GATB_THEMA
ID GATB_THEMA Reviewed; 482 AA.
AC Q9X100;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=TM_1273;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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}.
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DR EMBL; AE000512; AAD36348.1; -; Genomic_DNA.
DR PIR; H72274; H72274.
DR RefSeq; NP_229078.1; NC_000853.1.
DR RefSeq; WP_004079967.1; NZ_CP011107.1.
DR PDB; 3AL0; X-ray; 3.37 A; B=1-482.
DR PDBsum; 3AL0; -.
DR AlphaFoldDB; Q9X100; -.
DR SMR; Q9X100; -.
DR DIP; DIP-59229N; -.
DR IntAct; Q9X100; 1.
DR STRING; 243274.THEMA_07970; -.
DR EnsemblBacteria; AAD36348; AAD36348; TM_1273.
DR KEGG; tma:TM1273; -.
DR eggNOG; COG0064; Bacteria.
DR InParanoid; Q9X100; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 497127at2; -.
DR EvolutionaryTrace; Q9X100; -.
DR Proteomes; UP000008183; 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..482
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148857"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:3AL0"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 111..125
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3AL0"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:3AL0"
FT TURN 359..363
FT /evidence="ECO:0007829|PDB:3AL0"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:3AL0"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 468..478
FT /evidence="ECO:0007829|PDB:3AL0"
SQ SEQUENCE 482 AA; 55436 MW; 34988170E32F312F CRC64;
MRYRPVIGLE IHVQLSTKTK AFCSCPADVF ELPPNTAICP VCTGQPGALP VPNEEMIRFA
VKTALALNCK IHKYSRFDRK NYFYPDLPKG YQISQYFYPI ATEGFLEIDG DEGRKKVRIR
RLHLEEDAGK LVHEGDSITR ASYSLVDMNR CGVPLIEIVT EPDISSPREA RVFMEKLRSI
VRYLGVSTGD MEKGALRCDA NISVVDTETG RQSNRVEVKN MNSFRFVERA LEYEFERIVK
AMERGEDVER ETRGWDMATK ITVSMRGKEE ESDYRYFPEP DIPPVVLSDE YLEEVKKELP
ELPDEKAERF MREYGLPEYD AKVLTSSKEL AEFFEECVKV VNRPKDLSNW IMTEVLRELN
ERNIEITESK LTPQHFADLF KLMDEGKISI KIAKEIFPEV FETGKMPSQI VEEKGLTQIN
DEKLIEELVK KAMEQNPKAV QDYKSGKKKA AGFFVGYVMR ETKGKANPEL TNRIIQKLLE
GE
