(data stored in SCRATCH zone)

SWISSPROT: A2Q7C3_ASPNC

ID   A2Q7C3_ASPNC            Unreviewed;       504 AA.
AC   A2Q7C3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 78.
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   ORFNames=An01g00130 {ECO:0000313|EMBL:CAK36864.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36864.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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 GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C 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; AM269949; CAK36864.1; -; Genomic_DNA.
DR   RefSeq; XP_001388465.1; XM_001388428.1.
DR   PaxDb; A2Q7C3; -.
DR   EnsemblFungi; CAK36864; CAK36864; An01g00130.
DR   GeneID; 4977151; -.
DR   KEGG; ang:ANI_1_2064014; -.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7C3.
DR   SWISS-2DPAGE; A2Q7C3.
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}.
FT   DOMAIN          16..493
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT   ACT_SITE        164
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   504 AA;  53328 MW;  B27A51C0B6540865 CRC64;
     MSLLREAEKC LANQGSHAAL NALITTLHQS GQWLERVRDA DARRTRGTPK SEIDGRLVAV
     KDNMCTRDLP TTCASNALDK FVSPFNATVV QQLEDAGAVV AGKANLDEFG MGSHSIHSNF
     GPVRSSRRGQ DAEYLSAGGS SGGSAVAVAT AQCYAALGTD TGGSVRLPAA YTGTVGFKPS
     YGLVSRWGVV AYANSLDTVG VLGRDVASVR HVFGVVNQHD SRDPTNLSPS SRSRIDSHLK
     MSALASRTSS PLRIGVPLEY NISELSPSAR HAWSRSLAYL QRQGHSIQTV SLPTTKLALS
     AYYVLAPAEA SSNLAKYDGV RYGSRPEAPD GNASSERYLY AKTRGDGFGS EVKRRILLGA
     FSLSADAMDN YFIQAQRVRR LVQHDFNAAF RACQPLISSQ LGSKSGSADT GVDVLICPTA
     PSSPPRISSL IGPDATTSPL EAYTNDVFTV PASLAGLPAI SVPVTTENAD GAEDGDLAGI
     QVIGQYGDDE LVLKVAELLE GRHL
//

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