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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit D

Gene

gatD

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021UniRule annotation
Active sitei178 – 1781UniRule annotation
Active sitei179 – 1791UniRule annotation
Active sitei256 – 2561UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit DUniRule annotation (EC:6.3.5.-UniRule annotation)
Short name:
Glu-ADT subunit DUniRule annotation
Gene namesi
Name:gatDUniRule annotation
Ordered Locus Names:PYRAB07000
ORF Names:PAB1901
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000810 Componenti: Chromosome
  • UP000009139 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Glutamyl-tRNA(Gln) amidotransferase subunit DPRO_0000140058Add
BLAST

Interactioni

Subunit structurei

Heterodimer of GatD and GatE.UniRule annotation

Protein-protein interaction databases

DIPiDIP-48453N.
STRINGi272844.PAB1901.

Structurei

Secondary structure

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Beta strandi17 – 3014Combined sources
Beta strandi33 – 353Combined sources
Beta strandi45 – 517Combined sources
Beta strandi56 – 605Combined sources
Helixi61 – 633Combined sources
Beta strandi64 – 718Combined sources
Beta strandi93 – 986Combined sources
Beta strandi105 – 1084Combined sources
Turni109 – 1124Combined sources
Beta strandi113 – 1164Combined sources
Helixi120 – 1267Combined sources
Helixi128 – 1325Combined sources
Beta strandi134 – 1407Combined sources
Helixi146 – 1483Combined sources
Helixi151 – 16616Combined sources
Beta strandi170 – 1756Combined sources
Beta strandi178 – 1803Combined sources
Helixi181 – 19111Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi199 – 2024Combined sources
Helixi215 – 22612Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi232 – 24413Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi307 – 3115Combined sources
Helixi319 – 3268Combined sources
Beta strandi330 – 3378Combined sources
Turni338 – 3403Combined sources
Helixi344 – 3463Combined sources
Helixi347 – 3559Combined sources
Beta strandi359 – 36911Combined sources
Beta strandi374 – 3763Combined sources
Helixi377 – 3848Combined sources
Helixi395 – 40612Combined sources
Helixi412 – 4209Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZQ1X-ray3.00A/B1-438[»]
ProteinModelPortaliQ9V0T9.
SMRiQ9V0T9. Positions 2-438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9V0T9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 422331Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the asparaginase 1 family. GatD subfamily.UniRule annotation
Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG01924. Archaea.
COG0252. LUCA.
HOGENOMiHOG000227975.
KOiK09482.
OMAiMHGETGD.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
HAMAPiMF_00586. GatD.
InterProiIPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR011878. GatD.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF500175. Glu_ADT_D. 1 hit.
PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00519. asnASE_I. 1 hit.
TIGR02153. gatD_arch. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V0T9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVDEFLKER NINVGDFVRI TKEEDGEEVT YEGYIMPPYE LSAGDTLVLK
60 70 80 90 100
LENGYNIGIA LEKIRRIEVL ERAKVKPEVH FEALIEGKPG LPEVTIIGTG
110 120 130 140 150
GTIASRIDYE TGAVYPAFTA EELAKAVPEI FEVANVKPKL LFNIFSEDMK
160 170 180 190 200
PKHWVKIAHE VAKALNSGDY GVVVAHGTDT MGYTAAALSF MLRNLGKPVV
210 220 230 240 250
LVGAQRSSDR PSSDAAMNLI CSVRMATSEV AEVMVVMHGE TGDTYCLAHR
260 270 280 290 300
GTKVRKMHTS RRDAFRSIND VPIAKIWPNG EIEFLRKDYR KRSDEEVEVD
310 320 330 340 350
DKIEEKVALV KVYPGISSEI IDFLVDKGYK GIVIEGTGLG HTPNDIIPSI
360 370 380 390 400
ERAVEEGVAV CMTSQCIYGR VNLNVYSTGR KLLKAGVIPC EDMLPETAYV
410 420 430
KLMWVLGHTQ NLEEVRKMML TNYAGEITPY TRFDTYLR
Length:438
Mass (Da):48,860
Last modified:May 1, 2000 - v1
Checksum:i39C616E89496D61C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248285 Genomic DNA. Translation: CAB49614.1.
HE613800 Genomic DNA. Translation: CCE70091.1.
PIRiE75112.
RefSeqiWP_010867819.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB49614; CAB49614; PAB1901.
GeneIDi1495604.
KEGGipab:PAB1901.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248285 Genomic DNA. Translation: CAB49614.1.
HE613800 Genomic DNA. Translation: CCE70091.1.
PIRiE75112.
RefSeqiWP_010867819.1. NC_000868.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZQ1X-ray3.00A/B1-438[»]
ProteinModelPortaliQ9V0T9.
SMRiQ9V0T9. Positions 2-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48453N.
STRINGi272844.PAB1901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB49614; CAB49614; PAB1901.
GeneIDi1495604.
KEGGipab:PAB1901.

Phylogenomic databases

eggNOGiarCOG01924. Archaea.
COG0252. LUCA.
HOGENOMiHOG000227975.
KOiK09482.
OMAiMHGETGD.

Miscellaneous databases

EvolutionaryTraceiQ9V0T9.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
HAMAPiMF_00586. GatD.
InterProiIPR006033. AsnASEI.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR011878. GatD.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF500175. Glu_ADT_D. 1 hit.
PIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00519. asnASE_I. 1 hit.
TIGR02153. gatD_arch. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GE5 / Orsay.
  2. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
    Gao J., Wang J.
    Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: GE5 / Orsay.

Entry informationi

Entry nameiGATD_PYRAB
AccessioniPrimary (citable) accession number: Q9V0T9
Secondary accession number(s): G8ZJG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.