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Database: UniProt
Entry: A0A1D7NPC8_9SPHN
LinkDB: A0A1D7NPC8_9SPHN
Original site: A0A1D7NPC8_9SPHN 
ID   A0A1D7NPC8_9SPHN        Unreviewed;       498 AA.
AC   A0A1D7NPC8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=BG023_112725 {ECO:0000313|EMBL:AOL95634.1};
OS   Porphyrobacter sp. LM 6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX   NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL95634.1, ECO:0000313|Proteomes:UP000094080};
RN   [1] {ECO:0000313|EMBL:AOL95634.1, ECO:0000313|Proteomes:UP000094080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM 6 {ECO:0000313|EMBL:AOL95634.1,
RC   ECO:0000313|Proteomes:UP000094080};
RA   Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of southern
RT   Lake Michigan.";
RL   Submitted (AUG-2016) 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; CP017113; AOL95634.1; -; Genomic_DNA.
DR   RefSeq; WP_069310886.1; NZ_CP017113.1.
DR   AlphaFoldDB; A0A1D7NPC8; -.
DR   STRING; 1896196.BG023_112725; -.
DR   KEGG; porl:BG023_112725; -.
DR   PATRIC; fig|1896196.3.peg.2702; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000094080; 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; 2.
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}; Transferase {ECO:0000313|EMBL:AOL95634.1}.
FT   DOMAIN          345..497
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   498 AA;  54155 MW;  5F375297899B976D CRC64;
     MSNYRIQGAT GEWEVVIGLE VHAQVTSNSK LFSGAATAFG AEPNSQVSLV DAAMPGMLPV
     PNRECIRQAV RTGMAIEAQI NAWSRFDRKN YFYADLPQGY QISQLYHPLV GEGSLLIEAD
     EKAGIPEDKV IGIERIHVEQ DAGKLMHDQH PTMSYVDLNR SGVALMEIVS KPDMRSPAEA
     GAYLRKLRAI LRYVGSCDGN MEEGSMRADV NVSVRKVGEP FGTRTETKNV NSVRFVMQAI
     EHEAMRQVDV LEAGGSVVQE TRLFDPGTGT TRTMRSKEDA HDYRYFPDPD LLPLVLEEDF
     LAECRASLPE LPDAKRKRYV EVLGLTPYNA RELTAEVETF ARFETLLAET AKVIGKDEAK
     VATQVANWSL SVAPGVMKAL GDEADAANAT AAAQAAILAM QEKGEISGGQ AKEIFEIVLK
     TGRDPSEIAE AEGLKQVSDT GAIEAAVDAI IAANADKVEQ YRGGKEALFG FFVGQTMKAM
     QGKANPAVVN QLLKDKLG
//
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