ID F4LMJ4_TREBD Unreviewed; 777 AA.
AC F4LMJ4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Asn/Gln amidotransferase {ECO:0000313|EMBL:AEE15756.1};
GN OrderedLocusNames=Trebr_0309 {ECO:0000313|EMBL:AEE15756.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE15756.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC presence of glutamine and ATP through an activated phospho-Asp-
CC tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|ARBA:ARBA00024799}.
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:0000256|ARBA:ARBA00000924};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123}.
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DR EMBL; CP002696; AEE15756.1; -; Genomic_DNA.
DR RefSeq; WP_013757475.1; NC_015500.1.
DR AlphaFoldDB; F4LMJ4; -.
DR STRING; 906968.Trebr_0309; -.
DR KEGG; tbe:Trebr_0309; -.
DR eggNOG; COG0064; Bacteria.
DR HOGENOM; CLU_360130_0_0_12; -.
DR OrthoDB; 9788068at2; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1.
DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 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; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR042114; GatB_C_1.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
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; PF00710; Asparaginase; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546}.
FT DOMAIN 297..444
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 777 AA; 86399 MW; F8C2344162F0095C CRC64;
MYQSHVYLEA RILLSAADTV FSDEGKPCVT APGILETVCL LAGTLSCSFP EKARFERLTG
ALPESESRRL TGLSLKVAEN GRLEIEFHHR KKSVHIEEVR LEEDAGRLTR SEGKTRMDYT
YAGYPSVRIK TGADFELGEE AELFLNELRR LIQYLGISGD IQIETAIRCN AYAALARYPE
IPTYYVKLRN LNSFNFVRKA INSELDRQES VLTGGGTVAS ESRLWNERQN ITESYKQRSR
QDVRRFEPVT PAAYETIPAA GSVPCELPEP RRRRLCAEYS VSRIDADFIC DEKERADFFE
EAVRLGADPV AAAHIMNADL VRLLKRQNLS ISQNPVSAAR FASIVQLFVA HRIHGGLVKQ
LIQNIIDTDK DPEEAVERKG FAQISSEEEL LPLIRKVITA NPAEAEKLRA GDMAPLEFLT
GLIMKRTAGR ASPQTVKYLF KRELHISIVY VLSAGGAISA RRRPDGSISA EDGQVLRELF
AQSVPDVRVQ VVPVGRLFSE EMEPADFAPL IAEIAERIAA GIATGIVVAH GKDTLPYTAA
LLFWLFSDAA VPVVLTASAA LPEDSDEARR NLTLAAETAV REKSGVYVVF GGKVLSPLNL
KFVRPAPDGF VNWNLKEPVF TGSGPLAVQF SGIQEPDPHV MRNLLREAAG SMMLCRIYPG
FKAERYVSMI EEGTRTFFLE LYESGTGNMR DGDYSLKPLL LRGKKHNCRF YCTSQQECRT
EFSDYTTSRR VWREGAVPMG LLTTESAVAL YYAAALLCDS ADELDALMES YAEQYAV
//
