(data stored in SCRATCH zone)

SWISSPROT: D1CDH6_THET1

ID   D1CDH6_THET1            Unreviewed;        98 AA.
AC   D1CDH6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 62.
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   OrderedLocusNames=Tter_0059 {ECO:0000313|EMBL:ACZ40982.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40982.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40982.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
CC       {ECO:0000256|HAMAP-Rule:MF_00122, ECO:0000256|SAAS:SAAS00770835}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2
CC         H(+) + 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         ECO:0000256|SAAS:SAAS01116079};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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         ECO:0000256|SAAS:SAAS01116074};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00122, ECO:0000256|SAAS:SAAS00770807}.
CC   -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00122, ECO:0000256|SAAS:SAAS00573107}.
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DR   EMBL; CP001825; ACZ40982.1; -; Genomic_DNA.
DR   RefSeq; WP_012874017.1; NC_013525.1.
DR   STRING; 525904.Tter_0059; -.
DR   EnsemblBacteria; ACZ40982; ACZ40982; Tter_0059.
DR   KEGG; ttr:Tter_0059; -.
DR   eggNOG; ENOG41081AP; Bacteria.
DR   eggNOG; COG0721; LUCA.
DR   HOGENOM; HOG000017523; -.
DR   KO; K02435; -.
DR   OMA; PATSHPI; -.
DR   OrthoDB; 1780195at2; -.
DR   BioCyc; TTER525904:G1GGS-59-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
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   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   3: Inferred from homology;
DR   PRODOM; D1CDH6.
DR   SWISS-2DPAGE; D1CDH6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00122,
KW   ECO:0000256|SAAS:SAAS00512394};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00122,
KW   ECO:0000256|SAAS:SAAS00512401};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00122,
KW   ECO:0000256|SAAS:SAAS00512395};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00122,
KW   ECO:0000256|SAAS:SAAS00512400};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000313|EMBL:ACZ40982.1}.
SQ   SEQUENCE   98 AA;  10895 MW;  FC3C843F729D4590 CRC64;
     MGLSSEQVLH ISRLARLGLT DAEVELFRDQ LSSIIEHVNK LSELDTEAIP PTAQVIELLD
     VFAKDEPSTS YSTDEMLANA PEKEENCFKV ITVLGYET
//

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