ID A0A1Y4DLU5_9ACTN Unreviewed; 502 AA.
AC A0A1Y4DLU5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
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 ORFNames=B5F73_02445 {ECO:0000313|EMBL:OUO60183.1};
OS Olsenella sp. An270.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1965615 {ECO:0000313|EMBL:OUO60183.1, ECO:0000313|Proteomes:UP000195449};
RN [1] {ECO:0000313|Proteomes:UP000195449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An270 {ECO:0000313|Proteomes:UP000195449};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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|HAMAP-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|ARBA:ARBA00001243, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00008069, 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:OUO60183.1}.
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DR EMBL; NFJF01000002; OUO60183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4DLU5; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000195449; 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: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; IPR020556; Amidase_CS.
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.
DR PROSITE; PS00571; AMIDASES; 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}.
FT DOMAIN 25..470
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 139..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 179
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 502 AA; 51858 MW; 56D754EEACB3DAE7 CRC64;
MANFDQLSAR EIAAGVANGD FTATEVARAA LDAVEARDGE VKAFLQVSAD LALAAAEATD
KARAAGEKLG PLAGVPVAFK DNMHLVGTRT TCASRMLENY ESTFTATCVQ RMLDAGATPV
GKTNMDEFAF GSSTESSAFH PTANPWDTGR VPGGSSGGSA AAVAAGEVTV SLGSDTGGSI
RQPASLCGVV GMKPTYGAVS RYGVVAFGSS LDQVGPFGRS VEDVALAMNA LTAGGRDPWD
STSQPVDVDF LAHLNDPIEG RRVGVVPALM EAAGLTEEVR DAVNAAGRAL QDQGAELVEV
DLPNIASAIA AYYVIAPCEA FSNLARFDGV RYGYQEQGCA TLAEQTSLSR AHGFGEEAKR
RQMLGAYLLS SGTYDTYYYP AQQVRTLITA DYARAYEQCD VILMPAAPRT AFKFGEMSDP
TQMYASDLFT ISNNIVGNGG VSVPLGLGAT SGLPVSAQLQ GPAFADATLL TFARAIERSN
SADGGSGAPV APSFAGKGGE LA
//
