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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011By similarity
Active sitei177 – 1771By similarity
Active sitei178 – 1781By similarity
Active sitei254 – 2541By similarity

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.
MTHE187420:GJNM-708-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA(Gln) amidotransferase subunit DPRO_0000140056Add
BLAST

Interactioni

Subunit structurei

Heterodimer of GatD and GatE.

Protein-protein interaction databases

STRINGi187420.MTH706.

Structurei

Secondary structure

1
435
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Turni13 – 153Combined sources
Beta strandi21 – 255Combined sources
Beta strandi30 – 356Combined sources
Beta strandi44 – 507Combined sources
Beta strandi56 – 605Combined sources
Beta strandi68 – 703Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 998Combined sources
Turni108 – 1103Combined sources
Helixi121 – 1255Combined sources
Helixi127 – 1315Combined sources
Beta strandi134 – 1363Combined sources
Helixi145 – 1473Combined sources
Helixi150 – 16516Combined sources
Beta strandi169 – 1746Combined sources
Turni177 – 1793Combined sources
Helixi180 – 19011Combined sources
Beta strandi197 – 2004Combined sources
Helixi213 – 22513Combined sources
Beta strandi230 – 24213Combined sources
Beta strandi244 – 2485Combined sources
Helixi249 – 2513Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi304 – 3085Combined sources
Helixi315 – 3239Combined sources
Beta strandi327 – 3348Combined sources
Turni335 – 3373Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 3529Combined sources
Beta strandi357 – 3615Combined sources
Helixi374 – 3818Combined sources
Helixi392 – 40211Combined sources
Turni403 – 4053Combined sources
Helixi409 – 4179Combined sources
Beta strandi420 – 4223Combined sources
Helixi430 – 4323Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO26802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 419329Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

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

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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2D6FX-ray3.15A/B1-435[»]
ProteinModelPortaliO26802.
SMRiO26802. Positions 2-435.
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.
MTHE187420:GJNM-708-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO26802.

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: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / 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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

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: June 8, 2016
This is version 103 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.