GATD_PYRAB
ID GATD_PYRAB Reviewed; 438 AA.
AC Q9V0T9; G8ZJG4;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D {ECO:0000255|HAMAP-Rule:MF_00586};
DE Short=Glu-ADT subunit D {ECO:0000255|HAMAP-Rule:MF_00586};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00586};
GN Name=gatD {ECO:0000255|HAMAP-Rule:MF_00586}; OrderedLocusNames=PYRAB07000;
GN ORFNames=PAB1901;
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_00586}.
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_00586};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP-
CC Rule:MF_00586}.
CC -!- INTERACTION:
CC Q9V0T9; Q9V0U0: gatE; NbExp=3; IntAct=EBI-9023883, EBI-9023893;
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00586}.
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DR EMBL; AJ248285; CAB49614.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70091.1; -; Genomic_DNA.
DR PIR; E75112; E75112.
DR RefSeq; WP_010867819.1; NC_000868.1.
DR PDB; 1ZQ1; X-ray; 3.00 A; A/B=1-438.
DR PDBsum; 1ZQ1; -.
DR AlphaFoldDB; Q9V0T9; -.
DR SMR; Q9V0T9; -.
DR DIP; DIP-48453N; -.
DR IntAct; Q9V0T9; 1.
DR STRING; 272844.PAB1901; -.
DR EnsemblBacteria; CAB49614; CAB49614; PAB1901.
DR GeneID; 1495604; -.
DR KEGG; pab:PAB1901; -.
DR PATRIC; fig|272844.11.peg.735; -.
DR eggNOG; arCOG01924; Archaea.
DR HOGENOM; CLU_019134_2_1_2; -.
DR OMA; RKNHTSR; -.
DR OrthoDB; 61613at2157; -.
DR PhylomeDB; Q9V0T9; -.
DR EvolutionaryTrace; Q9V0T9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0004067; F:asparaginase 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:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd08962; GatD; 1.
DR Gene3D; 2.30.30.520; -; 1.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR HAMAP; MF_00586; GatD; 1.
DR InterPro; IPR006033; AsnA_fam.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR011878; GatD.
DR InterPro; IPR040918; GatD_N.
DR InterPro; IPR037222; GatD_N_sf.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR Pfam; PF18195; GatD_N; 1.
DR PIRSF; PIRSF500175; Glu_ADT_D; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF141300; SSF141300; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00519; asnASE_I; 1.
DR TIGRFAMs; TIGR02153; gatD_arch; 1.
DR PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..438
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140058"
FT DOMAIN 92..422
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 102
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 178
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 17..30
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 359..369
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:1ZQ1"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:1ZQ1"
SQ SEQUENCE 438 AA; 48860 MW; 39C616E89496D61C CRC64;
MRVDEFLKER NINVGDFVRI TKEEDGEEVT YEGYIMPPYE LSAGDTLVLK LENGYNIGIA
LEKIRRIEVL ERAKVKPEVH FEALIEGKPG LPEVTIIGTG GTIASRIDYE TGAVYPAFTA
EELAKAVPEI FEVANVKPKL LFNIFSEDMK PKHWVKIAHE VAKALNSGDY GVVVAHGTDT
MGYTAAALSF MLRNLGKPVV LVGAQRSSDR PSSDAAMNLI CSVRMATSEV AEVMVVMHGE
TGDTYCLAHR GTKVRKMHTS RRDAFRSIND VPIAKIWPNG EIEFLRKDYR KRSDEEVEVD
DKIEEKVALV KVYPGISSEI IDFLVDKGYK GIVIEGTGLG HTPNDIIPSI ERAVEEGVAV
CMTSQCIYGR VNLNVYSTGR KLLKAGVIPC EDMLPETAYV KLMWVLGHTQ NLEEVRKMML
TNYAGEITPY TRFDTYLR
