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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit D

Gene

gatD

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei101By similarity1
Active sitei177By similarity1
Active sitei178By similarity1
Active sitei254By 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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14998.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit D (EC:6.3.5.-)
Short name:
Glu-ADT subunit D
Gene namesi
Name:gatD
Ordered Locus Names:MTH_706
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001400561 – 435Glutamyl-tRNA(Gln) amidotransferase subunit DAdd BLAST435

Interactioni

Subunit structurei

Heterodimer of GatD and GatE.

Protein-protein interaction databases

STRINGi187420.MTH706.

Structurei

Secondary structure

1435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 12Combined sources8
Turni13 – 15Combined sources3
Beta strandi21 – 25Combined sources5
Beta strandi30 – 35Combined sources6
Beta strandi44 – 50Combined sources7
Beta strandi56 – 60Combined sources5
Beta strandi68 – 70Combined sources3
Beta strandi88 – 90Combined sources3
Beta strandi92 – 99Combined sources8
Turni108 – 110Combined sources3
Helixi121 – 125Combined sources5
Helixi127 – 131Combined sources5
Beta strandi134 – 136Combined sources3
Helixi145 – 147Combined sources3
Helixi150 – 165Combined sources16
Beta strandi169 – 174Combined sources6
Turni177 – 179Combined sources3
Helixi180 – 190Combined sources11
Beta strandi197 – 200Combined sources4
Helixi213 – 225Combined sources13
Beta strandi230 – 242Combined sources13
Beta strandi244 – 248Combined sources5
Helixi249 – 251Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi256 – 258Combined sources3
Beta strandi263 – 268Combined sources6
Beta strandi271 – 275Combined sources5
Beta strandi304 – 308Combined sources5
Helixi315 – 323Combined sources9
Beta strandi327 – 334Combined sources8
Turni335 – 337Combined sources3
Helixi341 – 343Combined sources3
Helixi344 – 352Combined sources9
Beta strandi357 – 361Combined sources5
Helixi374 – 381Combined sources8
Helixi392 – 402Combined sources11
Turni403 – 405Combined sources3
Helixi409 – 417Combined sources9
Beta strandi420 – 422Combined sources3
Helixi430 – 432Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D6FX-ray3.15A/B1-435[»]
ProteinModelPortaliO26802.
SMRiO26802.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO26802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 419Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST329

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

CDDicd08962. GatD. 1 hit.
Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
HAMAPiMF_00586. GatD. 1 hit.
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.

O26802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYQGRARKF LESASIDVGD MVLVEKPDVT YEGMVLDRAD DADDRHIVLK
60 70 80 90 100
LENGYNIGVE ISDARIELLE KGSEPRIELP PVEAAEDPEL PDVSIISTGG
110 120 130 140 150
TVASIIDYRT GAVHPAFTAD DLLRANPELL DIANIRGRAV FNILSENMKP
160 170 180 190 200
EYWVETARAV YGEIKDGADG VVVAHGTDTM HYTSAALSFM LRTPVPVVFT
210 220 230 240 250
GAQRSSDRPS SDASLNIQCS VRAATSEIAE VTVCMHATMD DLSCHLHRGV
260 270 280 290 300
KVRKMHTSRR DTFRSMNALP LAEVTPDGIK ILEENYRKRG SDELELSDRV
310 320 330 340 350
EERVAFIKSY PGISPDIIKW HLDEGYRGIV IEGTGLGHCP DTLIPVIGEA
360 370 380 390 400
HDMGVPVAMT SQCLNGRVNM NVYSTGRRLL QAGVIPCDDM LPEVAYVKMC
410 420 430
WVLGQTDDPE MAREMMRENI AGEINERTSI AYFRG
Length:435
Mass (Da):47,997
Last modified:January 1, 1998 - v1
Checksum:i34D8E4205486126F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85211.1.
PIRiC69194.
RefSeqiWP_010876345.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85211; AAB85211; MTH_706.
GeneIDi1470667.
KEGGimth:MTH_706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85211.1.
PIRiC69194.
RefSeqiWP_010876345.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D6FX-ray3.15A/B1-435[»]
ProteinModelPortaliO26802.
SMRiO26802.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH706.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85211; AAB85211; MTH_706.
GeneIDi1470667.
KEGGimth:MTH_706.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14998.

Miscellaneous databases

EvolutionaryTraceiO26802.

Family and domain databases

CDDicd08962. GatD. 1 hit.
Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
HAMAPiMF_00586. GatD. 1 hit.
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...

Entry informationi

Entry nameiGATD_METTH
AccessioniPrimary (citable) accession number: O26802
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 106 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.