75112.

RefSeq

NP_126382.1. NC_000868.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZQ1	X-ray	3.00	C/D	1-633	[»]

ProteinModelPortal

Q9V0U0.

SMR

Q9V0U0. Positions 5-512.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48454N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000003589; EBPYRP00000003520; EBPYRG00000003589.

GeneID

1495603.

GenomeReviews

Gene locus PYRAB06990 in contig AL096836_GR.

KEGG

pab:PAB1902.

NMPDR

fig|272844.1.peg.727.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022699.

HOGENOM

HBG297405.

OMA

TSGFQRT.

PhylomeDB

Q9V0U0.

ProtClustDB

PRK04028.

Enzyme and pathway databases

BioCyc

PABY272844:PAB1902-MONOMER.

Family and domain databases

HAMAP

MF_00588. GatE.
[Tree]

InterPro

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.
IPR004115. GAD_dom.
IPR023168. GatB_Yqey_C.
IPR004414. Gln-tRNA_amidoTrfase_esu.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]

Gene3D

G3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:1.10.10.410. GatB_Yqey_C. 1 hit.

K03330.

PANTHER

PTHR11659. GatB. 1 hit.

Pfam

PF02938. GAD. 1 hit.
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.
SSF55261. SSF55261. 1 hit.

TIGRFAMs

TIGR00134. GatE_arch. 1 hit.

PROSITE

PS01234. GATB. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GATE_PYRAB

Accession

Primary (citable) accession number: Q9V0U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents