GATA_CHLPN
ID GATA_CHLPN Reviewed; 492 AA.
AC Q9Z9G7; Q9JQ43;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.7;
GN Name=gatA; OrderedLocusNames=CPn_0003, CP_0772, CpB0004;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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 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) (By similarity). {ECO:0000250}.
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; EC=6.3.5.7;
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001363; AAD18161.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38572.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98213.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP97937.1; -; Genomic_DNA.
DR PIR; C86491; C86491.
DR PIR; H72130; H72130.
DR RefSeq; NP_224216.1; NC_000922.1.
DR RefSeq; WP_010882658.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z9G7; -.
DR SMR; Q9Z9G7; -.
DR STRING; 115711.CP_0772; -.
DR EnsemblBacteria; AAD18161; AAD18161; CPn_0003.
DR EnsemblBacteria; AAF38572; AAF38572; CP_0772.
DR KEGG; cpa:CP_0772; -.
DR KEGG; cpj:gatA; -.
DR KEGG; cpn:CPn_0003; -.
DR KEGG; cpt:CpB0004; -.
DR PATRIC; fig|115713.3.peg.4; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_0; -.
DR OrthoDB; 1239251at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; 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; 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;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..492
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105151"
FT ACT_SITE 77
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 176
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 397
FT /note="M -> V (in Ref. 4; AAP97937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 53596 MW; C11A31EBF091227E CRC64;
MYRYSALELA KAVTLGELTA TGVTQHFFHR IEEAEGQVGA FISLCKEQAL EQAELIDKKR
SRGEPLGKLA GVPVGIKDNI HVTGLKTTCA SRVLENYQPP FDATVVERIK KEDGIILGKL
NMDEFAMGST TLYSAFHPTH NPWDLSRVPG GSSGGSAAAV SARFCPVALG SDTGGSIRQP
AAFCGVVGFK PSYGAVSRYG LVAFASSLDQ IGPLANTVED VALMMDVFSG RDPKDATSRE
FFRDSFMSKL STEVPKVIGV PRTFLEGLRD DIRENFFSSL AIFEGEGTHL VDVELDILSH
AVSIYYILAS AEAATNLARF DGVRYGYRSP QAHTISQLYD LSRGEGFGKE VMRRILLGNY
VLSAERQNVY YKKATAVRAK IVKAFRTAFE KCEILAMPVC SSPAFEIGEI LDPVTLYLQD
IYTVAMNLAY LPAIAVPSGF SKEGLPLGLQ IIGQQGQDQQ VCQVGYSFQE HAQIKQLFSK
RYAKSVVLGG QS
