UniProt: V2QDJ9

Database: UniProt
Entry: V2QDJ9_9BACT

LinkDB:  V2QDJ9_9BACT 
Original site:  V2QDJ9_9BACT

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Ontology (5)   
   GO (5)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   V2QDJ9_9BACT            Unreviewed;       488 AA.
AC   V2QDJ9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
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:USF23808.1};
GN   ORFNames=N508_000875 {ECO:0000313|EMBL:USF23808.1}, N508_00336
GN   {ECO:0000313|EMBL:ESJ99041.1};
OS   Mucispirillum schaedleri ASF457.
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Mucispirillaceae; Mucispirillum.
OX   NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ99041.1};
RN   [1] {ECO:0000313|EMBL:ESJ99041.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF457 {ECO:0000313|EMBL:ESJ99041.1};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
RN   [2] {ECO:0000313|EMBL:USF23808.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF457 {ECO:0000313|EMBL:USF23808.1};
RA   Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:USF23808.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ASF457 {ECO:0000313|EMBL:USF23808.1};
RA   Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA   Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT   "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT   Model to Study Microbiome Function.";
RL   Submitted (JUN-2022) 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; AYGZ01000009; ESJ99041.1; -; Genomic_DNA.
DR   EMBL; CP097562; USF23808.1; -; Genomic_DNA.
DR   RefSeq; WP_023275178.1; NZ_FTRD01000023.1.
DR   AlphaFoldDB; V2QDJ9; -.
DR   STRING; 1379858.N508_00336; -.
DR   GeneID; 78587609; -.
DR   PATRIC; fig|1379858.3.peg.333; -.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_019240_0_0_0; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000017429; 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   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:UP000017429};
KW   Transferase {ECO:0000313|EMBL:ESJ99041.1}.
FT   DOMAIN          338..487
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   488 AA;  54149 MW;  2C75ACE2CDE9FE22 CRC64;
     MSYIIKGRTC DYEVVIGLEV HCQVISNAKL FSGASAASGG TPNDNVAFID AGFPGMLPVV
     NKFCVEQAVK TGLGLNAVIN KESVFARKNY FYADLPQGYQ ISQFDKPIVG NGSLEIELED
     GSTKTIGIER LHLEQDAGKS IHDMLSGKSC IDLNRSGVAL MEIVSKPDMS SPYEAGAYLT
     KLRSIVRYLE TCDGNMNEGS MRCDANVSVR PAGSTELRTR CEIKNVNSIR YLMQAIEYEA
     NRHVDAYDNG EEIYQETRLF NAHKKETRSM RGKENANDYR YFPDPDLAFP LIVSDELLEA
     VKSSMPEMPD EKSKRFMAEY KLSEDDAKRL VAEKSVAEYF EEAVREKGSD AKKAASLILV
     ELAAIMGEKQ VDNIRDLKTT ASRLGRITAL VEDGTIGLRI AKELLPMIEE TDKEPEAIID
     EKGLKQVSDT KEIEKIIDKI IADNPKNVED YKAGKEKLFG FFVGQAMKAT QGKANPGIIN
     NILKEKLK
//

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