(data stored in SCRATCH zone)

SWISSPROT: D1CDH5_THET1

ID   D1CDH5_THET1            Unreviewed;       494 AA.
AC   D1CDH5;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 69.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120};
GN   OrderedLocusNames=Tter_0058 {ECO:0000313|EMBL:ACZ40981.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40981.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40981.1, 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 Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in
CC       organisms which lack glutaminyl-tRNA synthetase. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
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         EC=6.3.5.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00120,
CC         ECO:0000256|SAAS:SAAS01115610};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00120, ECO:0000256|SAAS:SAAS00598568}.
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DR   EMBL; CP001825; ACZ40981.1; -; Genomic_DNA.
DR   RefSeq; WP_012874016.1; NC_013525.1.
DR   STRING; 525904.Tter_0058; -.
DR   EnsemblBacteria; ACZ40981; ACZ40981; Tter_0058.
DR   KEGG; ttr:Tter_0058; -.
DR   eggNOG; ENOG4105C3P; Bacteria.
DR   eggNOG; COG0154; LUCA.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   OrthoDB; 1239251at2; -.
DR   BioCyc; TTER525904:G1GGS-58-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P: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;
DR   PRODOM; D1CDH5.
DR   SWISS-2DPAGE; D1CDH5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013898};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Hydrolase {ECO:0000313|EMBL:ACZ40981.1};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013917};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013943};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013924};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000313|EMBL:ACZ40981.1}.
FT   DOMAIN       30    471       Amidase. {ECO:0000259|Pfam:PF01425}.
FT   ACT_SITE     84     84       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    159    159       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    183    183       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00120}.
SQ   SEQUENCE   494 AA;  53501 MW;  395759CE91F85006 CRC64;
     MKHRDNRDLV DLSIRELRKL LDNKHVSSVE LTEAYLRRIE QVDPQIRSYL TVTADLALQQ
     AQEADKKLAS GEKSPLLGIP MALKDIISTK GIKTTCGSKM LENYIPPYDA TVYEKLCAAG
     CVLLGKLNMD EFAMGSSTEN SAYGPTKNPW DLTTVPGGSS GGSASAVAAG EAAFTLGSDT
     GGSVRQPAAL CGVVGLKPTY GRVSRYGLVA FASSLDQIGP ITRTVEDLAD VLQVIAGYDP
     KDSTSVPIDV PQYGDALSED IRGIRIGVPK EYFVEGMEPG VERAVREAID KLGSLGAKIV
     DISLPSTDYA LATYYIIAPA EASSNLSRYT GVEYGHRAPD AEDIIDMYMK TREEGFGPEV
     KRRIMLGTYV LSAGYYDAYY LKAQKVRTII KSEFDAAFKE CDVIATPTSP TVAFKLGSKL
     QDPLSMYLSD LFTIPANMAG IPGLSIPCGF SDDLPVGLQL LGKAFDESTL LKVGYAYQQS
     TEWHLKRPQI LAYL
//

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