GATE_METTH
ID GATE_METTH Reviewed; 619 AA.
AC O26803;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E;
DE Short=Glu-ADT subunit E;
DE EC=6.3.5.-;
GN Name=gatE; OrderedLocusNames=MTH_707;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10993083; DOI=10.1038/35024120;
RA Tumbula D.L., Becker H.D., Chang W.-Z., Soell D.;
RT "Domain-specific recruitment of amide amino acids for protein synthesis.";
RL Nature 407:106-110(2000).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC tRNA(Gln). The GatDE system is specific for glutamate and does not act
CC on aspartate.
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 -!- SUBUNIT: Heterodimer of GatD and GatE.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000666; AAB85212.1; -; Genomic_DNA.
DR PIR; D69194; D69194.
DR RefSeq; WP_010876346.1; NC_000916.1.
DR PDB; 2D6F; X-ray; 3.15 A; C/D=1-619.
DR PDBsum; 2D6F; -.
DR AlphaFoldDB; O26803; -.
DR SMR; O26803; -.
DR STRING; 187420.MTH_707; -.
DR PRIDE; O26803; -.
DR EnsemblBacteria; AAB85212; AAB85212; MTH_707.
DR GeneID; 1470668; -.
DR KEGG; mth:MTH_707; -.
DR PATRIC; fig|187420.15.peg.690; -.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR BioCyc; MetaCyc:MON-14999; -.
DR EvolutionaryTrace; O26803; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 1.10.150.380; -; 1.
DR Gene3D; 3.30.1360.30; -; 1.
DR HAMAP; MF_00588; GatE; 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; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR042114; GatB_C_1.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR004414; GatE.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11659; PTHR11659; 1.
DR PANTHER; PTHR11659:SF2; PTHR11659:SF2; 1.
DR Pfam; PF02938; GAD; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF55261; SSF55261; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR SUPFAM; SSF89095; SSF89095; 1.
DR TIGRFAMs; TIGR00134; gatE_arch; 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..619
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_0000140075"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 124..144
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 245..268
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 374..393
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 497..501
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:2D6F"
SQ SEQUENCE 619 AA; 69533 MW; D362944674300A32 CRC64;
MDWEKVGLKM GLEIHQQLDT ESKLFCPCRT ELTDSEPDHD IVRNLRPTQS ELGKFDRAAF
EEAMRKLHFH YENYHEETCL VEADEEPPHP LNPEALEIAV TIALLLNMRV VDEFHTMRKQ
VIDGSNTGGF QRTGLVATDG HLETPQGTVK IENLCLEEDA ARRIRETGDG VVFRLDRLGI
PLVEITTDPS MSDPQQLREV AYQIGQILRS TRVKRGLGTI RQDLNISIRD GARVEVKGVQ
DLDLIPEIVE REVKRQLSLV EIRDTLQERG AVVEDKIFDV SEVFADTESR IISSAESVLA
VKLRGFDGLI GVEIQPGRRL GTEMADYAKK RGVSGIFHTD ELPAYGITEE EVRGLRDAVG
ASQGDAVVMV AHERVTAENA LREVIRRAEM AIQGVPEETR KALPDGNTQY LRPLPTSSRM
YLETDIPLFR IEDDLLEGIR RNLPELPSEK KERIMRDYGL SEDLASQLVK RNLVDEFEAL
TEFRVDTTVI ASLLAYTLRE LRREGHDVDG LGLDELRDAI KLLEVGKISK DALRDIVACM
ADEGLAAEDA ARKLNLLLLA EDEIESIIQE IVEGNLDMIS ERGMGAMGPL MGQAMGRLRG
RADGKVVNRI LREKIQERL
