GATD_METTH
ID GATD_METTH Reviewed; 435 AA.
AC O26802;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D;
DE Short=Glu-ADT subunit D;
DE EC=6.3.5.-;
GN Name=gatD; OrderedLocusNames=MTH_706;
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 asparaginase 1 family. GatD subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000666; AAB85211.1; -; Genomic_DNA.
DR PIR; C69194; C69194.
DR RefSeq; WP_010876345.1; NC_000916.1.
DR PDB; 2D6F; X-ray; 3.15 A; A/B=1-435.
DR PDBsum; 2D6F; -.
DR AlphaFoldDB; O26802; -.
DR SMR; O26802; -.
DR STRING; 187420.MTH_706; -.
DR EnsemblBacteria; AAB85211; AAB85211; MTH_706.
DR GeneID; 1470667; -.
DR KEGG; mth:MTH_706; -.
DR PATRIC; fig|187420.15.peg.689; -.
DR HOGENOM; CLU_019134_2_1_2; -.
DR OMA; RKNHTSR; -.
DR BioCyc; MetaCyc:MON-14998; -.
DR EvolutionaryTrace; O26802; -.
DR Proteomes; UP000005223; 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; Reference proteome.
FT CHAIN 1..435
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140056"
FT DOMAIN 91..419
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 230..242
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:2D6F"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:2D6F"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2D6F"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:2D6F"
SQ SEQUENCE 435 AA; 47997 MW; 34D8E4205486126F CRC64;
MSYQGRARKF LESASIDVGD MVLVEKPDVT YEGMVLDRAD DADDRHIVLK LENGYNIGVE
ISDARIELLE KGSEPRIELP PVEAAEDPEL PDVSIISTGG TVASIIDYRT GAVHPAFTAD
DLLRANPELL DIANIRGRAV FNILSENMKP EYWVETARAV YGEIKDGADG VVVAHGTDTM
HYTSAALSFM LRTPVPVVFT GAQRSSDRPS SDASLNIQCS VRAATSEIAE VTVCMHATMD
DLSCHLHRGV KVRKMHTSRR DTFRSMNALP LAEVTPDGIK ILEENYRKRG SDELELSDRV
EERVAFIKSY PGISPDIIKW HLDEGYRGIV IEGTGLGHCP DTLIPVIGEA HDMGVPVAMT
SQCLNGRVNM NVYSTGRRLL QAGVIPCDDM LPEVAYVKMC WVLGQTDDPE MAREMMRENI
AGEINERTSI AYFRG
