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Protein

Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial

Gene

HER2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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 the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for HMG2-induced ER-remodeling.UniRule annotation2 Publications

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 sitei52 – 521Charge relay systemUniRule annotation
Active sitei130 – 1301Charge relay systemUniRule annotation
Active sitei154 – 1541Acyl-ester intermediateUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Source: SGD

GO - Biological processi

  • endoplasmic reticulum organization Source: SGD
  • glutaminyl-tRNAGln biosynthesis via transamidation Source: SGD
  • mitochondrial translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32963-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrialUniRule annotation (EC:6.3.5.7UniRule annotation)
Short name:
Glu-AdT subunit AUniRule annotation
Alternative name(s):
HMG2-induced ER-remodeling protein 2
Loss of respiratory capacity protein 6
Gene namesi
Name:HER2UniRule annotation
Synonyms:GEP6, LRC6
Ordered Locus Names:YMR293C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR293C.
SGDiS000004907. HER2.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of mitochondrial inner membrane Source: SGD
  • glutamyl-tRNA(Gln) amidotransferase complex Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrialPRO_0000001205Add
BLAST

Proteomic databases

MaxQBiQ03557.

Interactioni

Subunit structurei

Subunit of the heterotrimeric GatFAB amidotransferase (AdT) complex, composed of A (HER2), B (PET112) and F (YGR102C) subunits.

Protein-protein interaction databases

BioGridi35473. 303 interactions.
DIPiDIP-2695N.
IntActiQ03557. 7 interactions.
MINTiMINT-540456.

Structurei

Secondary structure

1
464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2115Combined sources
Beta strandi24 – 274Combined sources
Turni43 – 464Combined sources
Beta strandi48 – 525Combined sources
Beta strandi58 – 603Combined sources
Helixi67 – 693Combined sources
Helixi79 – 868Combined sources
Beta strandi90 – 956Combined sources
Helixi99 – 1013Combined sources
Beta strandi104 – 1063Combined sources
Helixi121 – 1233Combined sources
Beta strandi129 – 1313Combined sources
Helixi132 – 1398Combined sources
Beta strandi142 – 15312Combined sources
Helixi156 – 1616Combined sources
Beta strandi164 – 1685Combined sources
Turni184 – 1863Combined sources
Beta strandi188 – 1947Combined sources
Helixi196 – 20611Combined sources
Helixi219 – 2279Combined sources
Beta strandi236 – 2405Combined sources
Helixi241 – 2433Combined sources
Helixi252 – 26514Combined sources
Beta strandi269 – 2746Combined sources
Helixi276 – 2805Combined sources
Helixi281 – 29616Combined sources
Turni297 – 2993Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi313 – 3153Combined sources
Helixi321 – 3244Combined sources
Helixi329 – 34214Combined sources
Helixi344 – 36825Combined sources
Beta strandi369 – 3713Combined sources
Turni374 – 3774Combined sources
Beta strandi384 – 3929Combined sources
Helixi400 – 4078Combined sources
Helixi411 – 4155Combined sources
Turni417 – 4215Combined sources
Helixi422 – 4265Combined sources
Beta strandi431 – 4377Combined sources
Beta strandi443 – 4475Combined sources
Helixi453 – 46210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N0HX-ray1.95A1-464[»]
4N0IX-ray2.00A1-464[»]
ProteinModelPortaliQ03557.
SMRiQ03557. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the amidase family. GatA subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074866.
HOGENOMiHOG000116699.
InParanoidiQ03557.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiEOG7P8PJ3.

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.

Q03557-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLKRSLKES IERLSSFQSK YNIFTSINPS PYSITNKKGT KETLTGCVAS
60 70 80 90 100
IKDNIVTKDF PTTCASHILE NFKSPFDATV VKLLKQAGVH ILGKTNLDEF
110 120 130 140 150
GMGSGGVHSI RGPVINPLYP HEDKKIMGGS SSGAAASVAC DLVDFALGTD
160 170 180 190 200
TGGSVRLPAC YGSVLGFKPS YGRLSRFGVI AYSQSLDTVG ILSKKINVLR
210 220 230 240 250
KVFHTLDKYD MKDPTSLSVE LRELIEGNKK VRRPLKVGIV KEFSHESMPI
260 270 280 290 300
GFHRLYLSLL EKLINLGLEI YPVSIPSVKN CLPIYYTLSP AEAASNLSRY
310 320 330 340 350
DGIRYGYRDS ELDIKDGILF APTRSKFGTE VKNRIILGNY NLCSDAFKNN
360 370 380 390 400
FIKAEKLRVN LIDEFDGIFR FPNVLTNSKG NPDGLDLLIV PTSSKLPGSI
410 420 430 440 450
RDFEEEEAKS PANSYINDVF TVPMSLAGLP SLSMPLKEKT PIGLQVVGQY
460
GDDSTVLDFV ESIS
Length:464
Mass (Da):50,919
Last modified:November 1, 1997 - v1
Checksum:iBFFB6502451F283C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80836 Genomic DNA. Translation: CAA56802.1.
BK006946 Genomic DNA. Translation: DAA10194.1.
PIRiS47454.
RefSeqiNP_014021.1. NM_001182801.1.

Genome annotation databases

EnsemblFungiiYMR293C; YMR293C; YMR293C.
GeneIDi855338.
KEGGisce:YMR293C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80836 Genomic DNA. Translation: CAA56802.1.
BK006946 Genomic DNA. Translation: DAA10194.1.
PIRiS47454.
RefSeqiNP_014021.1. NM_001182801.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N0HX-ray1.95A1-464[»]
4N0IX-ray2.00A1-464[»]
ProteinModelPortaliQ03557.
SMRiQ03557. Positions 6-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35473. 303 interactions.
DIPiDIP-2695N.
IntActiQ03557. 7 interactions.
MINTiMINT-540456.

Proteomic databases

MaxQBiQ03557.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR293C; YMR293C; YMR293C.
GeneIDi855338.
KEGGisce:YMR293C.

Organism-specific databases

EuPathDBiFungiDB:YMR293C.
SGDiS000004907. HER2.

Phylogenomic databases

GeneTreeiENSGT00550000074866.
HOGENOMiHOG000116699.
InParanoidiQ03557.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiEOG7P8PJ3.

Enzyme and pathway databases

BioCyciYEAST:G3O-32963-MONOMER.

Miscellaneous databases

PROiQ03557.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS."
    Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.
    Genes Dev. 23:1119-1130(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PET112 AND YGR102C, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. "Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum remodeling in Saccharomyces cerevisiae."
    Federovitch C.M., Jones Y.Z., Tong A.H., Boone C., Prinz W.A., Hampton R.Y.
    Mol. Biol. Cell 19:4506-4520(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGATA_YEAST
AccessioniPrimary (citable) accession number: Q03557
Secondary accession number(s): D6W0C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 486 molecules/cell in log phase SD medium.1 Publication

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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.