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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit A

Gene

gatA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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).

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 sitei79 – 791Charge relay systemBy similarity
Active sitei154 – 1541Charge relay systemBy similarity
Active sitei178 – 1781Acyl-ester intermediateBy 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

BioCyciBSUB:BSU06680-MONOMER.
MetaCyc:MONOMER-13955.

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
Synonyms:yedB, yerM
Ordered Locus Names:BSU06680
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamyl-tRNA(Gln) amidotransferase subunit APRO_0000105138Add
BLAST

Proteomic databases

PaxDbiO06491.

Interactioni

Subunit structurei

Heterotrimer of A, B and C subunits.

Protein-protein interaction databases

IntActiO06491. 1 interaction.
MINTiMINT-8365300.
STRINGi224308.Bsubs1_010100003773.

Structurei

3D structure databases

ProteinModelPortaliO06491.
SMRiO06491. Positions 1-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the amidase family. GatA subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C3P. Bacteria.
COG0154. LUCA.
HOGENOMiHOG000116699.
InParanoidiO06491.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiEOG61P6R9.
PhylomeDBiO06491.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
HAMAPiMF_00120. GatA.
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.

O06491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFDHKITE LKQLIHKKEI KISDLVDESY KRIQAVDDKV QAFLALDEER
60 70 80 90 100
ARAYAKELDE AVDGRSEHGL LFGMPIGVKD NIVTKGLRTT CSSKILENFD
110 120 130 140 150
PIYDATVVQR LQDAEAVTIG KLNMDEFAMG SSTENSAYKL TKNPWNLDTV
160 170 180 190 200
PGGSSGGSAA AVAAGEVPFS LGSDTGGSIR QPASFCGVVG LKPTYGRVSR
210 220 230 240 250
YGLVAFASSL DQIGPITRTV EDNAFLLQAI SGVDKMDSTS ANVDVPDFLS
260 270 280 290 300
SLTGDIKGLK IAVPKEYLGE GVGKEARESV LAALKVLEGL GATWEEVSLP
310 320 330 340 350
HSKYALATYY LLSSSEASAN LARFDGIRYG YRTDNADNLI DLYKQTRAEG
360 370 380 390 400
FGNEVKRRIM LGTFALSSGY YDAYYKKAQK VRTLIKKDFE DVFEKYDVIV
410 420 430 440 450
GPTTPTPAFK IGENTKDPLT MYANDILTIP VNLAGVPGIS VPCGLADGLP
460 470 480
LGLQIIGKHF DESTVYRVAH AFEQATDHHK AKPEL
Length:485
Mass (Da):52,664
Last modified:May 30, 2000 - v3
Checksum:iFD4BDDAE54E09DCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti435 – 44410GVPGISVPCG → AYRESGAMR in AAB83964 (PubMed:9342321).Curated
Sequence conflicti463 – 48523STVYR…AKPEL → ALYTALLMHLNKQQTIIKQN LNCKG in AAB83964 (PubMed:9342321).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008553 Genomic DNA. Translation: AAB83964.1.
AL009126 Genomic DNA. Translation: CAB12488.1.
AF011545 Genomic DNA. Translation: AAB72184.1.
U92466 Genomic DNA. Translation: AAB66513.1.
PIRiB69795.
T44452.
T51582.
RefSeqiNP_388550.1. NC_000964.3.
WP_003242878.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12488; CAB12488; BSU06680.
GeneIDi11238570.
938748.
KEGGibsu:BSU06680.
PATRICi18972982. VBIBacSub10457_0705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008553 Genomic DNA. Translation: AAB83964.1.
AL009126 Genomic DNA. Translation: CAB12488.1.
AF011545 Genomic DNA. Translation: AAB72184.1.
U92466 Genomic DNA. Translation: AAB66513.1.
PIRiB69795.
T44452.
T51582.
RefSeqiNP_388550.1. NC_000964.3.
WP_003242878.1. NZ_JNCM01000032.1.

3D structure databases

ProteinModelPortaliO06491.
SMRiO06491. Positions 1-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO06491. 1 interaction.
MINTiMINT-8365300.
STRINGi224308.Bsubs1_010100003773.

Proteomic databases

PaxDbiO06491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12488; CAB12488; BSU06680.
GeneIDi11238570.
938748.
KEGGibsu:BSU06680.
PATRICi18972982. VBIBacSub10457_0705.

Phylogenomic databases

eggNOGiENOG4105C3P. Bacteria.
COG0154. LUCA.
HOGENOMiHOG000116699.
InParanoidiO06491.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiEOG61P6R9.
PhylomeDBiO06491.

Enzyme and pathway databases

BioCyciBSUB:BSU06680-MONOMER.
MetaCyc:MONOMER-13955.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
HAMAPiMF_00120. GatA.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
    Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W., Henkin T.M., Soell D.
    Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a region devoted to purine uptake and metabolism, and containing the genes cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide sequence."
    Borriss R., Porwollik S., Schroeter R.
    Microbiology 142:3027-3031(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-256.
    Strain: 168.
  4. "Osmostress response in Bacillus subtilis: characterization of a proline uptake system (OpuE) regulated by high osmolarity and the alternative transcription factor sigma B."
    von Blohn C., Kempf B., Kappes R.M., Bremer E.
    Mol. Microbiol. 25:175-187(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
    Strain: 168 / JH642.

Entry informationi

Entry nameiGATA_BACSU
AccessioniPrimary (citable) accession number: O06491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: February 17, 2016
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.