UniProt: R9SPD6

Database: UniProt
Entry: R9SPD6_9EURY

LinkDB:  R9SPD6_9EURY 
Original site:  R9SPD6_9EURY

All links

Ontology (5)   
   GO (5)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (22)   

Download RDF

ID   R9SPD6_9EURY            Unreviewed;       450 AA.
AC   R9SPD6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000256|ARBA:ARBA00016923, ECO:0000256|HAMAP-Rule:MF_00121};
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   ECO:0000313|EMBL:AGN17473.1};
GN   ORFNames=Abm4_1609 {ECO:0000313|EMBL:AGN17473.1};
OS   Methanobrevibacter sp. AbM4.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=224719 {ECO:0000313|EMBL:AGN17473.1, ECO:0000313|Proteomes:UP000014066};
RN   [1] {ECO:0000313|EMBL:AGN17473.1, ECO:0000313|Proteomes:UP000014066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AbM4 {ECO:0000313|EMBL:AGN17473.1};
RA   Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA   Attwood G.T.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGN17473.1, ECO:0000313|Proteomes:UP000014066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abm4 {ECO:0000313|Proteomes:UP000014066};
RG   Pastoral Greenhouse Gas Research Consortium;
RA   Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA   Attwood G.T.;
RT   "The comlpete genome sequence of Methanobrevibacter sp. AbM4.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC       Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC       or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC       tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC       presence of glutamine and ATP through an activated phospho-Asp-
CC       tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|ARBA:ARBA00024799,
CC       ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000352, ECO:0000256|HAMAP-
CC         Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC         Rule:MF_00121};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC       {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_00121}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP004050; AGN17473.1; -; Genomic_DNA.
DR   RefSeq; WP_016359170.1; NC_021355.1.
DR   AlphaFoldDB; R9SPD6; -.
DR   STRING; 224719.Abm4_1609; -.
DR   GeneID; 15799099; -.
DR   KEGG; meb:Abm4_1609; -.
DR   eggNOG; arCOG01718; Archaea.
DR   HOGENOM; CLU_019240_0_1_2; -.
DR   OrthoDB; 52755at2157; -.
DR   Proteomes; UP000014066; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1.
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_amidoTrase-B-like.
DR   InterPro; IPR004413; GatB.
DR   InterPro; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   NCBIfam; TIGR00133; gatB; 1.
DR   PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR   PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00121};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00121};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00121};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00121}; Reference proteome {ECO:0000313|Proteomes:UP000014066};
KW   Transferase {ECO:0000313|EMBL:AGN17473.1}.
FT   DOMAIN          303..449
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   450 AA;  50915 MW;  90E935ACA65D6653 CRC64;
     MKCGLEIHVQ LETKSKLFCN CPTNYKEAPA NTNICPVCLN QPGAKPFPTN EKALENALMI
     SLMLNCKIEK GTAYFMRKHY DYPDLPSGYQ RTSIPIGYEG ELNGVRIREI HMEEDPGQYK
     PDKGVVDFNR SGIPLIEIVT EPDMHSPEEA RNFLNQLIRV LEYSGGARGE GTMRADVNVS
     IEGGNRVEMK NINSIKGAYK ALKFEVVRQK NLMKRGIEIK QETRAYLESQ MITVSMRSKE
     NADDYRFIPD PDLPPMKIYD NQIEEIKETM PEAPHNKARR FEEEYGLDKE TAKVLTSELD
     LADAFEEVAK EVDPVFAGNW MREELKRVLT YNKFDFTESG ISTADIVEII NLLQNKEITT
     KAGQRIVEQM PNNEKSPKEI GEELGLIGIV EEDAVVKAAK QAIDENPKAV NDYKEGQKNS
     INFLVGQVMR LTKGKADPGE TVKILKDLIE
//

DBGET integrated database retrieval system