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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit A

Gene

gatA

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 2 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) (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei72Charge relay systemBy similarity1
Active sitei147Charge relay systemBy similarity1
Active sitei171Acyl-ester intermediateBy similarity1

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 A (EC:6.3.5.7)
Short name:
Glu-ADT subunit A
Gene namesi
Name:gatA
Ordered Locus Names:aq_247
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001051331 – 478Glutamyl-tRNA(Gln) amidotransferase subunit AAdd BLAST478

Proteomic databases

PRIDEiO66610.

Interactioni

Subunit structurei

Heterotrimer of A, B and C subunits.By similarity

Protein-protein interaction databases

STRINGi224324.aq_247.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 15Combined sources9
Helixi21 – 39Combined sources19
Beta strandi42 – 45Combined sources4
Helixi47 – 55Combined sources9
Turni63 – 66Combined sources4
Beta strandi68 – 72Combined sources5
Helixi87 – 89Combined sources3
Helixi99 – 106Combined sources8
Beta strandi110 – 115Combined sources6
Helixi119 – 121Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi146 – 148Combined sources3
Helixi149 – 156Combined sources8
Beta strandi159 – 161Combined sources3
Beta strandi163 – 166Combined sources4
Beta strandi168 – 170Combined sources3
Helixi173 – 179Combined sources7
Beta strandi182 – 185Combined sources4
Turni201 – 203Combined sources3
Beta strandi206 – 212Combined sources7
Helixi213 – 223Combined sources11
Helixi241 – 244Combined sources4
Beta strandi253 – 257Combined sources5
Helixi258 – 262Combined sources5
Helixi267 – 282Combined sources16
Beta strandi286 – 290Combined sources5
Helixi295 – 297Combined sources3
Helixi298 – 313Combined sources16
Turni314 – 316Combined sources3
Beta strandi318 – 323Combined sources6
Helixi332 – 343Combined sources12
Helixi346 – 358Combined sources13
Turni361 – 367Combined sources7
Helixi368 – 385Combined sources18
Turni386 – 388Combined sources3
Beta strandi390 – 396Combined sources7
Beta strandi398 – 400Combined sources3
Turni404 – 407Combined sources4
Beta strandi408 – 410Combined sources3
Helixi411 – 415Combined sources5
Helixi416 – 418Combined sources3
Turni419 – 421Combined sources3
Helixi422 – 427Combined sources6
Beta strandi431 – 439Combined sources9
Beta strandi442 – 450Combined sources9
Helixi455 – 468Combined sources14
Helixi471 – 473Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H0LX-ray2.30A/D/G/J/M/P/S/V1-478[»]
3H0MX-ray2.80A/D/G/J/M/P/S/V1-478[»]
3H0RX-ray3.00A/D/G/J/M/P/S/V1-478[»]
ProteinModelPortaliO66610.
SMRiO66610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66610.

Family & Domainsi

Sequence similaritiesi

Belongs to the amidase family. GatA subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C3P. Bacteria.
COG0154. LUCA.
HOGENOMiHOG000116699.
InParanoidiO66610.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiPOG091H00O9.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
HAMAPiMF_00120. GatA. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR004412. GatA.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMiSSF75304. SSF75304. 1 hit.
TIGRFAMsiTIGR00132. gatA. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWKKSLSEL RELLKRGEVS PKEVVESFYD RYNQTEEKVK AYITPLYGKA
60 70 80 90 100
LKQAESLKER ELPLFGIPIA VKDNILVEGE KTTCASKILE NFVAPYDATV
110 120 130 140 150
IERLKKAGAL IVGKTNLDEF AMGSSTEYSA FFPTKNPWDL ERVPGGSSGG
160 170 180 190 200
SAASVAVLSA PVSLGSDTGG SIRQPASFCG VIGIKPTYGR VSRYGLVAFA
210 220 230 240 250
SSLDQIGVFG RRTEDVALVL EVISGWDEKD STSAKVPVPE WSEEVKKEVK
260 270 280 290 300
GLKIGLPKEF FEYELQPQVK EAFENFIKEL EKEGFEIKEV SLPHVKYSIP
310 320 330 340 350
TYYIIAPSEA SSNLARYDGV RYGYRAKEYK DIFEMYARTR DEGFGPEVKR
360 370 380 390 400
RIMLGTFALS AGYYDAYYLK AQKVRRLITN DFLKAFEEVD VIASPTTPTL
410 420 430 440 450
PFKFGERLEN PIEMYLSDIL TVPANLAGLP AISIPIAWKD GLPVGGQLIG
460 470
KHWDETTLLQ ISYLWEQKFK HYEKIPLT
Length:478
Mass (Da):53,524
Last modified:August 1, 1998 - v1
Checksum:i72EE383259D606E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06569.1.
PIRiF70322.
RefSeqiNP_213170.1. NC_000918.1.
WP_010880108.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06569; AAC06569; aq_247.
GeneIDi1192844.
KEGGiaae:aq_247.
PATRICi20958124. VBIAquAeo85532_0202.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06569.1.
PIRiF70322.
RefSeqiNP_213170.1. NC_000918.1.
WP_010880108.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H0LX-ray2.30A/D/G/J/M/P/S/V1-478[»]
3H0MX-ray2.80A/D/G/J/M/P/S/V1-478[»]
3H0RX-ray3.00A/D/G/J/M/P/S/V1-478[»]
ProteinModelPortaliO66610.
SMRiO66610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_247.

Proteomic databases

PRIDEiO66610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06569; AAC06569; aq_247.
GeneIDi1192844.
KEGGiaae:aq_247.
PATRICi20958124. VBIAquAeo85532_0202.

Phylogenomic databases

eggNOGiENOG4105C3P. Bacteria.
COG0154. LUCA.
HOGENOMiHOG000116699.
InParanoidiO66610.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiPOG091H00O9.

Miscellaneous databases

EvolutionaryTraceiO66610.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
HAMAPiMF_00120. GatA. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR004412. GatA.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMiSSF75304. SSF75304. 1 hit.
TIGRFAMsiTIGR00132. gatA. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGATA_AQUAE
AccessioniPrimary (citable) accession number: O66610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 93 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.