ID A0A195FQR6_9HYME Unreviewed; 600 AA.
AC A0A195FQR6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03147};
DE Short=Glu-AdT subunit B {ECO:0000256|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03147};
GN ORFNames=ALC56_03387 {ECO:0000313|EMBL:KYN42249.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN42249.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN42249.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN42249.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN42249.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000256|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:0000256|ARBA:ARBA00000924, ECO:0000256|HAMAP-
CC Rule:MF_03147};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000256|HAMAP-
CC Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_03147}.
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DR EMBL; KQ981382; KYN42249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195FQR6; -.
DR STRING; 34720.A0A195FQR6; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 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; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR004413; GatB.
DR InterPro; IPR023168; GatB_Yqey_C_2.
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 Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03147};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03147};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03147};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03147};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03147}; Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KYN42249.1}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..600
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012113709"
FT DOMAIN 27..156
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 600 AA; 67598 MW; ED73348C93CE1FDB CRC64;
MRLLLLIGLI AVVSCASNGP KVTDKVWFEI KIGDEVAGRV EIGLFGKTVP KTVKNFVELA
KLPEGEGYKG SKFHRVIKDF MIQGGDFTKG DGTGGRSIYG DRFADENFKL KHYGAGWLSM
ANAGKDTNGS QFFITVKQTP WLDGRHVVFG KVIKGMVLNR KCVELAVMTA LALSCQLNET
SLFERKHYFY ADLPAGFQIT QQGQPIAVNG EIKFHVFTPG LHKSPYLKSS KIKQIQLEQD
SGKSLHDENV AKSLIDLNRA GIPLMEFVFE PDLVDGEEAA ALVKELAFML QLLGVCSSKM
EEGALRVDAN VSVSNRDSLG IRTEIKNIGS VRAVAAAIQY EINRHISILE VGDKMFNETR
AWDAVNKKTV PMREKEDKED YRFMPETNLP PLCIHLREDL PNKSNLVDAV VLKRQLPELP
EQIRQRLKDV FKISPEIIIA LMSDFALLQL FNRITKNNEN REPQLVAKFL VMELLTFLYK
NKLTIEFCVP HEDFIGQLID LLQGNLINLI TAKKILKELI VNSNKLPKEI VKEHNWFLIS
DEKQLEQICL EIIEKNPKLV SAYKSGKKKC FNALMGEIAK TTEQRANLAI VAKIMERLLK
//
