(data stored in ACNUC7421 zone)

HOGENOM: SPISS_1_PE1014

ID   SPISS_1_PE1014                       STANDARD;      PRT;   467 AA.
AC   SPISS_1_PE1014; E1RCU4;
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 -; (SPISS_1.PE1014).
GN   Name=gatA; OrderedLocusNames=Spirs_1041;
OS   SPIROCHAETA SMARAGDINAE DSM 11293.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=573413;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SPISS_1.PE1014.
CC       Spirochaeta smaragdinae DSM 11293 chromosome, complete genome.
CC       nt) ;
CC   -!- ANNOTATIONS ORIGIN:E1RCU4_SPISS
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; E1RCU4; -.
DR   EMBL; CP002116; ADK80174.1; -; Genomic_DNA.
DR   RefSeq; YP_003802768.1; NC_014364.1.
DR   GeneID; 9489124; -.
DR   GenomeReviews; CP002116_GR; Spirs_1041.
DR   KEGG; ssm:Spirs_1041; -.
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; SPISS_1.PE1014; -.
KW   glutamyl-tRNA(Gln) amidotransferase, A subunit;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   467 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDAALFGWS STAEYCTYLD ENDKKLGAFL SRTGAAEFQS ALERSRSEAS GQNPLRGMPF
     AVKDNIAVKG LPLSCGSKML DTLSSPYSAT AVEKLQQAGA VVVGKTNLDE FGMGSSCDNS
     ALGTTNNPWD VARVAGGSSG GSAAVVAAGM VPFALGSDTG GSIRQPAAFC GTYGLKPSYG
     VVSRFGLVAY ASSLETIGII SLDTQLLRIV FDTMRGQDPK DQSSRPFSPK ASEKRQGEKP
     RIGVIADIEG LAPAMESAYR ERLDLIRKKG YEIVEIELPM LEYVVPAYYT IASAEASANL
     ARYAGIRYGH RTDWADEHGE LTEKSRDEGF GDEVKLRILL GTYVLRSGFK DQYYLRAQKI
     RTLLRNEILS AFQKVDQILS PVFPTTAFPH GDAGLDQFQQ KLADKFTATA NLAAIPALAF
     PAGQSEGLPF GLQLLGPEFS EHKLIDTASA FTELWEPKTA PGFREWR
//

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