(data stored in SCRATCH zone)

HOGENOM: THEEB_1_PE1003

ID   THEEB_1_PE1003                       STANDARD;      PRT;   496 AA.
AC   THEEB_1_PE1003; Q8DK65;
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 -; (THEEB_1.PE1003).
GN   Name=gatA; OrderedLocusNames=tll1003;
OS   THERMOSYNECHOCOCCUS ELONGATUS BP-1.
OC   Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEEB_1.PE1003.
CC       Thermosynechococcus elongatus BP-1, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:GATA_THEEB
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAC08555.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000116699 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8DK65; -.
DR   EMBL; BA000039; BAC08555.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_681793.1; NC_004113.1.
DR   ProteinModelPortal; Q8DK65; -.
DR   SMR; Q8DK65; 3-482.
DR   STRING; Q8DK65; -.
DR   GeneID; 1011319; -.
DR   GenomeReviews; BA000039_GR; tll1003.
DR   KEGG; tel:tll1003; -.
DR   NMPDR; fig|197221.1.peg.1002; -.
DR   eggNOG; COG0154; -.
DR   OMA; FDEETLF; -.
DR   ProtClustDB; PRK00012; -.
DR   BioCyc; TELO197221:TLL1003-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; THEEB_1.PE1003; -.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
SQ   SEQUENCE   496 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLYCYSIVIG EAAFMSVIQE LHRQLVRKER SATEITQAYL DRIAQVEPTL HSFLTVTRDR
     ALAQAAEVDK RLAAGEEIGL LTGIPLAIKD NLCTYGVRTT CASKMLEHFV PPYESTVTEK
     LQAAGAIMVG KTNLDEFAMG SSTENSAFGF TANPWNPERV SGGSSGGSAA AVAARECAAA
     LGSDTGGSIR QPAAFCGVVG LKPTYGLVSR YGLVAYASSL DQIGPLAPTV TDAAILLGAI
     AGHDPKDATS LRVPIPDYTQ ALKPDLKGMR IGLIQETVGE GVQPEVKSAL EAALKTLEAL
     GATLVELSCP RFAYGLPTYY IIAPSEASAN LARYDGVNFG FRAEGASDLL EMYMKTRAQG
     FGAEVKRRIM IGTYALSAGY YDAYYLRAQK VRTLIKEDFA RAFEQVDVLI CPTAPTTAFK
     AGEKTADPLS MYLSDLMTIP VNLAGLPGLS VPCGFDSNGL PIGLQLIGNV LQEATLFHVA
     YAYEQTTPWH QQQPQL
//

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