UniProt: A0A1C0AN86

Database: UniProt
Entry: A0A1C0AN86_9ACTN

LinkDB:  A0A1C0AN86_9ACTN 
Original site:  A0A1C0AN86_9ACTN

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Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (21)   

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ID   A0A1C0AN86_9ACTN        Unreviewed;       496 AA.
AC   A0A1C0AN86;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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   ECO:0000313|EMBL:VEP38770.1};
GN   ORFNames=BCR15_02820 {ECO:0000313|EMBL:OCL34642.1}, TLA_TLA_00242
GN   {ECO:0000313|EMBL:VEP38770.1};
OS   Tessaracoccus lapidicaptus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL34642.1, ECO:0000313|Proteomes:UP000093501};
RN   [1] {ECO:0000313|EMBL:OCL34642.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IPBSL-7 {ECO:0000313|EMBL:OCL34642.1};
RA   Puente-Sanchez F., Arce-Rodriguez A.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000093501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VEP38770.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TLA_E {ECO:0000313|EMBL:VEP38770.1};
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000516347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (JAN-2019) 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; MBQD01000020; OCL34642.1; -; Genomic_DNA.
DR   EMBL; LR214441; VEP38770.1; -; Genomic_DNA.
DR   RefSeq; WP_068751324.1; NZ_MBQD01000020.1.
DR   AlphaFoldDB; A0A1C0AN86; -.
DR   Proteomes; UP000093501; Unassembled WGS sequence.
DR   Proteomes; UP000516347; 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}; Reference proteome {ECO:0000313|Proteomes:UP000093501};
KW   Transferase {ECO:0000313|EMBL:OCL34642.1}.
FT   DOMAIN          348..495
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
FT   REGION          264..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  53515 MW;  79A92A27DD37B694 CRC64;
     MTETIPYDDL LTRYEPVLGL EVHVELNTNS KMFCGCPTTF GGDPNTQVCP VCLGLPGSLP
     VINGKAVESA IRIGLALNCR IAQWCRMARK NYFYPDMTKN FQTSQYDEPI AFDGWVDVEV
     DGETYRVEIE RAHMEEDAGK ALHMGGATGR IHGADYSLID YNRAGVPLIE IVTRPVRGAG
     AKAPEVARAY VAHLRDLLRA LGVSDVRMEQ GSLRCDANVS LMPIGSDVLG TRTETKNVNS
     LRSVERAIRY EMTRQAAILD GGARVKQETR HFHESDGTTS PGRSKEEAED YRYFAEPDLM
     PIAPSREWVE ELRATLPEPP AEHRRRLQTD WGFSDIDFGS IVSSGALGLV EATVAAGATP
     AAARKWWVTE LARRANEAGV ELDELPITPA QVAAVQGLVD AGKVNDKLAR QVIEGVLAGE
     GEPAAVVAAR GLAVVSDEGA LTVAVDEVIA ANPDVAAKIR DGKVAAAGAL IGQVMKAMKG
     QADAGKVREM ILAKLT
//

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