(data stored in ACNUC2780 zone)

HOGENOM: DICT6_1_PE1001

ID   DICT6_1_PE1001                       STANDARD;      PRT;   483 AA.
AC   DICT6_1_PE1001; B5YED0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE   Short=Glu-ADT subunit A; EC=6.3.5 -; (DICT6_1.PE1001).
GN   Name=gatA; OrderedLocusNames=DICTH_1039;
OS   DICTYOGLOMUS THERMOPHILUM H-6-12.
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICT6_1.PE1001.
CC       Dictyoglomus thermophilum H-6-12, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B5YED0_DICT6
CC   -!- FUNCTION: Furnishes a means for formation of correctly charged
CC       Gln-tRNA(Gln) through the transamidation of misacylated Glu-
CC       tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The
CC       reaction takes place in the presence of glutamine and ATP through
CC       an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the amidase family.
CC   -!- GENE_FAMILY: HOG000116699 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B5YED0; -.
DR   EMBL; CP001146; ACI18903.1; -; Genomic_DNA.
DR   RefSeq; YP_002250888.1; NC_011297.1.
DR   STRING; B5YED0; -.
DR   GeneID; 6945115; -.
DR   GenomeReviews; CP001146_GR; DICTH_1039.
DR   KEGG; dth:DICTH_1039; -.
DR   OMA; TESSCYG; -.
DR   ProtClustDB; PRK00012; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00120; GatA; 1; -.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR004412; GatA.
DR   Gene3D; G3DSA:3.90.1300.10; Amidase_sig_enz; 1.
DR   PANTHER; PTHR11895; Amidase; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase_sig_enz; 1.
DR   TIGRFAMs; TIGR00132; GatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
DR   HOGENOMDNA; DICT6_1.PE1001; -.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   483 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRTLREIKKI YENKEANVKE VVESYLEKIK EWEPYINAFL HIPYEDIEKQ VKELESKSPN
     LPLYGIPIAI KDNILTKNIK TTCASKILEN FIPPYDATVV KRLKENGAII IGKTNLDEFA
     MGSSCENSAF GPTKNPWDIE RVPGGSSGGS AACVSAGEVP VSLGSDTGGS IRLPASFTGV
     IGLKPTYGLV SRFGLVAFAS SLDQIGPFGR TVEDIAITLQ IIAGHDPMDS TSSPYEIPNY
     LEGLGKSVKN WRVGIPKELW YKGVSEEVLK TLENSFDVFK EMGVTIEEIS LPSLEYALPV
     YYIISTSEAS SNLARYDGVK YGYRDFTAED IISMYKQTRG KGFGSEVKRR IILGTYALSA
     GYYDAYYLKA TKVRRLIRME FEEAFKKVDI IASPTSPVLP FKLGERISDP LQMYLTDIMT
     IPVNLAGIPA ISMPAGFYNN LPVGIQFMSS FFTEDKLLQF AYAYQQFVDF SKKYPTLPNK
     ERV
//

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