(data stored in ACNUC9435 zone)

HOGENOM: ETHAR1_1_PE1005

ID   ETHAR1_1_PE1005                      STANDARD;      PRT;   478 AA.
AC   ETHAR1_1_PE1005; E6U496;
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=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
DE   1; Short=Asp/Glu-ADT subunit B 1; EC=6.3.5 -; (ETHAR1_1.PE1005).
GN   Name=gatB1; OrderedLocusNames=Ethha_1043;
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.PE1005.
CC       Ethanoligenens harbinense YUAN-3 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E6U496_ETHHY
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC       + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
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 gatB/gatE family. GatB subfamily.
CC   -!- GENE_FAMILY: HOG000223742 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E6U496; -.
DR   EMBL; CP002400; ADU26596.1; -; Genomic_DNA.
DR   RefSeq; YP_004091327.1; NC_014828.1.
DR   ProteinModelPortal; E6U496; -.
DR   GeneID; 10092009; -.
DR   GenomeReviews; CP002400_GR; Ethha_1043.
DR   KEGG; eha:Ethha_1043; -.
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_00121; GatB; 1; -.
DR   InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR   InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel.
DR   InterPro; IPR004413; Gln-tRNA_amidoTrfase_bsu.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   PANTHER; PTHR11659; GatB; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB_Yqey; 1.
DR   TIGRFAMs; TIGR00133; GatB; 1.
DR   PROSITE; PS01234; GATB; 1.
DR   HOGENOMDNA; ETHAR1_1.PE1005; -.
KW   glutamyl-tRNA(Gln) amidotransferase, B subunit;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   478 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEYEIVVGLE VHAELSTKSK IYCSCKNAFG AEVNTECCPV CTGLPGALPV LNEKVVESAV
     RMGYALGCTI NPVSKQDRKN YFYPDLPKAY QISQFDIPLC EHGYVDVLVD GEEKRIGVTR
     IHIEEDAGKL LHGDSFSGTL VDFNRCGVPL IEIVSEPDMR SAAEAKAYME TLRDILLALD
     VSDCKMQEGS MRADVNVSVR PKDSTTFGTR VEMKNVNSFS AAAHAIEYES KRQIEVLENG
     GVIEQETRRW DDTQGKNFVM RSKEDAQDYR YFPEPDLGVI VLDEDYLASL KESIPELPNK
     RRVRYMNDYG LPEFDAGLLA LDPERTAFFE AALAVGGAAP KALANWLIGD VARLLADKNQ
     VLSQTSLTPE ALVKLTALIE KGTISNTAGK AVLEELFANG GDPEAVVREK GLAQVSDTAA
     LEAIVKDVLA QNEKSVVDYK KGKTNAAGYL VGQCMRASKG KANPQIVREL VQNALDEA
//

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