GATA_SCHPO
ID GATA_SCHPO Reviewed; 471 AA.
AC O94509;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 118.
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};
GN ORFNames=SPBC646.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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).
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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 GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; CU329671; CAA22807.1; -; Genomic_DNA.
DR PIR; T40579; T40579.
DR RefSeq; NP_595361.1; NM_001021269.2.
DR AlphaFoldDB; O94509; -.
DR SMR; O94509; -.
DR STRING; 4896.SPBC646.03.1; -.
DR MaxQB; O94509; -.
DR PaxDb; O94509; -.
DR PRIDE; O94509; -.
DR EnsemblFungi; SPBC646.03.1; SPBC646.03.1:pep; SPBC646.03.
DR GeneID; 2541102; -.
DR KEGG; spo:SPBC646.03; -.
DR PomBase; SPBC646.03; -.
DR VEuPathDB; FungiDB:SPBC646.03; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; O94509; -.
DR OMA; TNPAAYN; -.
DR PhylomeDB; O94509; -.
DR PRO; PR:O94509; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; ISO:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; ISO:PomBase.
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 PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..471
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000001204"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 165
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 471 AA; 51684 MW; 8B652AB9DA655473 CRC64;
MSNKYNNLLK EVAAKYASII LNDAKIKSLT SINSAEYLYD SFVEISKLPL EKKLPLKWKL
ITVKENICTK TNLTTAASNM LKDYNSPFDA SIVESLKKAG GIILGKTNMD EFAMGVKSEN
NLFGRTVNPV VKDSNYDVGG SSGGAAAAIA ADICYASVGS DTGGSIRLPA AYVGCVGFKP
SFGRISRYGM LAFANSFDTV GIAANNVKGV TKVFNVLDHP DINDSTCLTK EARYFVKEQH
KKLSRKPIKI GIPIDWNVSE THPNVLDKWN EFISLLKSNG YLVQEIQLPI SLYANSVYST
MAYAEATSNL AKYNTIAFGN CLDEKFEEEI ISSTARSFFL GDEVKKRLLL GAYSLARMNS
SDLFSKARYV RRAIQLEFNK NFFLPSFSVD DPRGDIDFIV TPSFFNSSQP IETPSSYSHL
SDTMLVPANM AGIPSVSIPF GTLNNGLPMG IQIMAQYLND EDLLSFAGQF A
