GATB_CAMC5
ID GATB_CAMC5 Reviewed; 474 AA.
AC A7GYS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121};
GN Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121};
GN OrderedLocusNames=Ccur92_10590; ORFNames=CCV52592_0791;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_00121};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00121}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00121}.
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DR EMBL; CP000767; EAT99933.1; -; Genomic_DNA.
DR RefSeq; WP_011992356.1; NC_009715.2.
DR AlphaFoldDB; A7GYS1; -.
DR SMR; A7GYS1; -.
DR STRING; 360105.CCV52592_0791; -.
DR EnsemblBacteria; EAT99933; EAT99933; CCV52592_0791.
DR KEGG; ccv:CCV52592_0791; -.
DR HOGENOM; CLU_019240_0_0_7; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 497127at2; -.
DR Proteomes; UP000006380; 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 Gene3D; 1.10.150.380; -; 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; 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 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..474
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_1000015951"
SQ SEQUENCE 474 AA; 53113 MW; DBA0A1C18B7458CE CRC64;
MFEVVIGLEV HTQLNTKTKI FCSCSTSFGD EANTHVCPTC LALPGALPVL NKEAVKKAIS
FGTAINAKIN KKSVFNRKNY FYPDLPKAYQ ISQFEIPIVE GGELIIDVNG EKKRIGITRA
HLEEDAGKNI HESDHSLVDL NRAGTPLLEI VSEPDLRSSD EAVAYLKKLH SILRFLNISD
ANMQEGSFRC DANVSIRPKG DSKLYTRVEI KNLNSFKFIQ KAIDYEVERQ SAAWEDGKYD
EEVYQETRLF DTTNLVTRSM RGKEDSAEYR YFPDPDLLPV LVDKAMYDEA IKIPELADEK
VVRYQKEFGV KEDDALNLVS TIEMSRYFED LVNSKISPKL CVTWLLVELN GRLKNGVTIE
TSPINSAKMI EFLKRIEDGT ISGKAGKEVL DYLMEHPSED VDAVIEKLGL KQVSDDSAIV
AIIDQILAAN ADKVAEYKAG KDKMFGFFVG QVMKEGKGAF NPAKVNELLK SRLA
