ID A0A1E3HFW0_9TREE Unreviewed; 464 AA.
AC A0A1E3HFW0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000256|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_03150};
GN ORFNames=L202_06430 {ECO:0000313|EMBL:ODN75238.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN75238.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN75238.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN75238.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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 the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000256|HAMAP-Rule:MF_03150}.
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_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000256|HAMAP-
CC Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000256|ARBA:ARBA00008069, ECO:0000256|HAMAP-Rule:MF_03150}.
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:ODN75238.1}.
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DR EMBL; AWGJ01000010; ODN75238.1; -; Genomic_DNA.
DR RefSeq; XP_018990888.1; XM_019140913.1.
DR AlphaFoldDB; A0A1E3HFW0; -.
DR STRING; 1295533.A0A1E3HFW0; -.
DR GeneID; 30157739; -.
DR OrthoDB; 4001253at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
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:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial 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 PANTHER; PTHR11895:SF7; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL; 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_03150};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03150};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03150};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03150}; Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT DOMAIN 22..449
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 36
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 142
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ SEQUENCE 464 AA; 49343 MW; C9093A0D2F03D873 CRC64;
MRPSLRSLTH GPYAWRNPSP ATGPSGLLAG KHIAIKENIS YSQAPTSCSS QLLQGYIPPY
NATCVDDLIN AGAHIMGTTK MDEFGMGSQT TNIPPSYSPV HNPCAPSPDE PPRSAGGSSG
GSATAVAEGS CWAALGTDTG GSVRLPASYC GVVGLKPSYG LVSRRGVVAY GDSLDCVGVL
AKDIDIVTKV FNIISHPDDR DMTCAPSSVR STSLPLDLSS TSLKYLRIGI PAQTLLPHPY
TSIPPSLLTH LQSLGASLRP VSLPSVRKAL PAYYVLASAE ASSNLGRYGG GWYGSEGEKE
EGRIEGESGQ ERRVRVRSDG FGKEVKKRIL AGTHALSADE FNNTYLKALY LRRLLRQEYQ
RTFRIAHPLA APYTPNSDGV DLILHPTAIR TAPLLNQDAK TGESVYLQDL ITVPPSLAGL
PAMSVPAGKA EDGWPVGMSV TGQWGMEGLV FGLGRAIERW SRDL
//
