ID GATB_PARBD Reviewed; 603 AA.
AC C1G198;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 24-JAN-2024, entry version 61.
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=PADG_00638;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(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: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; KN275957; EEH44349.2; -; Genomic_DNA.
DR RefSeq; XP_010755914.1; XM_010757612.1.
DR AlphaFoldDB; C1G198; -.
DR SMR; C1G198; -.
DR STRING; 502780.C1G198; -.
DR GeneID; 22580447; -.
DR KEGG; pbn:PADG_00638; -.
DR VEuPathDB; FungiDB:PADG_00638; -.
DR eggNOG; KOG2438; Eukaryota.
DR HOGENOM; CLU_019240_4_1_1; -.
DR InParanoid; C1G198; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 5474932at2759; -.
DR Proteomes; UP000001628; 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; 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; 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; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..603
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000413268"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 66702 MW; B7D8C9ECFA18366A CRC64;
MIRQCLSRRA ACPCYRIAAG GTELTGCLYP QSSRISRRGR DWSSTSRRAI DTQTSGASNG
ADYVPLRKQL KEQAREGRAA TRKGEVSPPE HEDWELTVGI EIHAQLDTDT KLFSRASAAI
DDVPNSNVAL FDIALPGSQP LFQPATLIPA LRAAIALNCD VQRVSRFDRK HYFYQDQPAG
YQITQYYEPY AKNGSIWLGP HDGIAKEDGV GVKIGIKQIQ LEQDTAKSQE LPSSTYLLDF
NRVSRPLIEI ITLPQIHSPA TAAACVRKIQ TILQSVGAVT TGMEMGGLRA DVNVSVRKRS
EGVGDHQYHG ITGLGQRTEI KNLSSFKAVE NAIIAERDRQ IAVLRAGGAI EGETRGWTLG
STETRKLRGK EGEVDYRYMP DPDLGPVIIG IDVFFELKAK LPVLPDALLQ SLVQDPKYGL
STDDAKALIE LDDGDRLDYY KDAVDILITL QKDLSDDFSG GGKVVGNWVL HELGGLLTKS
NLHWDSERVP AQSLAEIINL LSRNKITGST AKSLLAMVFD GDKRSISQIV EDENLLLQSL
SREEYIALAE EVMRQNPKMV MEICEKRQLG KIGWLVGQIK QIGDRNRVEA QKAEEILREL
ILK
//
