GATA_COPC7
ID GATA_COPC7 Reviewed; 510 AA.
AC A8N8S3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=CC1G_00798;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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 {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; AACS02000007; EAU90414.1; -; Genomic_DNA.
DR RefSeq; XP_001831251.1; XM_001831199.1.
DR AlphaFoldDB; A8N8S3; -.
DR SMR; A8N8S3; -.
DR STRING; 5346.XP_001831251.1; -.
DR EnsemblFungi; EAU90414; EAU90414; CC1G_00798.
DR GeneID; 6007715; -.
DR KEGG; cci:CC1G_00798; -.
DR VEuPathDB; FungiDB:CC1G_00798; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; A8N8S3; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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: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;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..510
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000413352"
FT ACT_SITE 59
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 166
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 510 AA; 54575 MW; 4C7F126996055C44 CRC64;
MHGGLTKALR SSRLARRSVH SHALAAEANR ATNALVSLKF PDSPPAEKGP LSGLRIAVKD
NIVTRDFPTT CSSNVLKNFV SPFDATVVHR IRENGGQIIG KANCDEFGMG SLNTYTIHGP
VINPFPLSKV GLNNDKRSAG GSSGGSAAAV AADICDAALG TDTGGSIRLP ASYCGIVGLK
PSYGLVSRWG VVSYADSLDC VGVLARDVET TSCVFERISE YDPNDPTSAL PETREKADAL
SSQRLDELSS ALAEGSLHGL RIGIPQEFFP SELSNHVLNR FRQSVQLLKE RGAQIIPVSL
PSTSYSLSAY YVLASAEASS NMARYDGIQY GERIPTQDPS DLKKVSTVYA RTRSSTFGPE
VQRRILLGTY ALTADAFDNY FLQAQRVRQL IKDDFDRVFA MPNVRYAQPS NTPAQASQKV
DVLLHPSAIR SAPRLDEVET AASSLDAYVQ DVLTVPASLA GLPALSIPCP PSSSETEEVE
WPIGVSIVGQ WGSDHFVLAV GKFLESAASV
