Q03557 (GATA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
Short name=Glu-AdT subunit A
EC=6.3.5.-

Alternative name(s):
HMG2-induced ER-remodeling protein 2
Loss of respiratory capacity protein 6

Gene names

Name:	HER2
Synonyms:	GEP6, LRC6
Ordered Locus Names:	YMR293C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.8
Catalytic activity	ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
Subunit structure	Subunit of the heterotrimeric GatFAB amidotransferase(AdT) complex, composed of A (HER2), B (PET112) and F (YGR102C) subunits.
Subcellular location	Mitochondrion Ref.3 Ref.4 Ref.6 Ref.7.
Miscellaneous	Present with 486 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the amidase family. GatA subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endoplasmic reticulum organization Inferred from genetic interaction Ref.8. Source: SGD glutaminyl-tRNAGln biosynthesis via transamidation Inferred from direct assay Ref.6. Source: SGD translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glutamyl-tRNA(Gln) amidotransferase complex Inferred from direct assay Ref.6. Source: SGD mitochondrion Inferred from direct assay Ref.3Ref.4Ref.7Ref.6. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 464	464	Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial		PRO_0000001205
Sites
	Active site	52	1	Charge relay system By similarity
	Active site	130	1	Charge relay system By similarity
	Active site	154	1	Acyl-ester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03557 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: BFFB6502451F283C	FASTA	464	50,919
	10 20 30 40 50 60 MPLKRSLKES IERLSSFQSK YNIFTSINPS PYSITNKKGT KETLTGCVAS IKDNIVTKDF 70 80 90 100 110 120 PTTCASHILE NFKSPFDATV VKLLKQAGVH ILGKTNLDEF GMGSGGVHSI RGPVINPLYP 130 140 150 160 170 180 HEDKKIMGGS SSGAAASVAC DLVDFALGTD TGGSVRLPAC YGSVLGFKPS YGRLSRFGVI 190 200 210 220 230 240 AYSQSLDTVG ILSKKINVLR KVFHTLDKYD MKDPTSLSVE LRELIEGNKK VRRPLKVGIV 250 260 270 280 290 300 KEFSHESMPI GFHRLYLSLL EKLINLGLEI YPVSIPSVKN CLPIYYTLSP AEAASNLSRY 310 320 330 340 350 360 DGIRYGYRDS ELDIKDGILF APTRSKFGTE VKNRIILGNY NLCSDAFKNN FIKAEKLRVN 370 380 390 400 410 420 LIDEFDGIFR FPNVLTNSKG NPDGLDLLIV PTSSKLPGSI RDFEEEEAKS PANSYINDVF 430 440 450 460 TVPMSLAGLP SLSMPLKEKT PIGLQVVGQY GDDSTVLDFV ESIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Subcellular localization of the yeast proteome." Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P., Gerstein M., Roeder G.S., Snyder M. Genes Dev. 16:707-719(2002) [PubMed: 11914276] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] 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: 19417106] [Abstract] Cited for: FUNCTION, INTERACTION WITH PET112 AND YGR102C, SUBCELLULAR LOCATION.
[7]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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: 18667535] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80836 Genomic DNA. Translation: CAA56802.1. BK006946 Genomic DNA. Translation: DAA10194.1.
PIR	S47454.
RefSeq	NP_014021.1. NM_001182801.1.
3D structure databases
ProteinModelPortal	Q03557.
SMR	Q03557. Positions 1-463.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2695N.
IntAct	Q03557. 7 interactions.
MINT	MINT-540456.
STRING	Q03557.
Proteomic databases
PeptideAtlas	Q03557.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR293C; YMR293C; YMR293C.
GeneID	855338.
KEGG	sce:YMR293C.
NMPDR	fig|4932.3.peg.5079.
Organism-specific databases
CYGD	YMR293c.
SGD	S000004907. HER2.
Phylogenomic databases
eggNOG	fuNOG05801.
GeneTree	EFGT00050000001234.
HOGENOM	HBG481888.
OMA	TESSCYG.
OrthoDB	EOG4MKRR3.
Gene expression databases
ArrayExpress	Q03557.
Genevestigator	Q03557.
GermOnline	YMR293C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000120. Amidase. IPR020556. Amidase_CS. IPR023631. Amidase_dom. IPR004412. GatA. [Graphical view]
Gene3D	G3DSA:3.90.1300.10. Amidase_sig_enz. 1 hit.
KO	K02433.
PANTHER	PTHR11895. Amidase. 1 hit.
Pfam	PF01425. Amidase. 1 hit. [Graphical view]
SUPFAM	SSF75304. Amidase_sig_enz. 1 hit.
TIGRFAMs	TIGR00132. GatA. 1 hit.
PROSITE	PS00571. AMIDASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979073.

Entry information

Entry name

GATA_YEAST

Accession

Primary (citable) accession number: Q03557
Secondary accession number(s): D6W0C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program