ID G5BMJ2_HETGA Unreviewed; 623 AA.
AC G5BMJ2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-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 Synonyms=PET112 {ECO:0000256|HAMAP-Rule:MF_03147}, PET112L
GN {ECO:0000256|HAMAP-Rule:MF_03147};
GN ORFNames=GW7_21585 {ECO:0000313|EMBL:EHB10503.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB10503.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB10503.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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}.
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DR EMBL; JH171101; EHB10503.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BMJ2; -.
DR STRING; 10181.G5BMJ2; -.
DR eggNOG; KOG2438; Eukaryota.
DR InParanoid; G5BMJ2; -.
DR Proteomes; UP000006813; 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: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 Gene3D; 1.10.10.410; -; 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; IPR023168; GatB_Yqey_C_2.
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:UP000006813};
KW Transferase {ECO:0000313|EMBL:EHB10503.1};
KW Transit peptide {ECO:0000256|HAMAP-Rule:MF_03147}.
FT DOMAIN 473..621
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT REGION 90..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 68869 MW; 6A88145928C9AD59 CRC64;
MEIFISLIFR KPSVDSHSGN LRVAMIVGNG SLPVQAYRGL DHLQNYASQR SSRQRTTESP
DQNAGVAMAA PLLRWFGPGR RWPLAWVDSG SRHRRGAPTG SASNRTREQS SVAQHPLCTS
QKLRKGEHKW AAVVGLEIHA QISSNSKLFS GSQVCFAAPP NSLVSFFDAS LPGTLPVLNR
RCVEAAVMTG LALNCHINKK SLFDRKHYFY ADLPAGYQIT QQRLPIATHG SLTYRVSVGT
KRSHMATKTV RIKQIQLEQD SGKSLHDGLR SQTLIDLNRA GVGLLEVVLE PELSCGEEAA
TVIRELQLIL QALGTSQANM AEGQLRVDAN ISVHHPGEPL GIRTEVKNLN SIRFLARAID
YEIQRQINEL EHGGEILNET RSFDSKLGCT VPMRDKEGRQ DYRFMPEPNL PPLVLYDTAS
LPAGAQSQQV INIDQIRDAL PELPSVTRER LVQRYGMLPE HSFTLLNEVG LLQFFQNVMK
ETRAEPKKVT SWVLNVLLGY LKHHSLAVSE SPITPSALAG LLDLLDSKAI SSSAAKQVFE
ELWKGKGKTA VQIVSEKQLG LMQDQEALEQ LCRSTMEEHP QAVMDMKKGN PRAINKLIGL
VRKAALNRAD PAVIKALLEK LSS
//
