GATE_PYRAB
ID GATE_PYRAB Reviewed; 633 AA.
AC Q9V0U0; G8ZJG3;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE Short=Glu-ADT subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00588};
GN Name=gatE {ECO:0000255|HAMAP-Rule:MF_00588}; OrderedLocusNames=PYRAB06990;
GN ORFNames=PAB1902;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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. {ECO:0000255|HAMAP-Rule:MF_00588}.
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:0000255|HAMAP-Rule:MF_00588};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP-
CC Rule:MF_00588}.
CC -!- INTERACTION:
CC Q9V0U0; Q9V0T9: gatD; NbExp=3; IntAct=EBI-9023893, EBI-9023883;
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00588}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE70090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248285; CAB49613.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70090.1; ALT_INIT; Genomic_DNA.
DR PIR; D75112; D75112.
DR PDB; 1ZQ1; X-ray; 3.00 A; C/D=1-633.
DR PDBsum; 1ZQ1; -.
DR AlphaFoldDB; Q9V0U0; -.
DR SMR; Q9V0U0; -.
DR DIP; DIP-48454N; -.
DR IntAct; Q9V0U0; 1.
DR STRING; 272844.PAB1902; -.
DR EnsemblBacteria; CAB49613; CAB49613; PAB1902.
DR KEGG; pab:PAB1902; -.
DR PATRIC; fig|272844.11.peg.734; -.
DR eggNOG; arCOG01719; Archaea.
DR HOGENOM; CLU_030702_0_0_2; -.
DR OMA; SGFQRTM; -.
DR PhylomeDB; Q9V0U0; -.
DR EvolutionaryTrace; Q9V0U0; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 DisProt; DP01919; -.
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.
FT CHAIN 1..633
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT /id="PRO_0000140076"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 10..14
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 17..28
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 251..275
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 290..295
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 386..405
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 459..467
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:1ZQ1"
SQ SEQUENCE 633 AA; 71876 MW; 3F1BE701DBA6214A CRC64;
MMVMTDKFNY EELGLKVGLE IHRQLDTKKL FSPVPSELSD KVEFTFQRRL RPTMSELGEI
DPAALEEFKK GRVYVYEGNY ELTDLVYMDE EPPRGPDREA LEVALQIAYL LNAKPVDEVY
YMRKIVIDGS NVSGFQRTAI IATDGKVETP WGAVGIPTIC LEEDAARIIE RKDKEVIYRL
DRLGIPLIEI STTPDIHHPE QAKVVAKFIG DALRATKKVK RGLGTIRQDL NVSIKGGARI
EIKGVQELDM IPIIIEREVE RQLNLLKIRD ELRKRGVKPK DIKEEFYDVT DIFENTKSKI
IARVIKKGGK VLAIKLPKFR GLIGREIQPG RRLGTEFADR AKKYVPGIFH IDELPNYGIS
QEEVNKVIER LNLSEEDAFV LVAAEEEKAK NALREVIKRA REAIEGVPEE TRRALPDGNT
EYMRPLPGKA RMYPETDIPP LRIPDDLKKK IKENLPELPQ AKVERYVKEY KLDRSLAQTL
VDDERDELFE ELVSMGVKPS LAASILVVVL KGLRKEVPIE NVTDEHIREA FQLYLEGKIA
KEAFEEIFKE LARNPSKSAR EVAEEKGLTL LSEEEVTRII EEVIQQNIEV VKAKGMGAMG
LIMGRVMAKV RGKADGKLVS QIVRRKLQEI SGG
