GATB_FUSV7
ID GATB_FUSV7 Reviewed; 617 AA.
AC C7YPY3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
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 Flags: Precursor;
GN ORFNames=NECHADRAFT_39102;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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 -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
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DR EMBL; GG698898; EEU45929.1; -; Genomic_DNA.
DR RefSeq; XP_003051642.1; XM_003051596.1.
DR AlphaFoldDB; C7YPY3; -.
DR SMR; C7YPY3; -.
DR STRING; 140110.NechaP39102; -.
DR EnsemblFungi; NechaT39102; NechaP39102; NechaG39102.
DR GeneID; 9673390; -.
DR KEGG; nhe:NECHADRAFT_39102; -.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_4_1_1; -.
DR InParanoid; C7YPY3; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 898782at2759; -.
DR Proteomes; UP000005206; 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: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; 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; 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 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; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT CHAIN 57..617
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000413263"
FT REGION 53..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 68889 MW; 24706DE50DFDEBCF CRC64;
MPRIPTSVLG KYLLSGQISR QGCVGARQIT RHSALPSAAV SVANSARLLH VSSETVPPPP
AQPVPLRKQL KDEAKKAKKQ GKKKSKGDSQ TVDGWELTVG IEIHAQLNTA RKLFSPAVTS
FNDEPNSHVA LFDLSMPGSQ PLFQKETLIP ALRAALALNC DIQKLSRFDR KHYFWWDQPS
GYQITQYYEP FARNGHITLL ARDGISPQDG ESVTIGIKQV QLEQDTAKTL AQADKVNWLD
FNRVGVPLIE IITEPEMHHP RTAAVLVRKI QMLLNTVDAC VSGMETGGLR ADVNVSVRRT
DGSNPSLGTR TEIKNLSTIK AVEDAIIAER DRQISELEAG RAIPSETRGW TLGSNETRRL
RGKEGEVDYR YMPDPDIAPL VIGDDLVDHL RRSLAVSPDS ELDTLIARYG LTAKDALSLI
NLENGSRVQY FYKVLKSVEE KLAAELTEEE MPEFKSYSTL VGNWIIHELG RLTTFKAGPL
AARDLSFTPE GDCLQVPDAD LAQLLYHLVR KQITGKVAKE LLFAIYLNEI EGGITQAIED
NDLWFKEIPE EEYEKLADEV MEGEDKVLQE FVDYKQFPQG KLMYLVGKMM RLGPTERIVP
ANAERVMRAK VEKLRSE
