ID W5P2L5_SHEEP Unreviewed; 567 AA.
AC W5P2L5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:0000256|HAMAP-Rule:MF_03147,
GN ECO:0000313|Ensembl:ENSOARP00000004665.1};
GN Synonyms=PET112 {ECO:0000256|HAMAP-Rule:MF_03147}, PET112L
GN {ECO:0000256|HAMAP-Rule:MF_03147};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000004665.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000004665.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000004665.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000004665.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 (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}.
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; AMGL01037196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01037202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5P2L5; -.
DR SMR; W5P2L5; -.
DR STRING; 9940.ENSOARP00000004665; -.
DR PaxDb; 9940-ENSOARP00000004665; -.
DR Ensembl; ENSOART00000004746.1; ENSOARP00000004665.1; ENSOARG00000004355.1.
DR eggNOG; KOG2438; Eukaryota.
DR OMA; ARKWWMG; -.
DR Proteomes; UP000002356; Chromosome 17.
DR Bgee; ENSOARG00000004355; Expressed in heart right ventricle and 54 other cell types or tissues.
DR ExpressionAtlas; W5P2L5; baseline.
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 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; 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; 1.
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_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:UP000002356};
KW Transit peptide {ECO:0000256|HAMAP-Rule:MF_03147}.
FT DOMAIN 406..528
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT REGION 28..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 62564 MW; A75AD0688C7C17ED CRC64;
MAAPMLRWCC PGRRFAFARV GCGSCHRRGP PTGSTSNGKR GQSTVAQQPH ITAQKPRKGE
REWAAVVGLE IHAQIASNSK LFSGSQVHFA APPNSLVSFF DASLPGTLPV LNRRCVEAAV
MTGLALDCHI NRKSLFDRKH YFYADLPAGY QITQQRLPIA VNGSLAYSVS VGRKPSQMVT
RTVRVKQIQL EQDSGKSLHD DLRSQTLIDL NRAGIGLLEV VLEPDMSCGE EAATAVRELQ
LILQALGTSQ ANMAEGQLRV DANISVHRPG EPLGVRTEVK NLNSARFLAR AIDYEIQRQI
NELENGGEIL NETRSFDYKL GCTVPMRDKE GKQDYRFMPE PNLPPLLLYD SGSLPPGADP
QQVIDIDRLR ERLPELPRVT RERLVRQYGM LPEHSCALLN EVGLLEFFQS VIKETRAEPK
KVTSWVLNTF LGFLKQQNLA VSESPVTPSA LAELLDLLDR KAISSSAAKQ VFEELWRNEG
KTPAQIVAEK KLELLQDLEA LEQLCRSTLE AAPSRGTRPR GGGSLGRRSG FGQRGTSPAH
PSSPEELPNN GWPSFICNPQ LILSVFS
//
