UniProt: E4U5L2

Database: UniProt
Entry: E4U5L2_OCEP5

LinkDB:  E4U5L2_OCEP5 
Original site:  E4U5L2_OCEP5

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Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (22)   

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ID   E4U5L2_OCEP5            Unreviewed;       471 AA.
AC   E4U5L2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   OrderedLocusNames=Ocepr_0106 {ECO:0000313|EMBL:ADR35570.1};
OS   Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 /
OS   506).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Oceanithermus.
OX   NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR35570.1, ECO:0000313|Proteomes:UP000008722};
RN   [1] {ECO:0000313|Proteomes:UP000008722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC   {ECO:0000313|Proteomes:UP000008722};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Zhang X., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Faehnrich R.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Oceanithermus profundus DSM
RT   14977.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADR35570.1, ECO:0000313|Proteomes:UP000008722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC   {ECO:0000313|Proteomes:UP000008722};
RX   PubMed=21677858; DOI=10.4056/sigs.1734292;
RA   Pati A., Zhang X., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Hauser L.,
RA   Jeffries C.D., Brambilla E.M., Rohl A., Mwirichia R., Rohde M.,
RA   Tindall B.J., Sikorski J., Wirth R., Goker M., Woyke T., Detter J.C.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Oceanithermus profundus type strain (506).";
RL   Stand. Genomic Sci. 4:210-220(2011).
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}.
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DR   EMBL; CP002361; ADR35570.1; -; Genomic_DNA.
DR   RefSeq; WP_013456740.1; NC_014761.1.
DR   AlphaFoldDB; E4U5L2; -.
DR   STRING; 670487.Ocepr_0106; -.
DR   KEGG; opr:Ocepr_0106; -.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_019240_0_1_0; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000008722; Chromosome.
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:UP000008722};
KW   Transferase {ECO:0000313|EMBL:ADR35570.1}.
FT   DOMAIN          321..467
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   471 AA;  51707 MW;  5CFBB51B96B65862 CRC64;
     MYEPVIGLEV HLHLKTKTKM FCSCSADYFG AAPNTHVCPV CLGLPGVLPV PNAQAVDYGI
     MFALALGCEV PEWTQFHRKH YFYPDMPKNY QISQYDRPIG ARGVLEVAGE RIGITRVHLE
     EDAGKSLHPA GEAHTLLDFN RAGSPLIELV TEPDIKSPEQ ARLFLNHLRA IAQTLGISDA
     NPEEGKMRAD VNVSVRRPGE PLGTKVEIKN LNSFRSVQKA LEYEIERQTK ILKKGGQIEQ
     ATLGWDENAG RTYLMRTKEG EADYRYMPEP DIPMLHVTKE WLERVRAAMP ELPAEKMRRY
     REAGVKAYDA EILAYDRELS GLFDAALAAG APAQALANWL NADVRGFLAA GEKTVAETGL
     TPEHLAALVK LADEGKITSR VAKELLPEVM EGADPARLVK ERGLEAVSDE GALAKIVDEV
     IANNPAVVEQ IKGGKAKAIN ALLGQVMKAT RGTARPDLVR KLLAEKIGVE V
//

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