ID G4D4L2_9FIRM Unreviewed; 478 AA.
AC G4D4L2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ECO:0000313|EMBL:EGY79559.1};
GN ORFNames=HMPREF9129_1342 {ECO:0000313|EMBL:EGY79559.1};
OS Peptoniphilus indolicus ATCC 29427.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY79559.1, ECO:0000313|Proteomes:UP000003422};
RN [1] {ECO:0000313|EMBL:EGY79559.1, ECO:0000313|Proteomes:UP000003422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY79559.1,
RC ECO:0000313|Proteomes:UP000003422};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2011) 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). {ECO:0000256|ARBA:ARBA00025295, ECO:0000256|HAMAP-
CC Rule:MF_00120}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_00120};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGY79559.1}.
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DR EMBL; AGBB01000127; EGY79559.1; -; Genomic_DNA.
DR RefSeq; WP_004821899.1; NZ_JH165063.1.
DR AlphaFoldDB; G4D4L2; -.
DR STRING; 997350.HMPREF9129_1342; -.
DR PATRIC; fig|997350.3.peg.1289; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000003422; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR NCBIfam; TIGR00132; gatA; 1.
DR PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00120};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00120};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00120};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00120}; Reference proteome {ECO:0000313|Proteomes:UP000003422};
KW Transferase {ECO:0000313|EMBL:EGY79559.1}.
FT DOMAIN 24..466
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 478 AA; 53268 MW; C58507E92E85E4F7 CRC64;
MDLTKLKGHE LIKGYENRDF SCREVTEAYL KNIKEKDEEI NAYITITEEL ALENASKVDQ
KYENREHLGI LAGIPTAIKD NVAVKDVRMT CASKMLENFI SPYNSNVSEK ILECDGVILG
KVNMDEFAMG ATTRTSYFGN TKNPLDTNLV PGGSSGGSAA AVASHEAAIA IGTDTGGSTR
QPAGFCGIVG FKPTYGTVSR YGVSSMANTF DTVGTMGRDV EDAHLLMKSI AGRDLRDATS
VKNDSIFDEI NYENSNYLKE MKIAVPKEYL AMDLNSTVMN NYRETIEILK REGAKVEEVS
LKSLEYTIQT YHILVNGEIA SNLARFDSLR YGHRTNSEYY SYEEMFKKSR AEGFGEEVKK
RIMVGTHILS LDLANEYYYK ALKVRTMIKN EYEDIFKNFD LILSPTAPVL PFELNSDMKP
VEIYQADLFT IPANMSGCPS ICVPFKNSDF PTGIMFTASR FKDSKCIKAG VGFERSVK
//
