(data stored in ACNUC8465 zone)

SWISSPROT: C5DD85_LACTC

ID   C5DD85_LACTC            Unreviewed;       465 AA.
AC   C5DD85;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 62.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03150};
DE            Short=Glu-AdT subunit A {ECO:0000256|HAMAP-Rule:MF_03150};
DE            EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_03150};
GN   Name=HER2 {ECO:0000256|HAMAP-Rule:MF_03150};
GN   OrderedLocusNames=KLTH0B09152g {ECO:0000313|EMBL:CAR21746.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21746.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21746.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_03150};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatFAB amidotransferase (AdT)
CC       complex, composed of A, B and F subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_03150}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03150}.
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DR   EMBL; CU928166; CAR21746.1; -; Genomic_DNA.
DR   RefSeq; XP_002552184.1; XM_002552138.1.
DR   STRING; 381046.XP_002552184.1; -.
DR   EnsemblFungi; CAR21746; CAR21746; KLTH0B09152g.
DR   GeneID; 8291027; -.
DR   KEGG; lth:KLTH0B09152g; -.
DR   HOGENOM; HOG000116699; -.
DR   InParanoid; C5DD85; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   OrthoDB; 1195292at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; C5DD85.
DR   SWISS-2DPAGE; C5DD85.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03150};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03150};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03150};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03150};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN          12..458
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        54
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT   ACT_SITE        131
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT   ACT_SITE        155
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   465 AA;  50391 MW;  6B43B7B447111384 CRC64;
     MSFKSAISRL EKLPLIQKQY NAFTHLNPNC KELLIKDVSS SPKKSLTNLL YGIKDNIATS
     DMPTSCGSKV LHNYQSPFDA TIVELLESAG AISVGKTNLD EFGMGSGGLF SHFGPTKNPL
     FPFQDTVVGG SSSGSAAAVA ADAVDFSIGT DTGGSVRLPA AYTSLFGFKP SYGRISRFGV
     IAYAQSMDTV GIFSKNVSII KSVFDVLDKH DKKDPTSLSE NLRGKLRQLS SPQSSYKIGI
     PQELLQDNMP LELQDGFLLA LEKLEANGHE IYGVSIPQMV NSLPIYYTLA PAEAASNLAR
     FDGLRYGYRD DVADSRDDTL FAPTRSAFGD EVKSRIVLGN YNLCSESFNN HYIKAQRLRV
     DLINEFDNTF THPNILTGFP GNQNGVDFLI SFSSINLPPA MSDYDSDCTS NPTNSYVNDV
     FTTPMSLAGL PAINVPVMAS NPIGIQLVGQ YGDDSRLLDL AAELL
//

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