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Database: UniProt
Entry: U5E678_NOCAS
LinkDB: U5E678_NOCAS
Original site: U5E678_NOCAS 
ID   U5E678_NOCAS            Unreviewed;       501 AA.
AC   U5E678;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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:GAD81818.1};
GN   ORFNames=NCAST_05_02540 {ECO:0000313|EMBL:GAD81818.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD81818.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD81818.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD81818.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD81818.1}.
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DR   EMBL; BAFO02000005; GAD81818.1; -; Genomic_DNA.
DR   RefSeq; WP_022565549.1; NZ_VBUS01000001.1.
DR   AlphaFoldDB; U5E678; -.
DR   STRING; 1824.SAMN05444423_10743; -.
DR   eggNOG; COG0064; Bacteria.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000017048; Unassembled WGS sequence.
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   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; 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:UP000017048};
KW   Transferase {ECO:0000313|EMBL:GAD81818.1}.
FT   DOMAIN          353..500
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   501 AA;  54046 MW;  A3C8C44FB3A69673 CRC64;
     MSAPTVELMD YADVISRYEP VLGMEVHVEL STATKMFCGC PTEFGAEPNT QVCPVCLGLP
     GSLPVVNEQA VESAIRIGLA LNCSITPWGR FARKNYFYPD QPKNYQISQY DEPIATEGYL
     DVVLDDGSTF RVDIERAHME EDTGKSLHVG GATGRIHGAS HSLLDFNRAG VPLIEIVTKP
     ITGAGARAPE VARAYVTALR EVLRSLNVSD VKMEQGSLRC DANVSLMPVG AKEFGTRTET
     KNVNSLKSVE VAVRYEMRRQ AAVLTEGGEI VQETRHFNEA DGSTSAGRRK ETAEDYRYFP
     EPDLEPVAPA AERIEELRAT IPEYPWLVRA RIQADWGLSD EVMRDLVNAG ALDLIIATVD
     AGAPANEARS WWVAYLTEKA KEREVALADL PITPAQVAAV IALVEAKTVN NKVAKQVVDF
     VLAGEGEPAA IVEAKGLGMV SDDSALQAEV DKALAANPDI AEKIRSGKVQ AAGKIVGDVM
     KATRGQADAA KVRELVLAAC A
//
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