ID   GATB_PAUCH              Reviewed;         496 AA.
AC   B1X4D6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_03147};
DE            Short=Glu-AdT subunit B {ECO:0000255|HAMAP-Rule:MF_03147};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
GN   OrderedLocusNames=PCC_0364;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln). The reaction
CC       takes place in the presence of glutamine and ATP through an activated
CC       gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03147}.
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_03147};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03147}.
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DR   EMBL; CP000815; ACB42805.1; -; Genomic_DNA.
DR   RefSeq; YP_002049015.1; NC_011087.1.
DR   AlphaFoldDB; B1X4D6; -.
DR   SMR; B1X4D6; -.
DR   GeneID; 6481741; -.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0070111; C:organellar chromatophore; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR   GO; GO:0032543; P:mitochondrial 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; Organellar chromatophore; Plastid;
KW   Protein biosynthesis.
FT   CHAIN           1..496
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   organellar chromatophore"
FT                   /id="PRO_0000413236"
SQ   SEQUENCE   496 AA;  55541 MW;  DE6BEAB318356169 CRC64;
     MVSIAGQIGW EAVIGIETHV QLGTASKIFT QASTNFGDDP NTNINPVVCG LPGTLPVLNQ
     KVLEYAVKAA MALNLKVSEH SKFDRKQYFY PDLPKNYQIS QYDEPIAEDG WIEVEIAEKE
     KQTYTKRIGI ERLHMEEDAG KLVHIGSDRL TGSNHSLIDY NRAGIALAEI VSKPDLRTGR
     EAAEYASEIR RIMRYLGVSD GNMQEGSLRC DVNISVRKGK NAPFGIKIEI KNMNSFSAIQ
     KACEYEISRQ IKAINNGERI IQETRLWDEN KQLTTSMRSK EVASDYRYFP DPDLGPIEIE
     LDRREAWKHE LPELPAIKRH RYVEELGLSI YDARIITDEL PMAEYFESAI TAGAEAKALA
     NWLMGDISAY LNTNKTTIGE IKLRPSQLAE LIILISNGEI SGKIAKEILP ELIEKGLSPS
     ALIDDKGLAM ISDNNQIRTI IVELLSLYPE EVKAFRNGKI KLQGFFVGQL MKKTSGKADP
     KISNKILLEI LNASEN