GATA_YEAST
ID GATA_YEAST Reviewed; 464 AA.
AC Q03557; D6W0C0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
DE AltName: Full=HMG2-induced ER-remodeling protein 2;
DE AltName: Full=Loss of respiratory capacity protein 6;
GN Name=HER2 {ECO:0000255|HAMAP-Rule:MF_03150}; Synonyms=GEP6, LRC6;
GN OrderedLocusNames=YMR293C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, INTERACTION WITH PET112 AND YGR102C, AND SUBCELLULAR LOCATION.
RX PubMed=19417106; DOI=10.1101/gad.518109;
RA Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.;
RT "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated
RT transamidation pathway involving Arc1p-controlled subcellular sorting of
RT cytosolic GluRS.";
RL Genes Dev. 23:1119-1130(2009).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP FUNCTION.
RX PubMed=18667535; DOI=10.1091/mbc.e07-11-1188;
RA Federovitch C.M., Jones Y.Z., Tong A.H., Boone C., Prinz W.A.,
RA Hampton R.Y.;
RT "Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum
RT remodeling in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 19:4506-4520(2008).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for
CC HMG2-induced ER-remodeling. {ECO:0000255|HAMAP-Rule:MF_03150,
CC ECO:0000269|PubMed:18667535, ECO:0000269|PubMed:19417106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatFAB amidotransferase (AdT)
CC complex, composed of A (HER2), B (PET112) and F (YGR102C) subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150,
CC ECO:0000269|PubMed:11914276, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:19417106}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; X80836; CAA56802.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10194.1; -; Genomic_DNA.
DR PIR; S47454; S47454.
DR RefSeq; NP_014021.1; NM_001182801.1.
DR PDB; 4N0H; X-ray; 1.95 A; A=1-464.
DR PDB; 4N0I; X-ray; 2.00 A; A=1-464.
DR PDBsum; 4N0H; -.
DR PDBsum; 4N0I; -.
DR AlphaFoldDB; Q03557; -.
DR SMR; Q03557; -.
DR BioGRID; 35473; 316.
DR ComplexPortal; CPX-416; Glutamyl-tRNA(Gln) amidotransferase complex.
DR DIP; DIP-2695N; -.
DR IntAct; Q03557; 7.
DR MINT; Q03557; -.
DR STRING; 4932.YMR293C; -.
DR CarbonylDB; Q03557; -.
DR MaxQB; Q03557; -.
DR PaxDb; Q03557; -.
DR PRIDE; Q03557; -.
DR EnsemblFungi; YMR293C_mRNA; YMR293C; YMR293C.
DR GeneID; 855338; -.
DR KEGG; sce:YMR293C; -.
DR SGD; S000004907; HER2.
DR VEuPathDB; FungiDB:YMR293C; -.
DR eggNOG; KOG1211; Eukaryota.
DR GeneTree; ENSGT00550000074866; -.
DR HOGENOM; CLU_009600_0_3_1; -.
DR InParanoid; Q03557; -.
DR OMA; EVSCPHF; -.
DR BioCyc; YEAST:G3O-32963-MON; -.
DR PRO; PR:Q03557; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03557; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IGI:SGD.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR Gene3D; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..464
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000001205"
FT ACT_SITE 52
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 154
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT HELIX 7..21
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 329..342
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 344..368
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:4N0I"
FT TURN 417..421
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:4N0H"
SQ SEQUENCE 464 AA; 50919 MW; BFFB6502451F283C CRC64;
MPLKRSLKES IERLSSFQSK YNIFTSINPS PYSITNKKGT KETLTGCVAS IKDNIVTKDF
PTTCASHILE NFKSPFDATV VKLLKQAGVH ILGKTNLDEF GMGSGGVHSI RGPVINPLYP
HEDKKIMGGS SSGAAASVAC DLVDFALGTD TGGSVRLPAC YGSVLGFKPS YGRLSRFGVI
AYSQSLDTVG ILSKKINVLR KVFHTLDKYD MKDPTSLSVE LRELIEGNKK VRRPLKVGIV
KEFSHESMPI GFHRLYLSLL EKLINLGLEI YPVSIPSVKN CLPIYYTLSP AEAASNLSRY
DGIRYGYRDS ELDIKDGILF APTRSKFGTE VKNRIILGNY NLCSDAFKNN FIKAEKLRVN
LIDEFDGIFR FPNVLTNSKG NPDGLDLLIV PTSSKLPGSI RDFEEEEAKS PANSYINDVF
TVPMSLAGLP SLSMPLKEKT PIGLQVVGQY GDDSTVLDFV ESIS
