ID A0A0N7LS87_9RHOB Unreviewed; 502 AA.
AC A0A0N7LS87;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {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:CUH52932.1};
GN ORFNames=SHM7688_02379 {ECO:0000313|EMBL:CUH52932.1};
OS Shimia marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH52932.1, ECO:0000313|Proteomes:UP000054823};
RN [1] {ECO:0000313|EMBL:CUH52932.1, ECO:0000313|Proteomes:UP000054823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH52932.1,
RC ECO:0000313|Proteomes:UP000054823};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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: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; CYPW01000024; CUH52932.1; -; Genomic_DNA.
DR RefSeq; WP_058240112.1; NZ_FOMU01000003.1.
DR AlphaFoldDB; A0A0N7LS87; -.
DR STRING; 321267.SHM7688_02379; -.
DR OrthoDB; 9804078at2; -.
DR Proteomes; UP000054823; 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 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 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:UP000054823};
KW Transferase {ECO:0000313|EMBL:CUH52932.1}.
FT DOMAIN 356..500
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 502 AA; 55433 MW; F9000E551D3B054D CRC64;
MLDLTYETPK PKVIAGAKHD WELVIGMEVH AQVSSNAKLF SGASTAFGAE PNSNVAFVDS
AMPGMLPVIN EYCVEQAVRT GLGLNAEIHL KSAFDRKNYF YPDLPQGYQI SQLYEPIVGE
GEILVDMGPG VARLVRVERI HLEQDAGKSV HDMDPNMSFV DLNRTGVALM EIVSRPDIRG
PEEAAAYVTK MRQILRYLGT CDGNMQNGNL RADVNVSICR PGQYEKYMET QDFSHLGTRC
EIKNMNSMRF IQAAIEYEAR RQIAIVEAGG TVDQETRLYD PDKNETRSMR SKEEAHDYRY
FPDPDLLPLE IEQGWVDDIA KTLPELPDQK KSRFIKDYGV TEYDASVLTA EVDLADYFEA
SVGKGDGKKT ANWVINEVLG RANKAEVRPQ ELVAPEANAA ILAMVASDEI STKIAKDVLE
IHIETKDDPA KIVEEKGLKQ VTDTGAIEAA LDEIIAANPA QVEKAKQNPK LAGWFVGQVM
KATGGKANPK AVNQLVAQKL NG
//
