ID   GATB_OSTTA              Reviewed;         537 AA.
AC   Q00YU3;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial {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   Name=GATB {ECO:0000255|HAMAP-Rule:MF_03147}; OrderedLocusNames=Ot11g02110;
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts
CC       and mitochondria. The reaction takes place in the presence of glutamine
CC       and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {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: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC       Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_03147}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03147}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03147}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAID01000011; CAL55816.1; -; Genomic_DNA.
DR   RefSeq; XP_003082013.1; XM_003081965.1.
DR   AlphaFoldDB; Q00YU3; -.
DR   SMR; Q00YU3; -.
DR   STRING; 70448.Q00YU3; -.
DR   GeneID; 9833633; -.
DR   KEGG; ota:OT_ostta11g01930; -.
DR   eggNOG; KOG2438; Eukaryota.
DR   InParanoid; Q00YU3; -.
DR   OMA; QLEMDTG; -.
DR   OrthoDB; 898782at2759; -.
DR   Proteomes; UP000009170; Chromosome 11.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   Gene3D; 1.10.10.410; -; 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; 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; 2.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW   Plastid; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..537
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000413232"
SQ   SEQUENCE   537 AA;  57101 MW;  B69484F28A684160 CRC64;
     MSLASVAARR ASSLRASTLV RTTFNRAIAS ASAGDALETV VGVEIHVRLQ TRSKLFSGSA
     SAYGGEPNSR VAPFDASLPG TLPVLNAGAV ALAVKLGIAL EGEVQLRSAF DRKHYWYADL
     PHGYQITQKR SPIVLGGVVR CQGNLSGDDA GDERSTDGAL KVGIERVQLE MDTGKSSVAE
     DGRGTLVDLN RAGQALVEIV SEPDMRSGEE AVACVEALQR MLRYLHVSDA NMEEGSLRCD
     VNVSVRTSEE RARGVFGERV EIKNLNSLRS IARAVKYEAQ RHAKVLAGGG KIERETRSFD
     VNTGKTVVLR TKENLLDYKF TPEPDLPSLV LTSADVEAIA GRMPELPNAA YERLVSGGAS
     PSASNTIVAF PSTLKYFDVA MENCGAAKSA DVANFIANEI IGAARKDAGA THKEPLSTLP
     RAASARRVGE LLGKVADGTL SGRMAKQVLE ALMNSDERAL GDIVDDICGG GQISSDDHLR
     DICHSVVRDK PEEVRLLQGG KSKLMGALVG EVMKRTSGRA NPKDVSKLLA DIVAGEP