UniProt: A0A090CYR3

Database: UniProt
Entry: A0A090CYR3_9BACT

LinkDB:  A0A090CYR3_9BACT 
Original site:  A0A090CYR3_9BACT

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Ontology (5)   
   GO (5)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (20)   

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ID   A0A090CYR3_9BACT        Unreviewed;       483 AA.
AC   A0A090CYR3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000256|HAMAP-Rule:MF_00121};
DE            Short=Asp/Glu-ADT subunit B {ECO:0000256|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000256|HAMAP-Rule:MF_00121,
GN   ECO:0000313|EMBL:CDR33802.1};
GN   ORFNames=CSEC_0975 {ECO:0000313|EMBL:CDR33802.1};
OS   Criblamydia sequanensis CRIB-18.
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC   Criblamydia.
OX   NCBI_TaxID=1437425 {ECO:0000313|EMBL:CDR33802.1, ECO:0000313|Proteomes:UP000031552};
RN   [1] {ECO:0000313|EMBL:CDR33802.1, ECO:0000313|Proteomes:UP000031552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR33802.1,
RC   ECO:0000313|Proteomes:UP000031552};
RA   Linke B.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDR33802.1, ECO:0000313|Proteomes:UP000031552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR33802.1,
RC   ECO:0000313|Proteomes:UP000031552};
RA   Bertelli C., Goesmann A., Greub G.;
RT   "Criblamydia sequanensis harbors a mega-plasmid encoding arsenite
RT   resistance.";
RL   Submitted (SEP-2014) 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       ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00000352, ECO:0000256|HAMAP-
CC         Rule:MF_00121};
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, ECO:0000256|HAMAP-
CC         Rule:MF_00121};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC       {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_00121}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDR33802.1}.
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DR   EMBL; CCEJ010000004; CDR33802.1; -; Genomic_DNA.
DR   RefSeq; WP_041017350.1; NZ_CCEJ010000004.1.
DR   AlphaFoldDB; A0A090CYR3; -.
DR   STRING; 1437425.CSEC_0975; -.
DR   eggNOG; COG0064; Bacteria.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000031552; Unassembled WGS sequence.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1.
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; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00121};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00121};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00121};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00121}; Reference proteome {ECO:0000313|Proteomes:UP000031552};
KW   Transferase {ECO:0000313|EMBL:CDR33802.1}.
FT   DOMAIN          332..480
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   483 AA;  54947 MW;  CE75AC128EA708C8 CRC64;
     MANSKWETII GLEIHAELNT KSKLFSSAPN HFGDEPNTNI TVVCTGQPGA LPVLNKEAVK
     KAVQFGLAIN AKIAKFSKFD RKSYFYPDSP RNFQITQFDE PIVIGGTVIA EVEAQEKSFS
     VNRVHLEDDA GMLKHFSTFG GVDYNRAGVP LIEIVSEPCI RSSKEAVAYA MAVKSILEYL
     DASDCNMEEG SLRFDVNISV RPFGEEKFRN KAEIKNLNSF SFMEMAIEAE IKKQIKAYES
     AEDPEFRIPQ ATYRFDPEKK TTILMRKKEE ADDYRYFPEP DLVPIILTDA YIEEIKRNLP
     ELPLERKRRY ERELALSEHT AFVLTSEKKF ADYFEASLKK TKAARSLANW LTVEFSGRFK
     DQDHFVYESK IPPENVAELV NLIEDKAITG KIAKTVADEM VKFPHKTPLQ IVKEHDLQPS
     ENVEEIEKFI DEVLKENEQS ILDIKAGKDK AFGFLIGQVM KKCKGKAPPE LVNQLLKSKL
     EKH
//

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