(data stored in ACNUC7421 zone)

SWISSPROT: A1AZJ4_PARDP

ID   A1AZJ4_PARDP            Unreviewed;       493 AA.
AC   A1AZJ4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120};
GN   OrderedLocusNames=Pden_0576 {ECO:0000313|EMBL:ABL68688.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68688.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in
CC       organisms which lack glutaminyl-tRNA synthetase. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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         EC=6.3.5.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00120,
CC         ECO:0000256|SAAS:SAAS01115610};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00120, ECO:0000256|SAAS:SAAS00598568}.
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DR   EMBL; CP000489; ABL68688.1; -; Genomic_DNA.
DR   RefSeq; WP_011746921.1; NC_008686.1.
DR   STRING; 318586.Pden_0576; -.
DR   PRIDE; A1AZJ4; -.
DR   EnsemblBacteria; ABL68688; ABL68688; Pden_0576.
DR   KEGG; pde:Pden_0576; -.
DR   eggNOG; ENOG4105C3P; Bacteria.
DR   eggNOG; COG0154; LUCA.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   BioCyc; PDEN318586:G1GW1-584-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0004040; F:amidase 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZJ4.
DR   SWISS-2DPAGE; A1AZJ4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013898};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013917, ECO:0000313|EMBL:ABL68688.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013943};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00120,
KW   ECO:0000256|SAAS:SAAS00013924};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000313|EMBL:ABL68688.1}.
FT   DOMAIN       25    473       Amidase. {ECO:0000259|Pfam:PF01425}.
FT   ACT_SITE     78     78       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    156    156       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    180    180       Acyl-ester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00120}.
SQ   SEQUENCE   493 AA;  52403 MW;  C1D0828AAEA86EA1 CRC64;
     MSDLNKLTIA AARDGLRKGD FTSAELTETC LVAIEAAGAL NAWCHKTPEK AREMAAAADK
     RIAAGDAPAM CGIPLGIKDL FCTRDVPSQA ASRILDGFLP QYESTVTQNL WDAGAVMLGK
     LSMDEFAMGS SNESACYGPV VNPWKVDDRQ LTPGGSSGGS AAAVAADLCL AATGTDTGGS
     IRQPAAFTGT VGLKPTYGRV SRWGVIAFAS SLDQAGPMTK TVRDAAIMLG AMASVDAKDS
     TSAERAVPDY EAALTGDIRG RRIGIPREYR MEGMSDEIDA LWHKAAEMLR DAGAEVVDIT
     LPHTKYALPA YYVIAPAEAS SNLARYDGVR YGRRARLGAG DGVVEMYEKT RAEGFGPEVQ
     RRVMIGTYVL SAGFYDAYYN RARKVRALIK RDFDQVFADG IDAILTPATP SAAFGLGEMS
     GKDPVEMYLN DVFTVTVNLA GLPGISVPVG LDRQGLPLGM QLIGRPWDEG GLLNLAQSLE
     SAAGFTAKPS RWW
//

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