ID A0A1S3SKI1_SALSA Unreviewed; 488 AA.
AC A0A1S3SKI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
DE AltName: Full=Cytochrome oxidase assembly factor PET112 homolog {ECO:0000256|HAMAP-Rule:MF_03147};
DE AltName: Full=PET112-like {ECO:0000256|HAMAP-Rule:MF_03147};
GN Name=gatb {ECO:0000313|RefSeq:XP_014064847.1};
GN Synonyms=GATB {ECO:0000256|HAMAP-Rule:MF_03147}, PET112
GN {ECO:0000256|HAMAP-Rule:MF_03147}, PET112L
GN {ECO:0000256|HAMAP-Rule:MF_03147};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014064847.1};
RN [1] {ECO:0000313|RefSeq:XP_014064847.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014064847.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123}.
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC {ECO:0000256|HAMAP-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 RefSeq; XP_014064847.1; XM_014209372.1.
DR AlphaFoldDB; A0A1S3SKI1; -.
DR OrthoDB; 5474932at2759; -.
DR Proteomes; UP000087266; Chromosome ssa08.
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: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; 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; 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.
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:UP000087266}.
FT DOMAIN 338..487
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 488 AA; 54236 MW; D3D07C99F65E198D CRC64;
MYVCLPMPES SPNKTEKVGF QAPPNSLVSF FDASLPGTLP VLNRRCVEAA VMTGLALNCT
INRKSLFDRK HYFYADLPAG YQITQQRLPI AVDGTLTYSH LGGRKRNTVV TKSVRIKQIQ
LEQDSGKSLH DDYRSQTLID LNRAGVGLME LVMEPDMSCG EEAAAAVREM QLILQALGTC
QGNMAEGQLR VDANVSVHRP GDPWGIRTEV KNINSARNLA RAIDYEIQRQ MFVLESGGTV
QNETRSFDGK TGHTIPMRDK EGLQDYRFMP EPNLPPLMVY EACSTAPPGV APSQVVVLEE
VRERLPELPS VRRQRLVETY GILPEHSFTL VNEDGLMDYF EAVVKETKAG PKKVIGWVMN
ELQGLLHQQN LSVSQSPISP QALAQVLNLQ ENGQISSSIA KQVFQELWKT PGKTAQQIVK
EQDLGMVNDS TEIHRICQKV VDSHPDQVQA IRSGNKKVLN KLMGLVQKET KGRADPVLVR
AILEQKTS
//
