(data stored in ACNUC9435 zone)

HOGENOM: ETHAR1_1_PE1004

ID   ETHAR1_1_PE1004                      STANDARD;      PRT;   484 AA.
AC   ETHAR1_1_PE1004; E6U495;
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 1;
DE   Short=Glu-ADT subunit A 1; EC=6.3.5 -; (ETHAR1_1.PE1004).
GN   Name=gatA1; OrderedLocusNames=Ethha_1042;
OS   ETHANOLIGENENS HARBINENSE YUAN-3.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ethanoligenens.
OX   NCBI_TaxID=663278;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ETHAR1_1.PE1004.
CC       Ethanoligenens harbinense YUAN-3 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E6U495_ETHHY
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; E6U495; -.
DR   EMBL; CP002400; ADU26595.1; -; Genomic_DNA.
DR   RefSeq; YP_004091326.1; NC_014828.1.
DR   GeneID; 10092008; -.
DR   GenomeReviews; CP002400_GR; Ethha_1042.
DR   KEGG; eha:Ethha_1042; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; ETHAR1_1.PE1004; -.
KW   ATP-binding; Complete proteome; Hydrolase; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   484 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MELYENTASG LHTLFVEKKA SAVEIAEAHL ARIEAVDERV GAFLTVTKEE ALARAAEQDR
     KLAAGEPLGA LSGVPVAVKD NICTKGVRTT CASKMLHNFT PPYDATVADK LREAGAVMVG
     KTNMDEFAMG SSCETSHFKK THNPRDLECV PGGSSGGSAA AVAAGEVPLA LGSDTGGSIR
     QPAALCGVVG LKPTYGAVSR YGLVAFASSL DQIGPFARTA DDTALLLDAI KGRDTHDATS
     AHREQAPVAG TLDGNVKGLR IGIPQAYYGD GVDDAVKTQV LDTARALEQA GAALVDVSLS
     STRYALPTYY ILACAEASSN LARFDGVKYG YRTEHYDDLL SLYENSRSEG FGDEVKRRIM
     LGTFVLSSGY YDAYYHKAKL TQNLIRGEYD AAFGACDVIL TPTSPVTAFK IGERTADPLQ
     MYAADICTVP VNIAGLPAVS LPCGEVDGLP VGLQFIGRKF EERTILNAAK AVEQICGTAV
     PAAL
//

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