GenomeNet

Database: UniProt
Entry: F7PNB6_9EURY
LinkDB: F7PNB6_9EURY
Original site: F7PNB6_9EURY 
ID   F7PNB6_9EURY            Unreviewed;       495 AA.
AC   F7PNB6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:ERJ05067.1};
GN   ORFNames=HLRTI_002939 {ECO:0000313|EMBL:ERJ05067.1}, HTIA_2481
GN   {ECO:0000313|EMBL:CCQ34589.1};
OS   Halorhabdus tiamatea SARL4B.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ05067.1, ECO:0000313|Proteomes:UP000003861};
RN   [1] {ECO:0000313|EMBL:ERJ05067.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05067.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=21705593; DOI=10.1128/JB.05462-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT   a deep-sea anoxic brine lake.";
RL   J. Bacteriol. 193:4553-4554(2011).
RN   [2] {ECO:0000313|EMBL:ERJ05067.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05067.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
RN   [3] {ECO:0000313|EMBL:CCQ34589.1, ECO:0000313|Proteomes:UP000015381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC   SARL4B {ECO:0000313|EMBL:CCQ34589.1};
RX   PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA   Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA   Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA   Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA   Golyshin P.N., Teeling H.;
RT   "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT   identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT   lake as potential polysaccharide degrader.";
RL   Environ. Microbiol. 16:2525-2537(2014).
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; HF571520; CCQ34589.1; -; Genomic_DNA.
DR   EMBL; AFNT02000045; ERJ05067.1; -; Genomic_DNA.
DR   RefSeq; WP_008527512.1; NZ_AFNT02000045.1.
DR   STRING; 1033806.HTIA_2481; -.
DR   GeneID; 23798977; -.
DR   KEGG; hti:HTIA_2481; -.
DR   PATRIC; fig|1033806.12.peg.2469; -.
DR   eggNOG; arCOG01718; Archaea.
DR   HOGENOM; CLU_019240_0_0_2; -.
DR   OrthoDB; 52755at2157; -.
DR   Proteomes; UP000003861; Unassembled WGS sequence.
DR   Proteomes; UP000015381; Chromosome.
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}; Transferase {ECO:0000313|EMBL:ERJ05067.1}.
FT   DOMAIN          347..493
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   495 AA;  54898 MW;  49D5C8CE0B38C4BD CRC64;
     MTAQAIQERD LAVVIGLEVH VQLETATKIF CGCSTDLEDA EPNTHTCPVC LGLPGSLPVL
     NEGAVEAAVR VGKAIDADIP EQTRFHRKNY YYPDLPKNFQ ISQYDAPICQ DGELEFSVEG
     ERRTVGIERA HLEEDPGSLQ HAGGNIDTAD YTLVDYNRAG VPLMEVVTEP DFRDASEVRA
     FLAKLEEVLE YLGVFDATRD GSLRIDANLS LVDASEVGDR GEIDDAVLAD ANRTEVKNIS
     SHKGAEKALA YEAQRQKNAV ERGREVEQET RHWDESRGIT VSMRSKEEEK DYRYFREADL
     PPLEVSHWKA ELSIPELPDA RRERFGEEYG LDEEAASKLT TTKQVADFYE DLAAEFDPDL
     VATWVADELL GELNYRDMAI TDVTDRFDEI ERLVELVATE EITAKNARET VLRGMLDDGT
     DPDTVVEREG LGKTGGDELQ SAVEEAIEEN PDAVDDYHEG EGGAINFLVG QVMQKTGGSA
     DPGDVNQLLR AELEE
//
DBGET integrated database retrieval system