GATB_NEUCR
ID GATB_NEUCR Reviewed; 647 AA.
AC Q7S2V0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
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};
GN ORFNames=NCU09025;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC 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; CM002242; EAA29736.1; -; Genomic_DNA.
DR RefSeq; XP_958972.1; XM_953879.2.
DR AlphaFoldDB; Q7S2V0; -.
DR SMR; Q7S2V0; -.
DR STRING; 5141.EFNCRP00000008927; -.
DR EnsemblFungi; EAA29736; EAA29736; NCU09025.
DR GeneID; 3875119; -.
DR KEGG; ncr:NCU09025; -.
DR VEuPathDB; FungiDB:NCU09025; -.
DR HOGENOM; CLU_019240_4_1_1; -.
DR InParanoid; Q7S2V0; -.
DR OMA; ARKWWMG; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..647
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000413265"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71055 MW; E153D04EC4EE9B4D CRC64;
MPRIPTVELS RYLLTGHIAS PGCLRARAAL PGKNTRVALG GAPLPSRQLQ PRQHARYLTT
ETSFANPSAT TSSPAAAAPF RKQLKEQAKA LKKSGHKKKK SSDNQTVPGW ELTVGIEIHA
QLNTAHKLFS PATTSFNDPP NTHVAPFDLA LPGSQPLFQP ATLIPAVRAA LALNCSIQPV
SRFDRKHYFH WDQPSGYQIT QFYEPFAKDG FITLYARDGI AAEDGEEIKV GIKQVQMEQD
TAKTTAQPGD VQWLDFNRVG VPLIEIITLP EIHHPATAAA LVRKVQMVLA SVDACVSGLE
EGGLRADVNV SVRRTDDPSG KLGTRTEIKN LSSFKAVEDA IIAERDRQIE LLEEGGEVKG
ETRGWSLGST ETRRLRGKEG EVDYRYMPDP DLGPVVIGED LVARLRETMG VLPDQEADQL
MERYNLSAKD ALSLMLLDGG ARIQYFYNVL DSLEERLVAD GQAVPEGAEH ATLAANWCLH
ELGKLTDSAS SSSCSDPDVL EGLAMTPLGE SPLVPSSSLA AILHHLYSRT ITAKVAKDLL
WAVYRGEIPE GGTTSYIDTH GLWFKELPEE EYAKLADEVI QGEEKILGEF LRWKQGKMKA
YPQGKLMFLV GKMMRGGPEG RVEASGAERV LRRRIEEVYL PELEKGE
