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GATC_PICSI
ID   GATC_PICSI              Reviewed;         181 AA.
AC   A9P2J1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03149};
DE            Short=Glu-AdT subunit C {ECO:0000255|HAMAP-Rule:MF_03149};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149};
GN   Name=GATC {ECO:0000255|HAMAP-Rule:MF_03149};
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bark;
RX   PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA   Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA   Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA   Douglas C.J., Ritland K., Bohlmann J.;
RT   "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT   high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT   sitchensis).";
RL   BMC Genomics 9:484-484(2008).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts
CC       and mitochondria. The reaction takes place in the presence of glutamine
CC       and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_03149}.
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03149};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149}.
CC       Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_03149}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC       Rule:MF_03149}.
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DR   EMBL; EF087870; ABK27102.1; -; mRNA.
DR   AlphaFoldDB; A9P2J1; -.
DR   SMR; A9P2J1; -.
DR   OMA; FVCTKSP; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR003837; Asp/Glu-ADT_csu.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   PANTHER; PTHR15004; PTHR15004; 1.
DR   Pfam; PF02686; Glu-tRNAGln; 1.
DR   SUPFAM; SSF141000; SSF141000; 1.
DR   TIGRFAMs; TIGR00135; gatC; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW   Plastid; Protein biosynthesis.
FT   CHAIN           1..181
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000413320"
SQ   SEQUENCE   181 AA;  20336 MW;  6860C3093B0F59C7 CRC64;
     MIFLGPVLLT RGALSFFLTA GGSSVYRAWS WWLSGIHLFM AFSMSTSSLY KVGFGFVCTK
     SPCLRVSLIS RSQPWRFYSV HNNFEAPDVV QLAAKARISL TPKEVEDYGP KIGQVIDWFG
     QLQGVNLENV EPAIRADTDK LSNLRPDEPI IYEDREEMIA GVPTLEEPFI KVPKILKSSM
     E
 
 
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