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Database: UniProt/TrEMBL
Entry: F8GLK7_NITSI
LinkDB: F8GLK7_NITSI
Original site: F8GLK7_NITSI 
ID   F8GLK7_NITSI            Unreviewed;       479 AA.
AC   F8GLK7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   26-NOV-2014, entry version 21.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000256|HAMAP-Rule:MF_00121, ECO:0000256|SAAS:SAAS00081059};
DE            Short=Asp/Glu-ADT subunit B {ECO:0000256|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000256|HAMAP-Rule:MF_00121};
GN   OrderedLocusNames=Nit79A3_0883 {ECO:0000313|EMBL:AEJ00753.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ00753.1, ECO:0000313|Proteomes:UP000000501};
RN   [1] {ECO:0000313|EMBL:AEJ00753.1, ECO:0000313|Proteomes:UP000000501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ00753.1,
RC   ECO:0000313|Proteomes:UP000000501};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A.,
RA   Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D.,
RA   Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000256|HAMAP-Rule:MF_00121, ECO:0000256|SAAS:SAAS00081060}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC       + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00121, ECO:0000256|SAAS:SAAS00081063}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00121, ECO:0000256|SAAS:SAAS00081067}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00121}.
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DR   EMBL; CP002876; AEJ00753.1; -; Genomic_DNA.
DR   RefSeq; WP_013965048.1; NC_015731.1.
DR   RefSeq; YP_004694152.1; NC_015731.1.
DR   EnsemblBacteria; AEJ00753; AEJ00753; Nit79A3_0883.
DR   GeneID; 10932972; -.
DR   KEGG; nii:Nit79A3_0883; -.
DR   KO; K02434; -.
DR   BioCyc; NSP261292:GH7H-901-MONOMER; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.410; -; 1.
DR   HAMAP; MF_00121; GatB; 1.
DR   InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; IPR023168; GatB_Yqey_C.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000501};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00121};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00121};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000501};
KW   Transferase {ECO:0000313|EMBL:AEJ00753.1}.
SQ   SEQUENCE   479 AA;  52765 MW;  5F05C223BB0AB9B6 CRC64;
     MQWEIVIGLE VHAQLSTQSK IFSGSSTAYG AAPNTQASVI DLALPGVLPV LNKGAVERAI
     KLGLSVGAKI NSPSIFARKN YFYPDLPKGY QISQYELPVV QGGNIQIQID GIEKNVRLTR
     AHLEEDAGKS LHEDFHGMSG IDLNRAGTPL LEIVSEPDMR SSAEAVAYAK TLHALVRWIG
     ICDGNMQEGS FRCDANVSVR PRGTEKLGTR CEIKNLNSFR FLEKAIDYEA RRQIEILEDG
     GAIRQETRLY DANKDETRTM RTKEDANDYR YFPDPDLLPL EIPQSWIDQI KQTLPELPQA
     RRDRYISEFA LSAYDASVLT SSREMADYFD ATLKQLPAQA KLCANWIMGE ISGQLNKEGI
     EMTACPITPA QLAALLARIS DGTISGKAAK TVFESMWNGE LDKNVDAIIE AKGLKQISDD
     GAIEKLVDQV LAANAQQVAD YRNGKEKAFN SLIGQIMKAT QGKANPAQVN AMLKKKLDG
//
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