GATB_MOUSE
ID GATB_MOUSE Reviewed; 557 AA.
AC Q99JT1; Q8BMU3; Q8BUY3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, 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};
DE AltName: Full=Cytochrome c oxidase assembly factor PET112 homolog;
DE Flags: Precursor;
GN Name=Gatb {ECO:0000255|HAMAP-Rule:MF_03147};
GN Synonyms=Pet112 {ECO:0000255|HAMAP-Rule:MF_03147},
GN Pet112l {ECO:0000255|HAMAP-Rule:MF_03147};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-529, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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: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 (QRSL1), B (GATB) and C (GATC) subunits.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
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DR EMBL; AK028193; BAC25803.1; -; mRNA.
DR EMBL; AK034702; BAC28801.1; -; mRNA.
DR EMBL; AK081800; BAC38336.1; -; mRNA.
DR EMBL; BC005709; AAH05709.1; -; mRNA.
DR CCDS; CCDS17441.1; -.
DR RefSeq; NP_659145.1; NM_144896.4.
DR AlphaFoldDB; Q99JT1; -.
DR SMR; Q99JT1; -.
DR BioGRID; 230847; 5.
DR STRING; 10090.ENSMUSP00000119949; -.
DR iPTMnet; Q99JT1; -.
DR PhosphoSitePlus; Q99JT1; -.
DR EPD; Q99JT1; -.
DR MaxQB; Q99JT1; -.
DR PaxDb; Q99JT1; -.
DR PeptideAtlas; Q99JT1; -.
DR PRIDE; Q99JT1; -.
DR ProteomicsDB; 272931; -.
DR Antibodypedia; 27767; 138 antibodies from 20 providers.
DR DNASU; 229487; -.
DR Ensembl; ENSMUST00000127348; ENSMUSP00000119949; ENSMUSG00000028085.
DR GeneID; 229487; -.
DR KEGG; mmu:229487; -.
DR UCSC; uc008pqs.1; mouse.
DR CTD; 5188; -.
DR MGI; MGI:2442496; Gatb.
DR VEuPathDB; HostDB:ENSMUSG00000028085; -.
DR eggNOG; KOG2438; Eukaryota.
DR GeneTree; ENSGT00390000016644; -.
DR HOGENOM; CLU_019240_1_2_1; -.
DR InParanoid; Q99JT1; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 898782at2759; -.
DR PhylomeDB; Q99JT1; -.
DR TreeFam; TF314355; -.
DR BioGRID-ORCS; 229487; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Gatb; mouse.
DR PRO; PR:Q99JT1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99JT1; protein.
DR Bgee; ENSMUSG00000028085; Expressed in right kidney and 248 other tissues.
DR ExpressionAtlas; Q99JT1; baseline and differential.
DR Genevisible; Q99JT1; MM.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; ISO:MGI.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; ISO:MGI.
DR GO; GO:0032543; P:mitochondrial translation; ISO:MGI.
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; 1.
DR TIGRFAMs; TIGR00133; gatB; 1.
DR PROSITE; PS01234; GATB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT CHAIN 31..557
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000010711"
FT REGION 21..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 529
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 211
FT /note="N -> S (in Ref. 1; BAC38336)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="T -> P (in Ref. 1; BAC25803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 62118 MW; CD8D0EDFE595B1B5 CRC64;
MAAPMLRLGF PGRRWALTWL DGGSRHRSGS QTGPTSNWAR RQSSVAQPSL HTAQKPRKGE
HKWAAVVGLE IHAQISSNSK LFSGAQVCFA APPNSLVSYF DASLPGTLPV LNRRCVEAAV
MTGLALNCHI NKKSLFDRKH YFYSDLPAGY QITQQRLPIA ANGHLTYCIY LGKKPSQVTT
KTVRIKQIQL EQDSGKSLHD DLRSQTLIDL NRAGIGLLEV VLEPDLCCGE EAALAVRELQ
LILQALGTSQ ANMAEGQLRV DANISVHHPG EPLGVRTEVK NLNSLRFLAK AIDYEIQRQI
TELENGGEIL NETRSFDYKL GCTMPMRDKE GKQDYRFMPE PNLPPLVLYD DTSLPRGADS
QQVINIDQLR DMLPELPSAT RERLVQQYGM LPEHSFALLN EVGLLEFFQN VIKETRTEPK
KVTNWVLNTF LCYLKQQNLA VSESPVTPSA LAELLNLLDR KAISSSAAKQ VFEELWKGEG
KTAAQIVSEQ QLELMQDQEA LEKLCQTTID GHPQVVMDVK KRNPKAINKL IGLVRKASHS
RADPALIKKI LERKLSL
