UniProt: E4Q4U1

Database: UniProt
Entry: E4Q4U1_CALOW

LinkDB:  E4Q4U1_CALOW 
Original site:  E4Q4U1_CALOW

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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   E4Q4U1_CALOW            Unreviewed;       480 AA.
AC   E4Q4U1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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:ADQ04183.1};
GN   OrderedLocusNames=Calow_0607 {ECO:0000313|EMBL:ADQ04183.1};
OS   Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL).
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=632518 {ECO:0000313|EMBL:ADQ04183.1, ECO:0000313|Proteomes:UP000006889};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OL;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor owensensis OL.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ04183.1, ECO:0000313|Proteomes:UP000006889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700167 / DSM 13100 / OL
RC   {ECO:0000313|Proteomes:UP000006889};
RX   PubMed=21216991; DOI=10.1128/JB.01515-10;
RA   Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA   Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA   Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA   Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT   "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT   biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT   Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT   Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL   J. Bacteriol. 193:1483-1484(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; CP002216; ADQ04183.1; -; Genomic_DNA.
DR   RefSeq; WP_013411587.1; NC_014657.1.
DR   AlphaFoldDB; E4Q4U1; -.
DR   STRING; 632518.Calow_0607; -.
DR   KEGG; cow:Calow_0607; -.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_019240_0_0_9; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000006889; 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:UP000006889};
KW   Transferase {ECO:0000313|EMBL:ADQ04183.1}.
FT   DOMAIN          327..477
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   480 AA;  54666 MW;  57FD1AA3B469ED1B CRC64;
     MEYEVVIGLE VHAELATKSK IFCSCTTEFG GEPNTHCCPI CTGMPGVLPV LNKKAVEYAI
     MAGLATNCQI ARYSKQDRKN YFYPDLPKAY QISQYDLPLC YNGYIDIEVN GQKKRIGIKR
     IHIEEDAGKL LHDQWEEGSL VDFNRCGVPL IEIVTEPDLR SSEETRVFLE KLKAILQYTE
     VSDCKMQEGS LRVDVNLSVR PKGSKEFGTR TEMKNLNSFR SVVRAIEYEA RRQIEVLESG
     GVIVQETRRW DDAKGISLSM RTKEEAHDYR YFPEPDLPPI VVDDSWIEEI RKRIPELPDQ
     KKERYIKEYG LPEYDAGVLT SSKAIASFFE ECIKYTQNIK AASNWMMGEI MRILNDKGLE
     PEEIDNIKIK PNQLASLINL VDNKTISNTI AKQVFEEMFD TGKDPEVIVK EKGLVQITDR
     NVILEAVKQA IANNPKSVED YKNGKDKAFG FLVGQVMKIT KGKANPQLVN EILKEELEKI
//

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