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Database: UniProt
Entry: A0A1Q4WL74_9ACTN
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ID   A0A1Q4WL74_9ACTN        Unreviewed;        98 AA.
AC   A0A1Q4WL74;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            Short=Asp/Glu-ADT subunit C {ECO:0000256|HAMAP-Rule:MF_00122};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00122};
GN   Name=gatC {ECO:0000256|HAMAP-Rule:MF_00122};
GN   ORFNames=AMK13_06750 {ECO:0000313|EMBL:OKI10741.1};
OS   Streptomyces sp. CB02056.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI10741.1, ECO:0000313|Proteomes:UP000186379};
RN   [1] {ECO:0000313|EMBL:OKI10741.1, ECO:0000313|Proteomes:UP000186379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02056 {ECO:0000313|EMBL:OKI10741.1,
RC   ECO:0000313|Proteomes:UP000186379};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC       Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC       or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC       tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC       presence of glutamine and ATP through an activated phospho-Asp-
CC       tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|HAMAP-Rule:MF_00122}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00122};
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:0000256|HAMAP-Rule:MF_00122};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00122}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00122}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKI10741.1}.
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DR   EMBL; LIPD01000002; OKI10741.1; -; Genomic_DNA.
DR   RefSeq; WP_049657766.1; NZ_LIPD01000002.1.
DR   AlphaFoldDB; A0A1Q4WL74; -.
DR   OrthoDB; 5295223at2; -.
DR   Proteomes; UP000186379; Unassembled WGS sequence.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.20.60; Glu-tRNAGln amidotransferase C subunit, N-terminal domain; 1.
DR   HAMAP; MF_00122; GatC; 1.
DR   InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR   InterPro; IPR003837; GatC.
DR   NCBIfam; TIGR00135; gatC; 1.
DR   PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR   Pfam; PF02686; GatC; 1.
DR   SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186379};
KW   Transferase {ECO:0000313|EMBL:OKI10741.1}.
FT   REGION          70..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   98 AA;  10727 MW;  C297DBE22F804538 CRC64;
     MPGITREEVA HLARLSRLEL KPEELDHFAE QLDVIIGAVA RVSEVAGQDV PPTSHPLPLT
     NVMRADEVRP SLTPEQALSG APASEEQRFR VPQILGED
//
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