GATB_AJECH
ID GATB_AJECH Reviewed; 574 AA.
AC C6HRN2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 25-MAY-2022, entry version 46.
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=HCDG_08617;
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EER37166.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GG692436; EER37166.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C6HRN2; -.
DR SMR; C6HRN2; -.
DR STRING; 544712.C6HRN2; -.
DR EnsemblFungi; EER37166; EER37166; HCDG_08617.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_4_1_1; -.
DR Proteomes; UP000002624; 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; 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; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03147"
FT CHAIN 13..574
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000413239"
FT REGION 34..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 63667 MW; 67A4420C86CE0182 CRC64;
MIRQFVSHRG IPCYRLAVRR VELTEPFHHP SPWPLGRKNW STSDEAKSKR AAMRKGGAPP
PEHEDWELTV GIEIHAQLDT DAKLFSSASA ALDDVPNSNI ALFDIALPGS QPLFQPSTLI
PAIRAAIALN CDVQRVSRFD RKHYFYQDQP AGYQITQYYE PYAKNGSIWL GAHDGIAKED
GEGVQIGIKQ IQMEQDTAKS QELPSSTYLL DFNRVSRPLI EIITLPQIHS ATTAAACVRK
IQAILQSVGA VTTGMEMGGL RADVNVSVRK RSEAAGDHQY DGVAGLGQRT EIKNLSSFKA
VEYAIIAERD RQIAVLKAGG TIQGETRGWT LGSTETRKLR GKEGEVDYRY MPDPDLGPVI
IGDDVISDLR RNIPGLPDEL LQMLVQDPKY GLSTVDAKTL IELDDGQRLE YYQDAVEILT
TLQPDLSADF SAGKVVGNWV LHELGGLLTK SSAHWDSQRV PAQSLAEIIN LLSRKNITSS
SAKSLLAMAF DGDKRSISQI VEDKNLLFQS LSRHEYLALA EEVMRQNPKM VSEIREKAQL
GKMGWLVGQI KRIGDPNRVE AQKAEEILRE LILK
