(data stored in ACNUC7421 zone)

HOGENOM: SPISS_1_PE1013

ID   SPISS_1_PE1013                       STANDARD;      PRT;   475 AA.
AC   SPISS_1_PE1013; E1RCU3;
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 -; (SPISS_1.PE1013).
GN   Name=gatB; OrderedLocusNames=Spirs_1040;
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.PE1013.
CC       Spirochaeta smaragdinae DSM 11293 chromosome, complete genome.
CC       nt) ;
CC   -!- ANNOTATIONS ORIGIN:E1RCU3_SPISS
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; E1RCU3; -.
DR   EMBL; CP002116; ADK80173.1; -; Genomic_DNA.
DR   RefSeq; YP_003802767.1; NC_014364.1.
DR   GeneID; 9489123; -.
DR   GenomeReviews; CP002116_GR; Spirs_1040.
DR   KEGG; ssm:Spirs_1040; -.
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; SPISS_1.PE1013; -.
KW   glutamyl-tRNA(Gln) amidotransferase, B subunit;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   475 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYDTFIGLEI HIQLLTKTKV FCGCSNNYGD EPNTNVCPVC LGYPGTLPIL NTDALFMAYQ
     VVGALKCKRA EAAIFERKNY FYPDMPKNYQ ISQFADPVGI NGEVIFPFQG EEHRVRIHDV
     HLEEDAGKMI HAGDMSLLDY NRAGTPLLEI VTEPDLRSGE ETEAFLRYFR TLVRTIGVSR
     GNMEEGNLRC DANISINTHG AGLGTKVELK NINSSRFVRL ALEYEKERQI GIVEAGGSVD
     QETRLWNENK DITVVMRRKE ESKDYRYFPE PDLPPYRPGE DFFRRVVESL PELPLDRQKR
     MEAAFSLTDE QASYLCEEKA RADYFETAVA AGTEAQHLYF WMSGDLAALV NKSGTPLEES
     RLSPEKLATV LRLLDNGEIH GPIAKKMVAL LFEEEHDPEG LIAERGWKAL DDTSKILPVV
     KRAVDANPSA AEQLKQGETK VLGFFMGQVM KETGGRADPE TAKALITSYV KGEIV
//

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