ID GATB_BACSU Reviewed; 476 AA.
AC O30509; O31499; O50554;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 24-JAN-2024, entry version 136.
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; Synonyms=yerN; OrderedLocusNames=BSU06690;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=168;
RX PubMed=9342321; DOI=10.1073/pnas.94.22.11819;
RA Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W.,
RA Henkin T.M., Soell D.;
RT "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for
RT correct decoding of glutamine codons during translation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hong K.-W., Martins O.M., Kim S.-I., Soell D.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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).
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.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000305}.
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DR EMBL; U49788; AAB87634.1; -; Genomic_DNA.
DR EMBL; AF008553; AAB83965.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12489.2; -; Genomic_DNA.
DR PIR; T51583; T51583.
DR RefSeq; NP_388551.2; NC_000964.3.
DR AlphaFoldDB; O30509; -.
DR SMR; O30509; -.
DR IntAct; O30509; 1.
DR MINT; O30509; -.
DR STRING; 224308.BSU06690; -.
DR jPOST; O30509; -.
DR PaxDb; 224308-BSU06690; -.
DR DNASU; 936057; -.
DR EnsemblBacteria; CAB12489; CAB12489; BSU_06690.
DR GeneID; 936057; -.
DR KEGG; bsu:BSU06690; -.
DR PATRIC; fig|224308.43.peg.706; -.
DR eggNOG; COG0064; Bacteria.
DR InParanoid; O30509; -.
DR OrthoDB; 9804078at2; -.
DR BioCyc; BSUB:BSU06690-MONOMER; -.
DR BioCyc; MetaCyc:MONOMER-13956; -.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..476
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148762"
FT CONFLICT 27..28
FT /note="TP -> PN (in Ref. 2; AAB87634)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="G -> A (in Ref. 2; AAB87634)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..241
FT /note="FF -> GV (in Ref. 3; CAB12489)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..311
FT /note="FA -> LP (in Ref. 3; CAB12489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53553 MW; 095B056BF4B44676 CRC64;
MNFETVIGLE VHVELKTKSK IFSSSPTPFG AEANTQTSVI DLGYPGVLPV LNKEAVEFAM
KAAMALNCEI ATDTKFDRKN YFYPDNPKAY QISQFDKPIG ENGWIEIEVG GKTKRIGITR
LHLEEDAGKL THTGDGYSLV DFNRQGTPLV EIVSEPDIRT PEEAYAYLEK LKSIIQYTGV
SDCKMEEGSL RCDANISLRP IGQEEFGTKT ELKNLNSFAF VQKGLEHEEK RQEQVLLSGF
FIQQETRRYD EATKKTILMR VKEGSDDYRY FPEPDLVELY IDDEWKERVK ASIPELPDER
RKRYIEELGF AAYDAMVLTL TKEMADFFEE TVQKGAEAKQ ASNWLMGEVS AYLNAEQKEL
ADVALTPEGL AGMIKLIEKG TISSKIAKKV FKELIEKGGD AEKIVKEKGL VQISDEGVLL
KLVTEALDNN PQSIEDFKNG KDRAIGFLVG QIMKASKGQA NPPMVNKILL EEIKKR
//
