(data stored in ACNUC7421 zone)

HOGENOM: LACRG_1_PE1001

ID   LACRG_1_PE1001                       STANDARD;      PRT;   476 AA.
AC   LACRG_1_PE1001; C7TBC2; C8UT01;
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   Short=Asp/Glu-ADT subunit B; EC=6.3.5 -; (LACRG_1.PE1001).
GN   Name=gatB; OrderedLocusNames=LGG_01020, LRHM_0978;
OS   LACTOBACILLUS RHAMNOSUS GG.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
OX   NCBI_TaxID=568703;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LACRG_1.PE1001.
CC       Lactobacillus rhamnosus GG, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C7TBC2_LACRG
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; C7TBC2; C8UT01; -.
DR   EMBL; AP011548; BAI41505.1; -; Genomic_DNA.
DR   EMBL; FM179322; CAR86915.1; -; Genomic_DNA.
DR   RefSeq; YP_003170766.1; NC_013198.1.
DR   ProteinModelPortal; C7TBC2; -.
DR   STRING; C7TBC2; -.
DR   GeneID; 8422168; -.
DR   GenomeReviews; AP011548_GR; LRHM_0978.
DR   GenomeReviews; FM179322_GR; LGG_01020.
DR   KEGG; lrh:LGG_01020; -.
DR   OMA; KNYFYAD; -.
DR   ProtClustDB; PRK05477; -.
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; LACRG_1.PE1001; -.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   476 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNFETTIGLE VHVELKTKSK MFSPAPVTYG QEPNTETNVI DWGFPGVLPS INRGAYQLGI
     MLALALHADI TRQTHFDRKN YFYPDNPKAY QITQSEKPLG TNGWVEIEVG GKKKKVGIAE
     LHVEEDAGKN QHEDDGYSYV DLNRQGTPLV EIVSKPDITS PEEAYAYLET LRQIVQFTGA
     SDVKMEEGSM RVDTNLSVRP IGQKHFGTKT EIKNLNSFVH VRDGLAYEEK RQQAVLLSGG
     EVRQETRRWD PDTKETILMR VKEGADDYRY FPEPDLPPVT VSQQWIDEVQ ATLPQPPAER
     REHYIKDWGI PAYDAGVLTQ TKEMSDFFEA TVAQGADAKQ ASNWLMGEVS GYLNAKHTEL
     GDVALTPEHL AGMIKLIGDG TISSKMAKKV FKEIIQHDTD PDQWVHEKGL IQLSDPAKLT
     PIITTVLDNN QQSIDDFKAG KDRAIGFLVG QIMKQTHGQA NPKVVNQILM TEIKKR
//

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