ID K4IN82_BIFAP Unreviewed; 500 AA.
AC K4IN82;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=BAST_1508 {ECO:0000313|EMBL:AFU72077.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU72077.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU72077.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU72077.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
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}.
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DR EMBL; CP003325; AFU72077.1; -; Genomic_DNA.
DR RefSeq; WP_015022513.1; NC_018720.1.
DR AlphaFoldDB; K4IN82; -.
DR STRING; 1147128.BAST_1508; -.
DR GeneID; 41010717; -.
DR KEGG; bast:BAST_1508; -.
DR PATRIC; fig|1147128.3.peg.1533; -.
DR eggNOG; COG0064; Bacteria.
DR HOGENOM; CLU_019240_0_0_11; -.
DR Proteomes; UP000007006; 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 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}; Transferase {ECO:0000313|EMBL:AFU72077.1}.
FT DOMAIN 350..497
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 500 AA; 54572 MW; 4DE55FFB17062527 CRC64;
MAEKLMKYAD AVAKYDPVFG LEVHVELCTN TKLFCPAHIE FGGEPNTQLT PVSLGLPGSL
PVVNKTAIDY AVKLGLALHC QINEWSQFAR KNYFYPDMPR DYQISQYDKP LNGEGYLDVE
LDDGSIFRVP IERAHVEDDA GKNTHVGGAD GRIEGADHSL VDYNRAGVPL VEIVTKPIEG
AGARTPEVAG AYVRAIRDIV RALGISHARM EQGNMRADVN VSLHAGPDAP LGTRSETKNV
NTFKGIEKTL TYEIRRQAAL LESGGEVLQE TRHWDESTQT TAGGRVKTDA NDYRYFPDPD
LVMVHVTKDH IEELKAQMPE MPRERRARLK KEWDFTDRQM QDAVNADAVD LIEDTVKAGA
TAAGARKWWL GEISREANAR GVSLQELPIS AQDVADVEQL IADGKLNDKL AKQTVSGVLA
GEGKPAEVVK KHGYQVVSDD GALDAAVDQA LKDNPDIVAK LKGGNMKPMG AIIGAVMRAT
KGQADAKAVS KIVMERIAKS
//
