GATB_AQUAE
ID GATB_AQUAE Reviewed; 478 AA.
AC O66766;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE Short=Asp/Glu-ADT subunit B;
DE EC=6.3.5.-;
GN Name=gatB; OrderedLocusNames=aq_461;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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) (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC06727.1; -; Genomic_DNA.
DR PIR; B70342; B70342.
DR RefSeq; NP_213326.1; NC_000918.1.
DR RefSeq; WP_010880264.1; NC_000918.1.
DR PDB; 3H0L; X-ray; 2.30 A; B/E/H/K/N/Q/T/W=1-478.
DR PDB; 3H0M; X-ray; 2.80 A; B/E/H/K/N/Q/T/W=1-478.
DR PDB; 3H0R; X-ray; 3.00 A; B/E/H/K/N/Q/T/W=1-478.
DR PDBsum; 3H0L; -.
DR PDBsum; 3H0M; -.
DR PDBsum; 3H0R; -.
DR AlphaFoldDB; O66766; -.
DR SMR; O66766; -.
DR STRING; 224324.aq_461; -.
DR EnsemblBacteria; AAC06727; AAC06727; aq_461.
DR KEGG; aae:aq_461; -.
DR PATRIC; fig|224324.8.peg.382; -.
DR eggNOG; COG0064; Bacteria.
DR HOGENOM; CLU_019240_0_0_0; -.
DR InParanoid; O66766; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 497127at2; -.
DR EvolutionaryTrace; O66766; -.
DR Proteomes; UP000000798; 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; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 1.10.150.380; -; 1.
DR HAMAP; MF_00121; GatB; 1.
DR InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; 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 PANTHER; PTHR11659; PTHR11659; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR SUPFAM; SSF89095; SSF89095; 1.
DR TIGRFAMs; TIGR00133; gatB; 1.
DR PROSITE; PS01234; GATB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..478
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148757"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3H0L"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3H0R"
FT STRAND 116..128
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 191..202
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 220..239
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:3H0L"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:3H0L"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:3H0L"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:3H0L"
SQ SEQUENCE 478 AA; 55041 MW; F725AE78944BD79A CRC64;
MNEKYEAVIG LEIHVQMDTK TKMFCGCKVE FGAEPNTNVC PVCLGMPGAL PIVNKRAVEY
AIRASLALNC EVHEESVFAR KHYFYPDLPK GYQISQYEKP LATNGWVELN LPNGEKKKVR
IRRLHIEEDA GKNIHEGDKT LVDLNRAGTP LMEIVTEPDI RTPEEARLFL EKLRNIMRYA
GVSKADMEKG QLRCDINVSI RPKGSKEFGT RVEIKNVNSF RFVQKALEYE IERQINVVEE
GGEVVQETRT FDPQTGKTYP MRTKEEAEDY RYFPDPDLVP LKVKKEWIEE IKKNMPELPD
QRFERLIKEY GLSEYEAGIL VNHKEVGDFF EEAVRHFKEP KGIVNWLIND LLGLLRDKGI
SIEESPVKPE HLAELVKLIK EKVISTKIGK EVIKEMVETG KTPSQIVEEK GLKQITDENQ
IKELVKKIFE KHPKEVERLK QGEEKLIGFF VGQVMRETRG KANPQVVNKV IRELVKEV
