Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei52Charge relay systemUniRule annotation1
Active sitei130Charge relay systemUniRule annotation1
Active sitei154Acyl-ester intermediateUniRule annotation1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000012051 – 464Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrialAdd BLAST464

Proteomic databases

MaxQBiQ03557.
PRIDEiQ03557.

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 interactors.
DIPiDIP-2695N.
IntActiQ03557. 7 interactors.
MINTiMINT-540456.

Structurei

Secondary structure

1464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 21Combined sources15
Beta strandi24 – 27Combined sources4
Turni43 – 46Combined sources4
Beta strandi48 – 52Combined sources5
Beta strandi58 – 60Combined sources3
Helixi67 – 69Combined sources3
Helixi79 – 86Combined sources8
Beta strandi90 – 95Combined sources6
Helixi99 – 101Combined sources3
Beta strandi104 – 106Combined sources3
Helixi121 – 123Combined sources3
Beta strandi129 – 131Combined sources3
Helixi132 – 139Combined sources8
Beta strandi142 – 153Combined sources12
Helixi156 – 161Combined sources6
Beta strandi164 – 168Combined sources5
Turni184 – 186Combined sources3
Beta strandi188 – 194Combined sources7
Helixi196 – 206Combined sources11
Helixi219 – 227Combined sources9
Beta strandi236 – 240Combined sources5
Helixi241 – 243Combined sources3
Helixi252 – 265Combined sources14
Beta strandi269 – 274Combined sources6
Helixi276 – 280Combined sources5
Helixi281 – 296Combined sources16
Turni297 – 299Combined sources3
Beta strandi301 – 306Combined sources6
Beta strandi313 – 315Combined sources3
Helixi321 – 324Combined sources4
Helixi329 – 342Combined sources14
Helixi344 – 368Combined sources25
Beta strandi369 – 371Combined sources3
Turni374 – 377Combined sources4
Beta strandi384 – 392Combined sources9
Helixi400 – 407Combined sources8
Helixi411 – 415Combined sources5
Turni417 – 421Combined sources5
Helixi422 – 426Combined sources5
Beta strandi431 – 437Combined sources7
Beta strandi443 – 447Combined sources5
Helixi453 – 462Combined sources10

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the amidase family. GatA subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074866.
HOGENOMiHOG000116699.
InParanoidiQ03557.
KOiK02433.
OMAiKEYFGAG.
OrthoDBiEOG092C2W6G.

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4N0HX-ray1.95A1-464[»]
4N0IX-ray2.00A1-464[»]
ProteinModelPortaliQ03557.
SMRiQ03557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiQ03557.
PRIDEiQ03557.

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.
OrthoDBiEOG092C2W6G.

Enzyme and pathway databases

BioCyciYEAST:G3O-32963-MONOMER.

Miscellaneous databases

PROiQ03557.

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_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: November 2, 2016
This is version 131 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.