ID A0A099NXN2_PICKU Unreviewed; 527 AA.
AC A0A099NXN2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 Name=HER2 {ECO:0000256|HAMAP-Rule:MF_03150};
GN ORFNames=C5L36_0D04480 {ECO:0000313|EMBL:AWU77721.1}, JL09_g4083
GN {ECO:0000313|EMBL:KGK36754.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK36754.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
RN [2] {ECO:0000313|EMBL:KGK36754.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|EMBL:KGK36754.1};
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for Succinic Acid Production.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWU77721.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU77721.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) 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 GatFAB amidotransferase (AdT)
CC complex, composed of A, B and F 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}.
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DR EMBL; CP028776; AWU77721.1; -; Genomic_DNA.
DR EMBL; JQFK01000054; KGK36754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099NXN2; -.
DR STRING; 4909.A0A099NXN2; -.
DR VEuPathDB; FungiDB:C5L36_0D04480; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_7_6_1; -.
DR OrthoDB; 4001253at2759; -.
DR Proteomes; UP000029867; Unassembled WGS sequence.
DR Proteomes; UP000249293; Chromosome 4.
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; 2.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 2.
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:UP000249293}.
FT DOMAIN 34..112
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 172..514
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 204
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ SEQUENCE 527 AA; 58076 MW; A37856AED78FF0A6 CRC64;
MKTNLNHIKQ VNKRYNIFTS LRKAPVVHED FSYAPLVHTT YAIKDNFTTR EEPTTCSSKI
LSSYISPFDS TVVTLLKQNG THCIGKTNMD EFAMGNSTTS GVFGPTLNPL YEQNEDLVEK
YEEFEFGTKD SISETDGETI SREILFGKGE DISEHSYLVP KLSSDFSAKI SDKQRIVGGS
SGGSAAAVAS DLVDFSIGSD TGGSVRLPAS YTGIYGFKPT YGRISRWGLV AYSQSLDTVG
IMSKSVDNIW KVFTCLDLPD AKDPSCLTES VREDMAIERL NSKKNVGKKF KVGIPVELQL
EGMSGAVKGA WKDLLIKLQK SKLIEVYSVS VPSIKYALPT YYTLVTSEAS SNLSRYDGIR
YGYRAGESVC DLAKEPEFVT TRSRGFGEEV KSRILLGNYT LSSYGYNSHF MKATGVRGML
IDEFNKVFRD RNMLVDKYFP NSAGVDMMIV PTAVHEPAPI NEVCGSTDAV KSYMDDVCTI
PMSLAGLPSM SIPFGGKSMG FQLVGQHGQD YKVLEFTRLV EEVLDAK
//
