ID   GATB_MYCPN              Reviewed;         477 AA.
AC   P75533;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE            Short=Asp/Glu-ADT subunit B;
DE            EC=6.3.5.-;
GN   Name=gatB; OrderedLocusNames=MPN_238; ORFNames=MP593;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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) (By similarity). {ECO:0000250}.
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   -!- 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   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB96241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U00089; AAB96241.1; ALT_INIT; Genomic_DNA.
DR   PIR; S73919; S73919.
DR   RefSeq; NP_109926.1; NC_000912.1.
DR   RefSeq; WP_014574916.1; NC_000912.1.
DR   AlphaFoldDB; P75533; -.
DR   SMR; P75533; -.
DR   STRING; 272634.MPN_238; -.
DR   EnsemblBacteria; AAB96241; AAB96241; MPN_238.
DR   GeneID; 66609116; -.
DR   KEGG; mpn:MPN_238; -.
DR   PATRIC; fig|272634.6.peg.257; -.
DR   HOGENOM; CLU_019240_0_1_14; -.
DR   OMA; QIYAYEN; -.
DR   Proteomes; UP000000808; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
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_amidoTrase-B-like.
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   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..477
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_0000148811"
SQ   SEQUENCE   477 AA;  54431 MW;  FAB5E8B5A9E60307 CRC64;
     MINFEAIIGI EVHVVLNTAT KMFSPAPNQA QNATPNQFIN AIDLGLPGTM PQVNEQAVQK
     ALILADALNM QRVQPVLVFD RKHYFYQDLP KGFQITQQNF PIAQNGYVEI VENNKAQRII
     IERFHLEEDT AKQHFVDGQI LLDFNRCGAP LIEVVTAPVI KSAKQSKAYL QKLRQILIVN
     NISNAKLEDG SMRSDCNVSV RLKGQTAFGT KVEIKNINSL NNVEKAIDLE IARQVKALIK
     GEPVQQVTLT YDDKTNTNVF MRKKDNSVDY RYFIEPNIMS SNIDELLQKP NKAFNLTEFF
     TKLKEAGVNE QLNQLVVDDL TLFNAYTKIN SVINSPQDTI RWLCIELMGQ LNKLQKPLKD
     KTIDHLIILI QMVQKGTVNQ KQAKQLIELM LDNGQDPQSL AKLHNLEQIT DEKQLTQIIQ
     QIFKENEGEI LKNLDRVERI QKLIIGQVMQ RTHNRANPQQ VFIIVEKLLH DFSERAS